POLG_FMDVO
ID POLG_FMDVO Reviewed; 2332 AA.
AC P03305;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Leader protease;
DE Short=Lb(pro);
DE EC=3.4.22.46 {ECO:0000269|PubMed:11034318};
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 AltName: Full=P52;
DE Contains:
DE RecName: Full=Protein 2B;
DE Short=P2B;
DE Contains:
DE RecName: Full=Protein 2C;
DE Short=P2C;
DE EC=3.6.1.15;
DE Contains:
DE RecName: Full=Protein 3A;
DE Short=P3A;
DE Contains:
DE RecName: Full=Protein 3B-1;
DE Short=P3B-1;
DE AltName: Full=Genome-linked protein VPg1;
DE Contains:
DE RecName: Full=Protein 3B-2;
DE Short=P3B-2;
DE AltName: Full=Genome-linked protein VPg2;
DE Contains:
DE RecName: Full=Protein 3B-3;
DE Short=P3B-3;
DE AltName: Full=Genome-linked protein VPg3;
DE Contains:
DE RecName: Full=Protease 3C;
DE EC=3.4.22.28 {ECO:0000269|PubMed:3041041};
DE AltName: Full=Picornain 3C;
DE Short=P3C;
DE AltName: Full=Protease P20B;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase 3D-POL;
DE Short=P3D-POL;
DE EC=2.7.7.48;
DE AltName: Full=P56A;
OS Foot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/1966
OS serotype O) (FMDV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Aphthovirus.
OX NCBI_TaxID=73482;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=9925; Capra hircus (Goat).
OH NCBI_TaxID=9850; Cervidae (deer).
OH NCBI_TaxID=9363; Erinaceidae (hedgehogs).
OH NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH NCBI_TaxID=9940; Ovis aries (Sheep).
OH NCBI_TaxID=10116; Rattus norvegicus (Rat).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6089122; DOI=10.1093/nar/12.16.6587;
RA Forss S., Strebel K., Beck E., Schaller H.;
RT "Nucleotide sequence and genome organization of foot-and-mouth disease
RT virus.";
RL Nucleic Acids Res. 12:6587-6601(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate O1BFS/Britain/1968;
RX PubMed=6298715; DOI=10.1093/nar/10.24.8285;
RA Makoff A.J., Paynter C.A., Rowlands D.J., Boothroyd J.C.;
RT "Comparison of the amino acid sequence of the major immunogen from three
RT serotypes of foot and mouth disease virus.";
RL Nucleic Acids Res. 10:8285-8295(1982).
RN [3]
RP CHARACTERIZATION.
RX PubMed=15350134; DOI=10.1021/bi049340d;
RA Kuehnel E., Cencic R., Foeger N., Skern T.;
RT "Foot-and-mouth disease virus leader proteinase: specificity at the P2 and
RT P3 positions and comparison with other papain-like enzymes.";
RL Biochemistry 43:11482-11490(2004).
RN [4]
RP ALTERNATIVE INITIATION.
RX PubMed=3033601; DOI=10.1093/nar/15.8.3305;
RA Sangar D.V., Newton S.E., Rowlands D.J., Clarke B.E.;
RT "All foot and mouth disease virus serotypes initiate protein synthesis at
RT two separate AUGs.";
RL Nucleic Acids Res. 15:3305-3315(1987).
RN [5]
RP FUNCTION (PROTEASE 3C).
RX PubMed=3041041; DOI=10.1128/jvi.61.10.3199-3207.1987;
RA Vakharia V.N., Devaney M.A., Moore D.M., Dunn J.J., Grubman M.J.;
RT "Proteolytic processing of foot-and-mouth disease virus polyproteins
RT expressed in a cell-free system from clone-derived transcripts.";
RL J. Virol. 61:3199-3207(1987).
RN [6]
RP FUNCTION (CAPSID PROTEIN VP1).
RX PubMed=2543752; DOI=10.1099/0022-1317-70-3-625;
RA Fox G., Parry N.R., Barnett P.V., McGinn B., Rowlands D.J., Brown F.;
RT "The cell attachment site on foot-and-mouth disease virus includes the
RT amino acid sequence RGD (arginine-glycine-aspartic acid).";
RL J. Gen. Virol. 70:625-637(1989).
RN [7]
RP FUNCTION (PROTEIN 2A).
RX PubMed=1658199; DOI=10.1099/0022-1317-72-11-2727;
RA Ryan M.D., King A.M., Thomas G.P.;
RT "Cleavage of foot-and-mouth disease virus polyprotein is mediated by
RT residues located within a 19 amino acid sequence.";
RL J. Gen. Virol. 72:2727-2732(1991).
RN [8]
RP FUNCTION (LEADER PROTEASE).
RX PubMed=8386879; DOI=10.1006/viro.1993.1267;
RA Medina M., Domingo E., Brangwyn J.K., Belsham G.J.;
RT "The two species of the foot-and-mouth disease virus leader protein,
RT expressed individually, exhibit the same activities.";
RL Virology 194:355-359(1993).
