ID   POLG_EMCVB              Reviewed;        2292 AA.
AC   P17593;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   24-JAN-2024, entry version 162.
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=Rho;
DE     AltName: Full=Virion protein 4;
DE   Contains:
DE     RecName: Full=Capsid protein VP2;
DE     AltName: Full=Beta;
DE     AltName: Full=P1B;
DE     AltName: Full=Virion protein 2;
DE   Contains:
DE     RecName: Full=Capsid protein VP3;
DE     AltName: Full=Gamma;
DE     AltName: Full=P1C;
DE     AltName: Full=Virion protein 3;
DE   Contains:
DE     RecName: Full=Capsid protein VP1;
DE     AltName: Full=Alpha;
DE     AltName: Full=P1D;
DE     AltName: Full=Virion protein 1;
DE   Contains:
DE     RecName: Full=Protein 2A;
DE              Short=P2A;
DE     AltName: Full=G;
DE   Contains:
DE     RecName: Full=Protein 2B;
DE              Short=I;
DE              Short=P2B;
DE   Contains:
DE     RecName: Full=Protein 2C;
DE              Short=C;
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=H;
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     AltName: Full=p22;
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=E;
DE     AltName: Full=Protein 3D;
DE              Short=3D;
DE   Flags: Precursor;
OS   Encephalomyocarditis virus (strain emc-b nondiabetogenic).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Caphthovirinae; Cardiovirus; Cardiovirus A.
OX   NCBI_TaxID=12105;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
OH   NCBI_TaxID=42415; Sigmodon hispidus (Hispid cotton rat).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2541543; DOI=10.1016/0042-6822(89)90379-6;
RA   Bae Y.S., Eun H.M., Yoon J.W.;
RT   "Genomic differences between the diabetogenic and nondiabetogenic variants
RT   of encephalomyocarditis virus.";
RL   Virology 170:282-287(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2537245; DOI=10.2337/diab.38.3.316;
RA   Bae Y.S., Eun H.M., Yoon J.W.;
RT   "Molecular identification of diabetogenic viral gene.";
RL   Diabetes 38:316-320(1989).
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).
CC       {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:P12296}.
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:P12296}.
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:P12296}.
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:P03300, ECO:0000250|UniProtKB:P12296}.
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 (By similarity). It displays
CC       RNA-binding, nucleotide binding and NTPase activities (By similarity).
CC       Interacts with IFIH1/MDA5 to inhibit the induction of the IFN-beta
CC       signal pathway (By similarity). {ECO:0000250|UniProtKB:P03304,
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). Cleaves host TANK and disrupts the TANK-
CC       TBK1-IKKepsilon-IRF3 complex, thereby inhibiting the induction of the
CC       IFN-beta signal pathway (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: [Protease 3C]: Interacts with host TRIM22; this interaction
CC       leads to the ubiquitination of protease 3C and may restrict the virus
CC       replication (By similarity). {ECO:0000250|UniProtKB:P03304,
CC       ECO:0000250|UniProtKB:Q66765}.
CC   -!- SUBUNIT: [Protein 2A]: Interacts with host EIF4E (By similarity).
CC       Interacts with the leader protein (By similarity).
CC       {ECO:0000250|UniProtKB:P03304, 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       {ECO:0000250|UniProtKB:P03304, ECO:0000250|UniProtKB:Q66765}.
CC   -!- SUBUNIT: [Protein 2C]: Interacts with host IFIH1/MDA5; this interaction
CC       inhibits the induction of the IFN-beta signal pathway (By similarity).
CC       {ECO:0000250|UniProtKB:P03304, ECO:0000250|UniProtKB:Q66765}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion
CC       {ECO:0000250|UniProtKB:P12296}. Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
CC       {ECO:0000250|UniProtKB:P12296}. Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC       {ECO:0000250|UniProtKB:P12296}. 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   -!- 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   -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M22457; AAA43033.1; ALT_SEQ; Genomic_RNA.
DR   PIR; B31473; GNNYEB.
DR   SMR; P17593; -.
DR   MEROPS; C03.009; -.
DR   Proteomes; UP000008661; 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: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: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; IPR021573; Leader_pept_picornaV.
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   InterPro; IPR037243; Viral_lead_polypep_zc_finger.
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   Pfam; PF11475; VP_N-CPKC; 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   SUPFAM; SSF144251; Viral leader polypeptide zinc finger; 1.
