POLG_EMCVR
ID POLG_EMCVR Reviewed; 2292 AA.
AC Q66765;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
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 Rueckert) (EMCV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Cardiovirus.
OX NCBI_TaxID=650129;
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=1310768; DOI=10.1128/jvi.66.3.1602-1609.1992;
RA Duke G.M., Hoffman M.A., Palmenberg A.C.;
RT "Sequence and structural elements that contribute to efficient
RT encephalomyocarditis virus RNA translation.";
RL J. Virol. 66:1602-1609(1992).
RN [2]
RP PHOSPHORYLATION (LEADER PROTEIN).
RX PubMed=11883190; DOI=10.1006/viro.2001.1193;
RA Dvorak C.M., Hall D.J., Hill M., Riddle M., Pranter A., Dillman J.,
RA Deibel M., Palmenberg A.C.;
RT "Leader protein of encephalomyocarditis virus binds zinc, is phosphorylated
RT during viral infection, and affects the efficiency of genome translation.";
RL Virology 290:261-271(2001).
RN [3]
RP FUNCTION (PROTEIN 2A), AND SUBCELLULAR LOCATION (PROTEIN 2A).
RX PubMed=12921995; DOI=10.1016/s0168-1702(03)00162-x;
RA Aminev A.G., Amineva S.P., Palmenberg A.C.;
RT "Encephalomyocarditis viral protein 2A localizes to nucleoli and inhibits
RT cap-dependent mRNA translation.";
RL Virus Res. 95:45-57(2003).
RN [4]
RP FUNCTION (LEADER PROTEIN), INTERACTION WITH HOST RAN (LEADER PROTEIN), AND
RP MUTAGENESIS OF CYS-19.
RX PubMed=16888036; DOI=10.1073/pnas.0605375103;
RA Porter F.W., Bochkov Y.A., Albee A.J., Wiese C., Palmenberg A.C.;
RT "A picornavirus protein interacts with Ran-GTPase and disrupts
RT nucleocytoplasmic transport.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12417-12422(2006).
RN [5]
RP FUNCTION (LEADER PROTEIN), AND MUTAGENESIS OF CYS-19; TYR-41 AND THR-47.
RX PubMed=19073724; DOI=10.1128/jvi.01752-08;
RA Porter F.W., Palmenberg A.C.;
RT "Leader-induced phosphorylation of nucleoporins correlates with nuclear
RT trafficking inhibition by cardioviruses.";
RL J. Virol. 83:1941-1951(2009).
RN [6]
RP FUNCTION (LEADER PROTEIN).
RX PubMed=20881039; DOI=10.1128/jvi.01484-09;
RA Porter F.W., Brown B., Palmenberg A.C.;
RT "Nucleoporin phosphorylation triggered by the encephalomyocarditis virus
RT leader protein is mediated by mitogen-activated protein kinases.";
RL J. Virol. 84:12538-12548(2010).
RN [7]
RP FUNCTION (PROTEIN 2A), SUBCELLULAR LOCATION (PROTEIN 2A), INTERACTION WITH
RP HUMAN EIF4E (PROTEIN 2A), AND MUTAGENESIS OF 993-TYR-TYR-994; ARG-996;
RP ARG-998; GLN-1006 AND LEU-1035.
RX PubMed=21145089; DOI=10.1016/j.virol.2010.11.002;
RA Groppo R., Brown B.A., Palmenberg A.C.;
RT "Mutational analysis of the EMCV 2A protein identifies a nuclear
RT localization signal and an eIF4E binding site.";
RL Virology 410:257-267(2011).
RN [8]
RP INTERACTION WITH THE LEADER PROTEIN (PROTEIN 2A), INTERACTION WITH PROTEIN
RP 2A (LEADER PROTEIN), FUNCTION (PROTEIN 2A), AND MUTAGENESIS OF LYS-35;
RP ASP-37 AND TRP-40.
RX PubMed=25210192; DOI=10.1128/jvi.02148-14;
RA Petty R.V., Basta H.A., Bacot-Davis V.R., Brown B.A., Palmenberg A.C.;
RT "Binding interactions between the encephalomyocarditis virus leader and
RT protein 2A.";
RL J. Virol. 88:13503-13509(2014).
RN [9]
RP PHOSPHORYLATION AT TYR-41 AND THR-47, AND MUTAGENESIS OF TYR-41 AND THR-47.
RX PubMed=24335301; DOI=10.1128/jvi.03150-13;
RA Basta H.A., Bacot-Davis V.R., Ciomperlik J.J., Palmenberg A.C.;
RT "Encephalomyocarditis virus leader is phosphorylated by CK2 and syk as a
RT requirement for subsequent phosphorylation of cellular nucleoporins.";
RL J. Virol. 88:2219-2226(2014).
