POLG_EMCV
ID POLG_EMCV Reviewed; 2290 AA.
AC P03304; Q66764;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 164.
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.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Cardiovirus.
OX NCBI_TaxID=12104;
OH NCBI_TaxID=9505; Aotus trivirgatus (Three-striped night monkey) (Douroucouli).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
OH NCBI_TaxID=9567; Mandrillus (forest baboons).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
OH NCBI_TaxID=10114; Rattus.
OH NCBI_TaxID=42415; Sigmodon hispidus (Hispid cotton rat).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
OH NCBI_TaxID=38020; marmosets.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND PROTEOLYTIC CLEAVAGE (GENOME
RP POLYPROTEIN).
RX PubMed=6324136; DOI=10.1093/nar/12.6.2969;
RA Palmenberg A.C., Kirby E.M., Janda M.R., Drake N.L., Duke G.M.,
RA Potratz K.F., Collett M.S.;
RT "The nucleotide and deduced amino acid sequences of the
RT encephalomyocarditis viral polyprotein coding region.";
RL Nucleic Acids Res. 12:2969-2985(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1337-2290.
RX PubMed=6091680;
RA Petrov N.A., Chizhikov V.E., Blinov V.M., Karginov V.A., Mikryukov N.N.,
RA Gutorov V.V., Grishaev M.P., Beklemishev A.B., Vassilenko S.K.;
RT "Nucleotide sequence of the 3'-terminus of encephalomyocarditis virus
RT RNA.";
RL Bioorg. Khim. 10:274-279(1984).
RN [3]
RP FUNCTION (VPG).
RX PubMed=6096134; DOI=10.1002/j.1460-2075.1984.tb02179.x;
RA Vartapetian A.B., Koonin E.V., Agol V.I., Bogdanov A.A.;
RT "Encephalomyocarditis virus RNA synthesis in vitro is protein-primed.";
RL EMBO J. 3:2593-2598(1984).
RN [4]
RP PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
RX PubMed=3467351; DOI=10.1073/pnas.84.1.21;
RA Arnold E., Luo M., Vriend G., Rossmann M.G., Palmenberg A.C., Parks G.D.,
RA Nicklin M.J., Wimmer E.;
RT "Implications of the picornavirus capsid structure for polyprotein
RT processing.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:21-25(1987).
RN [5]
RP INTERACTION WITH HUMAN TRIM22 (PROTEASE 3C).
RX PubMed=19218198; DOI=10.1099/vir.0.006288-0;
RA Eldin P., Papon L., Oteiza A., Brocchi E., Lawson T.G., Mechti N.;
RT "TRIM22 E3 ubiquitin ligase activity is required to mediate antiviral
RT activity against encephalomyocarditis virus.";
RL J. Gen. Virol. 90:536-545(2009).
RN [6]
RP SUBCELLULAR LOCATION (PROTEIN 3A).
RC STRAIN=BJC3;
RX PubMed=21460631; DOI=10.4161/auto.7.6.15267;
RA Zhang Y., Li Z., Ge X., Guo X., Yang H.;
RT "Autophagy promotes the replication of encephalomyocarditis virus in host
RT cells.";
RL Autophagy 7:613-628(2011).
RN [7]
RP FUNCTION (PROTEASE 3C).
RX PubMed=22837200; DOI=10.1128/jvi.00896-12;
RA Kobayashi M., Arias C., Garabedian A., Palmenberg A.C., Mohr I.;
RT "Site-specific cleavage of the host poly(A) binding protein by the
RT encephalomyocarditis virus 3C proteinase stimulates viral replication.";
RL J. Virol. 86:10686-10694(2012).
RN [8]
RP CLEAVAGE BY RIBOSOMAL SKIP (GENOME POLYPROTEIN).
RX PubMed=25258322; DOI=10.1074/jbc.m114.593343;
RA Machida K., Mikami S., Masutani M., Mishima K., Kobayashi T., Imataka H.;
RT "A translation system reconstituted with human factors proves that
RT processing of encephalomyocarditis virus proteins 2A and 2B occurs in the
RT elongation phase of translation without eukaryotic release factors.";
RL J. Biol. Chem. 289:31960-31971(2014).
RN [9]
RP FUNCTION (PROTEASE 3C).