DR   PROSITE; PS51874; PCV_3C_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51218; SF3_HELICASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Capsid protein; Covalent protein-RNA linkage;
KW   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 mRNA nuclear export by virus;
KW   Inhibition of host RIG-I 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..2292
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000446094"
FT   CHAIN           1..67
FT                   /note="Leader protein"
FT                   /id="PRO_0000039792"
FT   CHAIN           68..393
FT                   /note="Capsid protein VP0"
FT                   /id="PRO_0000310968"
FT   CHAIN           68..137
FT                   /note="Capsid protein VP4"
FT                   /id="PRO_0000039793"
FT   CHAIN           138..393
FT                   /note="Capsid protein VP2"
FT                   /id="PRO_0000039794"
FT   CHAIN           394..624
FT                   /note="Capsid protein VP3"
FT                   /id="PRO_0000039795"
FT   CHAIN           625..901
FT                   /note="Capsid protein VP1"
FT                   /id="PRO_0000039796"
FT   CHAIN           902..1044
FT                   /note="Protein 2A"
FT                   /id="PRO_0000039797"
FT   CHAIN           1045..1194
FT                   /note="Protein 2B"
FT                   /id="PRO_0000039798"
FT   CHAIN           1195..1519
FT                   /note="Protein 2C"
FT                   /id="PRO_0000039799"
FT   CHAIN           1520..1607
FT                   /note="Protein 3A"
FT                   /id="PRO_0000039800"
FT   CHAIN           1608..1627
FT                   /note="VPg"
FT                   /id="PRO_0000039801"
FT   CHAIN           1628..1832
FT                   /note="Protease 3C"
FT                   /id="PRO_0000039802"
FT   CHAIN           1833..2292
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000039803"
FT   DOMAIN          1281..1447
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1630..1822
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          2061..2179
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   ZN_FING         10..22
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   REGION          37..61
FT                   /note="Acidic"
FT                   /evidence="ECO:0000305"
FT   REGION          1030..1036
FT                   /note="Host EIF4E binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q66765"
FT   MOTIF           995..1003
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q66765"
FT   ACT_SITE        1673
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1707
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1786
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        2067
FT                   /note="For RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   ACT_SITE        2165
FT                   /note="For RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   BINDING         22
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   BINDING         46
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   BINDING         47
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   BINDING         48
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   BINDING         49
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   BINDING         50
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   BINDING         69
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   BINDING         70
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   BINDING         93
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   BINDING         95
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   BINDING         97
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   BINDING         100
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   BINDING         1313..1320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   SITE            137..138