RN [10]
RP FUNCTION (LEADER PROTEIN).
RX PubMed=26115166; DOI=10.1016/j.virol.2015.06.004;
RA Ciomperlik J.J., Basta H.A., Palmenberg A.C.;
RT "Three cardiovirus leader proteins equivalently inhibit four different
RT nucleocytoplasmic trafficking pathways.";
RL Virology 484:194-202(2015).
RN [11]
RP FUNCTION (LEADER PROTEIN), INTERACTION WITH XPO1/CRM1 (LEADER PROTEIN), AND
RP INTERACTION WITH CSE1L/CAS (LEADER PROTEIN).
RX PubMed=26492198; DOI=10.1016/j.virol.2015.10.001;
RA Ciomperlik J.J., Basta H.A., Palmenberg A.C.;
RT "Cardiovirus Leader proteins bind exportins: Implications for virus
RT replication and nucleocytoplasmic trafficking inhibition.";
RL Virology 487:19-26(2016).
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 (PubMed:19073724, PubMed:20881039, PubMed:16888036, PubMed:26492198,
CC PubMed:26115166). Proteins with NLS signals fail to import, cellular
CC mRNAs fail to export, and some proteins small enough for diffusion are
CC not retained anymore (efflux) (PubMed:19073724, PubMed:20881039,
CC PubMed:16888036). The resulting inhibition of cellular protein
CC synthesis serves to ensure maximal viral gene expression and to evade
CC host immune response (PubMed:19073724, PubMed:20881039,
CC PubMed:16888036). {ECO:0000269|PubMed:16888036,
CC ECO:0000269|PubMed:19073724, ECO:0000269|PubMed:20881039,
CC ECO:0000269|PubMed:26115166, ECO:0000269|PubMed:26492198}.
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 (PubMed:12921995,
CC PubMed:21145089). Nuclear localization is required for this function
CC (PubMed:12921995, PubMed:21145089). The resulting inhibition of
CC cellular protein synthesis serves to ensure maximal viral gene
CC expression and to evade host immune response (Probable). Inhibits the
CC phosphorylation of the leader protein (PubMed:25210192). Binds to the
CC RNA stem-loop essential for the ribosomal frameshift event and trans-
CC activates the production of protein 2B* (By similarity).
CC {ECO:0000250|UniProtKB:P12296, ECO:0000269|PubMed:12921995,
CC ECO:0000269|PubMed:21145089, ECO:0000269|PubMed:25210192, ECO:0000305}.
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 -!- SUBUNIT: [Protein 2A]: Interacts with host EIF4E (PubMed:21145089).
CC Interacts with the leader protein (PubMed:25210192).
CC {ECO:0000269|PubMed:21145089, ECO:0000269|PubMed:25210192}.
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 (PubMed:16888036). The complex
CC L-RAN can further bind to the host exportins XPO1/CRM1 and CSE1L/CAS
CC (PubMed:26492198). Interacts with the protein 2A (PubMed:25210192).
CC {ECO:0000269|PubMed:16888036, ECO:0000269|PubMed:25210192,
CC ECO:0000269|PubMed:26492198}.
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}.
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:0000269|PubMed:12921995, ECO:0000269|PubMed:21145089}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Genome polyprotein;
CC IsoId=Q66765-1; Sequence=Displayed;
CC Name=2B*;
CC IsoId=P0DJX6-1; Sequence=External;
CC -!- PTM: [Leader protein]: Phosphorylated. {ECO:0000269|PubMed:11883190,
CC ECO:0000269|PubMed:24335301}.
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: [Isoform Genome polyprotein]: Produced by conventional
CC translation. {ECO:0000250|UniProtKB:P12296}.
CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC {ECO:0000305}.
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DR EMBL; M81861; AAA43037.1; -; Genomic_RNA.
DR RefSeq; NP_056777.1; NC_001479.1.
DR SMR; Q66765; -.
DR MEROPS; C03.009; -.
DR iPTMnet; Q66765; -.
DR GeneID; 1493923; -.
DR KEGG; vg:1493923; -.
DR Proteomes; UP000002319; 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:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
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:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0039520; P:induction by virus of host autophagy; ISS:UniProtKB.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; 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; IDA:UniProtKB.