RX PubMed=26363073; DOI=10.1074/jbc.m115.660761;
RA Huang L., Liu Q., Zhang L., Zhang Q., Hu L., Li C., Wang S., Li J.,
RA Zhang Y., Yu H., Wang Y., Zhong Z., Xiong T., Xia X., Wang X., Yu L.,
RA Deng G., Cai X., Cui S., Weng C.;
RT "Encephalomyocarditis Virus 3C Protease Relieves TRAF Family Member-
RT associated NF-kappaB Activator (TANK) Inhibitory Effect on TRAF6-mediated
RT NF-kappaB Signaling through Cleavage of TANK.";
RL J. Biol. Chem. 290:27618-27632(2015).
RN [10]
RP FUNCTION (PROTEASE 3C), MUTAGENESIS OF HIS-1671 AND CYS-1784, AND ACTIVE
RP SITE (PROTEASE 3C).
RC STRAIN=HB10;
RX PubMed=28487378; DOI=10.1042/bcj20161037;
RA Huang L., Xiong T., Yu H., Zhang Q., Zhang K., Li C., Hu L., Zhang Y.,
RA Zhang L., Liu Q., Wang S., He X., Bu Z., Cai X., Cui S., Li J., Weng C.;
RT "Encephalomyocarditis virus 3C protease attenuates type I interferon
RT production through disrupting the TANK-TBK1-IKKepsilon-IRF3 complex.";
RL Biochem. J. 474:2051-2065(2017).
RN [11]
RP FUNCTION (PROTEIN 2C), MUTAGENESIS OF LYS-1217; VAL-1218 AND VAL-1219, AND
RP INTERACTION WITH HOST IFIH1/MDA5.
RC STRAIN=NJ08;
RX PubMed=30312637; DOI=10.1016/j.antiviral.2018.10.010;
RA Li L., Fan H., Song Z., Liu X., Bai J., Jiang P.;
RT "Encephalomyocarditis virus 2C protein antagonizes interferon-beta
RT signaling pathway through interaction with MDA5.";
RL Antiviral Res. 161:70-84(2018).
RN [12]
RP INTERACTION WITH HUMAN TMEM39A (CAPSID PROTEINS VP1 AND VP2).
RX PubMed=31849860; DOI=10.3389/fmicb.2019.02680;
RA Li X., Ma R., Li Q., Li S., Zhang H., Xie J., Bai J., Idris A., Feng R.;
RT "Transmembrane Protein 39A Promotes the Replication of Encephalomyocarditis
RT Virus via Autophagy Pathway.";
RL Front. Microbiol. 10:2680-2680(2019).
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 (PubMed:30312637). {ECO:0000250|UniProtKB:P03305,
CC ECO:0000250|UniProtKB:P08545, ECO:0000269|PubMed:30312637}.
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:0000269|PubMed:6096134}.
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 (PubMed:22837200). Cleaves host TANK and disrupts the TANK-
CC TBK1-IKKepsilon-IRF3 complex, thereby inhibiting the induction of the
CC IFN-beta signal pathway (PubMed:28487378, PubMed:26363073).
CC {ECO:0000250|UniProtKB:P12296, ECO:0000269|PubMed:22837200,
CC ECO:0000269|PubMed:26363073, ECO:0000269|PubMed:28487378}.
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 (PubMed:19218198). {ECO:0000269|PubMed:19218198}.
CC -!- SUBUNIT: [Protein 2A]: Interacts with host EIF4E (By similarity).
CC Interacts with the leader protein (By similarity).
CC {ECO:0000250|UniProtKB:Q66765}.
CC -!- SUBUNIT: [Leader protein]: Interacts with host RAN; the complex L-RAN
CC recruits cellular kinases responsible for the L-induced
CC nucleocytoplasmic trafficking inhibition (By similarity). The complex
CC L-RAN can further bind to the host exportins XPO1/CRM1 and CSE1L/CAS
CC (By similarity). Interacts with the protein 2A (By similarity).
CC {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
CC (PubMed:30312637). {ECO:0000269|PubMed:30312637}.
CC -!- SUBUNIT: [Capsid protein VP1]: Interacts with host TMEM39A.
CC {ECO:0000269|PubMed:31849860}.
CC -!- SUBUNIT: [Capsid protein VP2]: Interacts with host TMEM39A.
CC {ECO:0000269|PubMed:31849860}.