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            393..394
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            624..625
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            901..902
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1044..1045
FT                   /note="Cleavage; by ribosomal skip"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1194..1195
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1519..1520
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1607..1608
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1627..1628
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1832..1833
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   MOD_RES         41
FT                   /note="Phosphotyrosine; by host SYK"
FT                   /evidence="ECO:0000250|UniProtKB:Q66765"
FT   MOD_RES         47
FT                   /note="Phosphothreonine; by host CK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q66765"
FT   MOD_RES         1610
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   LIPID           68
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q66282"
SQ   SEQUENCE   2292 AA;  255497 MW;  8540D0EB1437E8D4 CRC64;
     MATTMEQEIC AHSLTLKGCP KCSALQYRNG FYLLKYDEEW YPEELLTDGE DDVFDPELDM
     EVVFELQGNS TSSDKNNSSS DGNEGVIINN FYSNQYQNSI DLSANATGSD PPRTYGQFSN
     LLSGAVNAFS NMIPLLADQN TEEMENLSDR VLQDTAGNTV TNTQSTVGRL VGYGAVHDGE
     HPASCADTAS EKILAVERYY TFKVNDWTST QKPFEYIRIP LPHVLSGEDG GVFGAALRRH
     YLVKTGWRVQ VQCNASQFHA GSLLVFMAPE YPTLDAFAMD NRWSKDNLPN GTKTQTNRKG
     PFAMDHQNFW QWTLYPHQFL NLRTNTTVDL EVPYVNIAPT SSWTQHASWT LVIAVVAPLT
     YSTGASTSLD ITASIQPVRP VFNGLRHETL SRQSPIPVTI REHAGTWYST LPDSTVPIYG
     KTPVAPANYM VGEYKDFLEI AQIPTFIGNK IPNAVPYIEA SNTAVKTQPL ATYQVTLSCS
     CLANTFLAAL SRNFAQYRGS LVYTFVFTGT AMMKGKFLIA YTPPGAGKPT SRDQAMQATY
     AIWDLGLNSS YSFTVPFISP THFRMVGTDQ VNITNVDGWV TVWQLTPLTY PPGCPTSAKI
     LTMVSAGKDF SLKMPISPAP WSPQGVENAE RGVTEDTDAT ADFVAQPVYL PENQTKVAFF
     YDRSSPIGAF TVKSGSLESG FTPFSNQTCP NSVILTPGPQ FDPAYDQLRP QRLTEIWGNG
     NEETSKVFPL KSKQDYSFCL FSPFVYYKCD LEVTLSPHTS GNHGLLVRWC PTGTPTKPTT
     QVLHEVSSLS EGRTPQVYSA GPGITNQISF VVPYNSPLSV LPAVWYNGHK RFDNTGSLGI
     APNSDFGTLF FAGTKPDIKF TVYLRYKNMR VFCPRPTVFF PWPSSGDKID MTPRAGVLML
     ESPNALDISR TYPTLHILIQ FNHGGLEIRL FRHGMFWAEA HADVILRSRT KQISFLNNGS
     FPSMDARAPW NPWKNTYHAV LRAEPYRVTM DVYHKRIRPF RLPLVQKEWN VREENVFGLY
     GIFNAHYAGY FADLLIHDIE TNPGPFMAKP KKQVFQTQGA AVSSMAQTLL PNDLASKVMG
     SAFTALLDAN EDAQKAMRII KTLSSLSDAW ENVKETLNNP EFWKQLLSRC VQLIAGMTIA
     VMHPDPLTLL CLGTLTAAEI TSQTSLCEEI VAKFKKIFTT PPPRFPTISL FQQQSPLKQV
     NDVFSLAKNL DWAVKTVEKV VDWFGTWVVQ EEKEQTLDQL LQRFPEHAKR ISDLRNGMSA
     YVECKESFDF FEKLYNQAVK EKRTGIAAVC EKFRQKHDHA TARCEPVVIV LRGDAGQGKS
     LSSQVIAQAV SKTIFGRQSV YSLPPDSDFF DGYENQFAAI MDDLGQNPDG SDFTTFCQMV
     STTNFLPNMA SLERNGTPFT SQIVVATTNL PEFRPVTIAH YPAVERRITF DYSVSAGPVC
     SKTEAGYKVL DVERAFRPTG DAPLPCFQNN CLFLEKAGLQ FRDNRTKEIL SLVDVIERAV
     ARIERKKKVL TTVQTLVAQA PVDEVSFHSV VQQLKARQEA TDEQLEELQE AFAKTQERSS
     VFSDWMKISA MLCAATLALS QVVKMAKTVK QMVRPDLVRV QLDEQEQGPY NEAVRAKPKT
     LQLLDIQGPN PVMDFEKYVA KFVTAPIDFV YPTGVSTQTC LLVKGRTLAV NRHMAESDWS
     SIVVRGVTHA RSTVRILAIA KAGKETDVSF IRLSSGPLFR DNTSKFVKAD DVLPATSAPV
     IGIMNTDIPM MFTGTFLKAG VSVPVETGQT FNHCIHYKAN TRKGWCGSAL LADLGGKKKI
     LGMHSAGSMG RTAASIVSQE MICAVVSAFE PQGALERLPD GPRIHVPRKT ALRPTVARRV
     FQPAYAPAVL SKFDPRTEAD VDEVAFSKHT SNQESLPPVF RMVAKEYANR VFTLLGRDNG
     RLTVKQALEG LEGMDPMDKN TSPGLPYTAL GMRRTDVVDW ESATLIPYAA DRLKKMNEGD
     FSDIVYQTFL KDELRPVEKV QAAKTRIVDV PPFEHCILGR QLLGRFASKF QTQPGLELGS
     AIGCDPDVHW TAFGVAMQGF ERVYDVDYSN FDSTHSVAMF RLLAEEFFTP ENGFDPLVKE
     YLESLAISTH AFEEKRYLIT GGLPSGCAAT SMLNTIMNNI IIRAGLYLTY KNFEFDDVKV
     LSYGDDLLVA TNYQLNFDKV RASLAKTGYK ITPANKTSTF PLDSTLEDVV FLKRKFKKEG
     PLYRPVMNRE ALEAMLSYYR PGTLSEKLTS ITMLAVHSGK PEYDRLFAPF REVGVVVPSF
     ESVEYRWRSL FW
//