DR GO; GO:0039604; P:suppression by virus of host translation; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
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 CDD; cd00205; rhv_like; 3.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.60.120.20; -; 3.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 4.10.90.10; -; 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; SSF144251; SSF144251; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56672; SSF56672; 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 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; Reference proteome; Ribosomal frameshifting; RNA-binding;
KW RNA-directed RNA polymerase; T=pseudo3 icosahedral capsid protein;
KW Thiol protease; Transferase; Transport; Viral attachment to host cell;
KW Viral immunoevasion; 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_0000446100"
FT CHAIN 1..67
FT /note="Leader protein"
FT /id="PRO_0000423146"
FT CHAIN 68..393
FT /note="Capsid protein VP0"
FT /id="PRO_0000423147"
FT CHAIN 68..137
FT /note="Capsid protein VP4"
FT /id="PRO_5000143569"
FT CHAIN 138..393
FT /note="Capsid protein VP2"
FT /id="PRO_5000143570"
FT CHAIN 394..624
FT /note="Capsid protein VP3"
FT /id="PRO_5000143571"
FT CHAIN 625..901
FT /note="Capsid protein VP1"
FT /id="PRO_5000143572"
FT CHAIN 902..1044
FT /note="Protein 2A"
FT /id="PRO_5000143573"
FT CHAIN 1045..1194
FT /note="Protein 2B"
FT /id="PRO_5000143574"
FT CHAIN 1195..1519
FT /note="Protein 2C"
FT /id="PRO_5000143575"
FT CHAIN 1520..1607
FT /note="Protein 3A"
FT /id="PRO_5000143576"
FT CHAIN 1608..1627
FT /note="VPg"
FT /id="PRO_0000423148"
FT CHAIN 1628..1832
FT /note="Protease 3C"
FT /id="PRO_5000143577"
FT CHAIN 1833..2292
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_5000143578"
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:0000269|PubMed:21145089"
FT MOTIF 995..1003
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:21145089"
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 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:0000269|PubMed:24335301"
FT MOD_RES 47
FT /note="Phosphothreonine; by host CK2"
FT /evidence="ECO:0000269|PubMed:24335301"
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"
FT MUTAGEN 19
FT /note="C->A: Complete loss of inhibitory activity of
FT nucleocytoplasmic transport."
FT /evidence="ECO:0000269|PubMed:16888036,
FT ECO:0000269|PubMed:19073724"
FT MUTAGEN 35
FT /note="K->Q: 25% loss of 2A-Leader interaction."
FT /evidence="ECO:0000269|PubMed:25210192"
FT MUTAGEN 37
FT /note="D->A: 30% loss of 2A-Leader interaction."
FT /evidence="ECO:0000269|PubMed:25210192"
FT MUTAGEN 40
FT /note="W->A: 20% loss of 2A-Leader interaction."
FT /evidence="ECO:0000269|PubMed:25210192"
FT MUTAGEN 41
FT /note="Y->F: No effect on the inhibitory activity of
FT nucleocytoplasmic transport."
FT /evidence="ECO:0000269|PubMed:19073724"
FT MUTAGEN 47
FT /note="T->A: No effect on the inhibitory activity of
FT nucleocytoplasmic transport."
FT /evidence="ECO:0000269|PubMed:19073724"
FT MUTAGEN 993..994
FT /note="YY->AA: 5-10 fold decreased viral growth."
FT /evidence="ECO:0000269|PubMed:21145089"
FT MUTAGEN 996
FT /note="R->A: No effect on viral growth."
FT /evidence="ECO:0000269|PubMed:21145089"
FT MUTAGEN 998
FT /note="R->E: 5-10 fold decreased viral growth."
FT /evidence="ECO:0000269|PubMed:21145089"
FT MUTAGEN 1006
FT /note="Q->A: No effect on viral growth."
FT /evidence="ECO:0000269|PubMed:21145089"
FT MUTAGEN 1035
FT /note="L->A: Complete loss of interaction with host EIF4E."