CC -!- INTERACTION:
CC PRO_0000039791; P29590-5: PML; Xeno; NbExp=3; IntAct=EBI-6726189, EBI-304008;
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:0000269|PubMed:21460631}; 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:0000269|PubMed:21460631}.
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=P03304-1; Sequence=Displayed;
CC Name=2B*;
CC IsoId=P0DJX7-1; Sequence=External;
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
CC (PubMed:6324136, PubMed:3467351). The polyprotein seems to be
CC cotranslationally cleaved at the 2A/2B junction by a ribosomal skip
CC from one codon to the next without formation of a peptide bond
CC (PubMed:25258322). This process would release the P1-2A peptide from
CC the translational complex (PubMed:25258322).
CC {ECO:0000269|PubMed:25258322, ECO:0000269|PubMed:3467351,
CC ECO:0000269|PubMed:6324136}.
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; X00463; CAA25152.1; -; Genomic_RNA.
DR EMBL; M54935; AAA43036.1; -; Genomic_RNA.
DR PIR; A03906; GNNYE.
DR SMR; P03304; -.
DR IntAct; P03304; 1.
DR MEROPS; C03.009; -.
DR PRIDE; P03304; -.
DR Proteomes; UP000008660; 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; IDA:CACAO.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0039520; P:induction by virus of host autophagy; IDA: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:0039503; P:suppression by virus of host innate immune response; IDA:UniProtKB.
DR GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0039554; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host MDA-5 activity; 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; IEA:UniProtKB-KW.
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; 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..2290
FT /note="Genome polyprotein"
FT /id="PRO_0000446093"
FT CHAIN 1..67
FT /note="Leader protein"
FT /id="PRO_0000039780"
FT CHAIN 68..391
FT /note="Capsid protein VP0"
FT /id="PRO_0000310967"
FT CHAIN 68..136
FT /note="Capsid protein VP4"
FT /id="PRO_0000039781"
FT CHAIN 137..391
FT /note="Capsid protein VP2"
FT /id="PRO_0000039782"
FT CHAIN 392..622
FT /note="Capsid protein VP3"
FT /id="PRO_0000039783"
FT CHAIN 623..899
FT /note="Capsid protein VP1"
FT /id="PRO_0000039784"
FT CHAIN 900..1042
FT /note="Protein 2A"
FT /id="PRO_0000039785"
FT CHAIN 1043..1192
FT /note="Protein 2B"
FT /id="PRO_0000039786"
FT CHAIN 1193..1517
FT /note="Protein 2C"
FT /id="PRO_0000039787"
FT CHAIN 1518..1605
FT /note="Protein 3A"
FT /id="PRO_0000039788"
FT CHAIN 1606..1625
FT /note="VPg"
FT /id="PRO_0000039789"
FT CHAIN 1626..1830
FT /note="Protease 3C"
FT /id="PRO_0000039790"
FT CHAIN 1831..2290
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000039791"
FT DOMAIN 1279..1445
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1628..1820
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 2059..2177
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 1028..1034
FT /note="Host EIF4E binding"
FT /evidence="ECO:0000250|UniProtKB:Q66765"
FT MOTIF 993..1001
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q66765"
FT ACT_SITE 1671
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222,
FT ECO:0000305|PubMed:28487378"
FT ACT_SITE 1705
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1784
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222,
FT ECO:0000305|PubMed:28487378"
FT ACT_SITE 2065
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT ACT_SITE 2163
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT BINDING 1311..1318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 136..137
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 391..392
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000269|PubMed:3467351,
FT ECO:0000269|PubMed:6324136"
FT SITE 622..623
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000269|PubMed:3467351,
FT ECO:0000269|PubMed:6324136"
FT SITE 899..900
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000269|PubMed:3467351,
FT ECO:0000269|PubMed:6324136"
FT SITE 1042..1043
FT /note="Cleavage; by ribosomal skip"
FT /evidence="ECO:0000269|PubMed:25258322"
FT SITE 1192..1193
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000269|PubMed:3467351,
FT ECO:0000269|PubMed:6324136"
FT SITE 1517..1518
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000269|PubMed:3467351,
FT ECO:0000269|PubMed:6324136"
FT SITE 1605..1606
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000269|PubMed:3467351,
FT ECO:0000269|PubMed:6324136"
FT SITE 1625..1626
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000269|PubMed:3467351,
FT ECO:0000269|PubMed:6324136"
FT SITE 1830..1831
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000269|PubMed:3467351,
FT ECO:0000269|PubMed:6324136"
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 1608
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 1217
FT /note="K->A: No effect on the interaction between protein
FT 2C and host IFIH1/MDA5 and on the inhibition of IRF3
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:30312637"
FT MUTAGEN 1218
FT /note="V->A: Loss of interaction between protein 2C and
FT host IFIH1/MDA5 and loss of inhibition of IRF3
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:30312637"
FT MUTAGEN 1219
FT /note="V->A: No effect on the interaction between protein
FT 2C and host IFIH1/MDA5 and on the inhibition of IRF3
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:30312637"
FT MUTAGEN 1671
FT /note="H->A: Complete loss of inhibition of host TBK1-TANK
FT and IKKepsilon-TANK-mediated IFN-beta expression, complete
FT loss of IRF3 phosphorylation; when associated with A-1784."
FT /evidence="ECO:0000269|PubMed:28487378"
FT MUTAGEN 1784
FT /note="C->A: Complete loss of inhibition of host TBK1-TANK
FT and IKKepsilon-TANK-mediated IFN-beta expression, complete
FT loss of IRF3 phosphorylation; when associated with A-1671."
FT /evidence="ECO:0000269|PubMed:28487378"
FT CONFLICT 1337
FT /note="S -> P (in Ref. 2; AAA43036)"
FT /evidence="ECO:0000305"
FT CONFLICT 1397
FT /note="F -> L (in Ref. 2; AAA43036)"
FT /evidence="ECO:0000305"
FT CONFLICT 1518
FT /note="G -> A (in Ref. 2; AAA43036)"
FT /evidence="ECO:0000305"
FT CONFLICT 1537
FT /note="Q -> E (in Ref. 2; AAA43036)"
FT /evidence="ECO:0000305"
FT CONFLICT 1557
FT /note="N -> S (in Ref. 2; AAA43036)"
FT /evidence="ECO:0000305"
FT CONFLICT 1612
FT /note="A -> T (in Ref. 2; AAA43036)"
FT /evidence="ECO:0000305"
FT CONFLICT 1755
FT /note="L -> V (in Ref. 2; AAA43036)"
FT /evidence="ECO:0000305"
FT CONFLICT 1916
FT /note="D -> N (in Ref. 2; AAA43036)"
FT /evidence="ECO:0000305"
FT CONFLICT 1987..1988
FT /note="FL -> IH (in Ref. 2; AAA43036)"
FT /evidence="ECO:0000305"
FT CONFLICT 2008
FT /note="V -> I (in Ref. 2; AAA43036)"
FT /evidence="ECO:0000305"
FT CONFLICT 2049
FT /note="T -> H (in Ref. 2; AAA43036)"
FT /evidence="ECO:0000305"
FT CONFLICT 2194
FT /note="T -> K (in Ref. 2; AAA43036)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2290 AA; 255758 MW; 26BC81BB7CF68CB5 CRC64;
MATTMEQETC AHSLTFEECP KCSALQYRNG FYLLKYDEEW YPEELLTDGE DDVFDPELDM
EVVFELQGNS TSSDKNNSSS EGNEGVIINN FYSNQYQNSI DLSANAAGSD PPRLRSIFES
LSGAVNAFSN MLPLLADQNT EEMENLSDRG LKTLPAIRSQ TPSQQWAVLS VMVPFMMESI
RHHVLTLLQK RFWRWKGTTP SRLMIGHQHK SPLSTSAFPF LTSCPVKMVV SLVALRRHYL
VKTGWRVQVQ CNASQFHAGG LLVFMAPEYP TLDAFAMDNR WSKDNLPNGT RTQTNKKGPF
AMDHQNFWQW TLYPHQFLNL RTNTTVDLEV PYVNIAPTSS WTQHASWTLV IAVVAPLTYS
TGASTSLDIT ASIQPVRPVF NGLRHETLSR QSPIPVTIRE HAGTWYSTLP DSTVPIYGKT
PVAPSNYMVG EYKDFLEIAQ IPTFIGNKIP NAVPYIEASN TAVKTQPLAT YQVTLSCSCL
ANTFLAALSR NFAQYRGSLV YTFVFTGTAM MKGKFLIAYT PPGAGKPTSR DQAMQATYAI