FT /evidence="ECO:0000269|PubMed:21145089"
SQ SEQUENCE 2292 AA; 255459 MW; 01C0537888CEFC94 CRC64;
MATTMEQETC AHSLTFEECP KCSALQYRNG FYLLKYDEEW YPEELLTDGE DDVFDPELDM
EVVFELQGNS TSSDKNNSSS EGNEGVIINN FYSNQYQNSI DLSANAAGSD PPRTYGQFSN
LFSGAVNAFS NMLPLLADQN TEEMENLSDR VSQDTAGNTV TNTQSTVGRL VGYGTVHDGE
HPASCADTAS EKILAVERYY TFKVNDWTST QKPFEYIRIP LPHVLSGEDG GVFGAALRRH
YLVKTGWRVQ VQCNASQFHA GGLLVFMAPE YPTLDAFAMD NRWSKDNLPN GTRTQTNKKG
PFAMDHQNFW QWTLYPHQFL NLRTNTTVDL EVPYVNIAPT SSWTQHASWT LVIAVVAPLT
YSTGASTSLD ITASIQPVRP VFNGLRHETL SRQSPIPVTI REHAGTWYST LPDSTVPIYG
KTPVAPSNYM VGEYKDFLEI AQIPTFIGNK IPNAVPYIEA SNTAVKTQPL ATYQVTLSCS
CLANTFLAAL SRNFAQYRGS LVYTFVFTGT AMMKGKFLIA YTPPGAGKPT SRDQAMQATY
AIWDLGLNSS YSFTVPFISP THFRMVGTDQ VNITNADGWV TVWQLTPLTY PPGCPTSAKI
LTMVSAGKDF SLKMPISPAP WSPQGVENAE KGVTENTNAT ADFVAQPVYL PENQTKVAFF
YNRSSPIGAF TVKSGSLESG FAPFSNGTCP NSVILTPGPQ FDPAYDQLRP QRLTEIWGNG
NEETSKVFPL KSKQDYSFCL FSPFVYYKCD LEVTLSPHTS GNHGLLVRWC PTGTPTKPTT
QVLHEVSSLS EGRTPQVYSA GPGISNQISF VVPYNSPLSV LSAVWYNGHK RFDNTGSLGI
APNSDFGTLF FAGTKPDIKF TVYLRYKNKR VFCPRPTVFF PWPTSGDKID MTPRAGVLML
ESPNALDISR TYPTLHVLIQ FNHRGLEVRL FRHGHFWAET RADVILRSKT KQVSFLSNGN
YPSMDSRAPW NPWKNTYQAV LRAEPCRVTM DIYYKRVRPF RLPLVQKEWP VREENVFGLY
RIFNAHYAGY FADLLIHDIE TNPGPFMFRP RKQVFQTQGA AVSSMAQTLL PNDLASKAMG
SAFTALLDAN EDAQKAMKII KTLSSLSDAW ENVKETLNNP EFWKQLLSRC VQLIAGMTIA
VMHPDPLTLL CLGTLTAAEI TSQTSLCEEI AAKFKTIFIT PPPRFPTISL FQQQSPLKQV
NDIFSLAKNL DWAVKTVEKV VDWFGTWIVQ EEKEQTLDQL LQRFPEHAKR ISDLRNGMAA
YVECKESFDF FEKLYNQAVK EKRTGIAAVC EKFRQKHDHA TARCEPVVIV LRGDAGQGKS
LSSQVIAQAV SKTIFGRQSV YSLPPDSDFF DGYENQFAAI MDDLGQNPDG SDFTTFCQMV
STTNFLPNMA SLERKGTPFT SQLVVATTNL PEFRPVTIAH YPAVERRITF DYSVSAGPVC
SKTEAGYKVL DVERAFRPTG EAPLPCFQNN CLFLEKAGLQ FRDNRTKEII SLVDVIERAV
ARIERKKKVL TTVQTLVAQG PVDEVSFHSV VQQLKARQQA TDEQLEELQE AFAKVQERNS
VFSDWLKISA MLCAATLALS QVVKMAKAVK QMVKPDLVRV QLDEQEQGPY NETARVKPKT
LQLLDIQGPN PVMDFEKYVA KHVTAPIGFV YPTGVSTQTC LLVRGRTLVV NRHMAESDWT
SIVVRGVTHA RSTVKILAIA KAGKETDVSF IRLSSGPLFR DNTSKFVKAG DVLPTGAAPV
TGIMNTDIPM MYTGTFLKAG VSVPVETGQT FNHCIHYKAN TRKGWCGSAL LADLGGSKKI
LGIHSAGSMG IAAASIVSQE MIRAVVNAFE PQGALERLPD GPRIHVPRKT ALRPTVARQV
FQPAYAPAVL SKFDPRTEAD VDEVAFSKHT SNQESLPPVF RMVAKEYANR VFTLLGKDNG
RLTVKQALEG LEGMDPMDRN TSPGLPYTAL GMRRTDVVDW ESATLIPFAA ERLRKMNEGD
FSEVVYQTFL KDELRPIEKV QAAKTRIVDV PPFEHCILGR QLLGKFASKF QTQPGLELGS
AIGCDPDVHW TAFGVAMQGF ERVYDVDYSN FDSTHSVAMF RLLAEEFFTP ENGFDPLTRE
YLESLAISTH AFEEKRFLIT GGLPSGCAAT SMLNTIMNNI IIRAGLYLTY KNFEFDDVKV
LSYGDDLLVA TNYQLDFDKV RASLAKTGYK ITPANTTSTF PLNSTLEDVV FLKRKFKKEG
PLYRPVMNRE ALEAMLSYYR PGTLSEKLTS ITMLAVHSGK QEYDRLFAPF REVGVVVPSF
ESVEYRWRSL FW