WDLGLNSSYS FTVPFISPTH FRMVGTDQVN ITNADGWVTV WQLTPLTYPP GCPTSAKILT
MVSAGKDFSL KMPISPAPWS PQGVENAEKG VTENTNATAD FVAQPVYLPE NQTKVAFFYN
RSSPIGAFTV KSGSLESGFA PFSNGTCPNS VILTPGPQFD PAYDQLRPQR LTEIWGNGNE
ETSKVFPLKS KQDYSFCLFS PFVYYKCDLE VTLSPHTSGN HGLLVRWCPT GTPTKPTTQV
LHEVSSLSEG RTPQVYSAGP GISNQISFVV PYNSPLSVLS AVWYNGHKRF DNTGSLGIAP
NSDFGTLFFA GTKPDIKFTV YLRYKNKRVF CPRPTVFFPW PTSGDKIDMT PRAGVLMLES
PNALDISRTY PTLHVLIQFN HRGLEVRLFR HGHFWAETRA DVILRSKTKQ VSFLSNGNYP
SMDSRAPWNP WKNTYQAVLR AEPCRVTMDI YYKRVRPFRL PLVQKEWPVR EENVFGLYRI
FNAHYAGYFA DLLIHDIETN PGPFMFRPRK QVFQTQGAAV SSMAQTLLPN DLASKAMGSA
FTALLDANED AQKAMKIIKT LSSLSDAWEN VKETLNNPEF WKQLLSRCVQ LIAGMTIAVM
HPDPLTLLCL GTLTAAEITS QTSLCEEIAA KFKTIFITPP PRFPTISLFQ QQSPLKQVND
IFSLAKNLDW AVKTVEKVVD WFGTWIVQEE KEQTLDQLLQ RFPEHAKRIS DLRNGMAAYV
ECKESFDFFE KLYNQAVKEK RTGIAAVCEK FRQKHDHATA RCEPVVIVLR GDAGQGKSLS
SQVIAQAVSK TIFGRQSVYS LPPDSDFFDG YENQFAAIMD DLGQNPDGSD FTTFCQMVST
TNFLPNMASL ERKGTPFTSQ LVVATTNLPE FRPVTIAHYP AVERRITFDY SVSAGPVCSK
TEAGYKVLDV ERAFRPTGEA PLPCFQNNCL FLEKAGLQFR DNRTKEIISL VDVIERAVAR
IERKKKVLTT VQTLVAQGPV DEVSFHSVVQ QLKARQQATD EQLEELQEAF AKVQERNSVF
SDWLKISAML CAATLALSQV VKMAKAVKQM VKPDLVRVQL DEQEQGPYNE TARVKPKTLQ
LLDIQGPNPV MDFEKYVAKH VTAPIGFVYP TGVSTQTCLL VRGRTLVVNR HMAESDWTSI
VVRGVTHARS TVKILAIAKA GKETDVSFIR LSSGPLFRDN TSKFVKAGDV LPTGAAPVTG
IMNTDIPMMY TGTFLKAGVS VPVETGQTFN HCIHYKANTR KGWCGSALLA DLGGSKKILG
IHSAGSMGIA AASIVSQEMI RAVVNAFEPQ GALERLPDGP RIHVPRKTAL RPTVARQVFQ
PAYAPAVLSK FDPRTEADVD EVAFSKHTSN QESLPPVFRM VAKEYANRVF TLLGKDNGRL
TVKQALEGLE GMDPMDRNTS PGLPYTALGM RRTDVVDWES ATLIPFAAER LRKMNEGDFS
EVVYQTFLKD ELRPIEKVQA AKTRIVDVPP FEHCILGRQL LGKFASKFQT QPGLELGSAI
GCDPDVHWTA FGVAMQGFER VYDVDYSNFD STHSVAMFRL LAEEFFTPEN GFDPLTREYL
ESLAISTHAF EEKRFLITGG LPSGCAATSM LNTIMNNIII RAGLYLTYKN FEFDDVKVLS
YGDDLLVATN YQLDFDKVRA SLAKTGYKIT PANTTSTFPL NSTLEDVVFL KRKFKKEGPL
YRPVMNREAL EAMLSYYRPG TLSEKLTSIT MLAVHSGKQE YDRLFAPFRE VGVVVPSFES
VEYRWRSLFW