RN [9]
RP FUNCTION (LEADER PROTEASE).
RC STRAIN=Isolate O1k;
RX PubMed=11034318; DOI=10.1016/s0014-5793(00)01928-1;
RA Glaser W., Skern T.;
RT "Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A
RT in vitro.";
RL FEBS Lett. 480:151-155(2000).
RN [10]
RP POLYPROTEIN PROCESSING.
RX PubMed=11297676; DOI=10.1099/0022-1317-82-5-1013;
RA Donnelly M.L.L., Luke G., Mehrotra A., Li X., Hughes L.E., Gani D.,
RA Ryan M.D.;
RT "Analysis of the aphthovirus 2A/2B polyprotein 'cleavage' mechanism
RT indicates not a proteolytic reaction, but a novel translational effect: a
RT putative ribosomal 'skip'.";
RL J. Gen. Virol. 82:1013-1025(2001).
RN [11]
RP FUNCTION (LEADER PROTEASE).
RX PubMed=15016848; DOI=10.1128/jvi.78.7.3271-3278.2004;
RA Gradi A., Foeger N., Strong R., Svitkin Y.V., Sonenberg N., Skern T.,
RA Belsham G.J.;
RT "Cleavage of eukaryotic translation initiation factor 4GII within foot-and-
RT mouth disease virus-infected cells: identification of the L-protease
RT cleavage site in vitro.";
RL J. Virol. 78:3271-3278(2004).
RN [12]
RP COVALENT RNA LINKAGE OF 3B PROTEINS, URIDYLYLATION, AND FUNCTION
RP (RNA-DIRECTED RNA POLYMERASE 3D-POL).
RX PubMed=15919922; DOI=10.1128/jvi.79.12.7698-7706.2005;
RA Nayak A., Goodfellow I.G., Belsham G.J.;
RT "Factors required for the uridylylation of the foot-and-mouth disease virus
RT 3B1, 3B2, and 3B3 peptides by the RNA-dependent RNA polymerase (3Dpol) in
RT vitro.";
RL J. Virol. 79:7698-7706(2005).
RN [13]
RP FUNCTION (LEADER PROTEASE), AND SUBCELLULAR LOCATION (LEADER PROTEASE).
RX PubMed=17881445; DOI=10.1128/jvi.01467-07;
RA de Los Santos T., Diaz-San Segundo F., Grubman M.J.;
RT "Degradation of nuclear factor kappa B during foot-and-mouth disease virus
RT infection.";
RL J. Virol. 81:12803-12815(2007).
RN [14]
RP FUNCTION (CAPSID PROTEIN VP2), FUNCTION (CAPSID PROTEIN VP3), AND FUNCTION
RP (CAPSID PROTEIN VP1).
RX PubMed=18614639; DOI=10.1128/jvi.00732-08;
RA O'Donnell V., Larocco M., Baxt B.;
RT "Heparan sulfate-binding foot-and-mouth disease virus enters cells via
RT caveola-mediated endocytosis.";
RL J. Virol. 82:9075-9085(2008).
RN [15]
RP FUNCTION (CAPSID PROTEIN VP1).
RX PubMed=18045932; DOI=10.1128/jvi.01480-07;
RA Dicara D., Burman A., Clark S., Berryman S., Howard M.J., Hart I.R.,
RA Marshall J.F., Jackson T.;
RT "Foot-and-mouth disease virus forms a highly stable, EDTA-resistant complex
RT with its principal receptor, integrin alphavbeta6: implications for
RT infectiousness.";
RL J. Virol. 82:1537-1546(2008).
RN [16]
RP REVIEW.
RX PubMed=19556802; DOI=10.1159/000226121;
RA Ruiz-Saenz J., Goez Y., Tabares W., Lopez-Herrera A.;
RT "Cellular receptors for foot and mouth disease virus.";
RL Intervirology 52:201-212(2009).
RN [17]
RP FUNCTION (PROTEIN 2C).
RX PubMed=20507978; DOI=10.1074/jbc.m110.129940;
RA Sweeney T.R., Cisnetto V., Bose D., Bailey M., Wilson J.R., Zhang X.,
RA Belsham G.J., Curry S.;
RT "Foot-and-mouth disease virus 2C is a hexameric AAA+ protein with a
RT coordinated ATP hydrolysis mechanism.";
RL J. Biol. Chem. 285:24347-24359(2010).
RN [18]
RP FUNCTION (LEADER PROTEASE).
RX PubMed=21307201; DOI=10.1128/jvi.02589-10;
RA Wang D., Fang L., Li P., Sun L., Fan J., Zhang Q., Luo R., Liu X., Li K.,
RA Chen H., Chen Z., Xiao S.;
RT "The leader proteinase of foot-and-mouth disease virus negatively regulates
RT the type I interferon pathway by acting as a viral deubiquitinase.";
RL J. Virol. 85:3758-3766(2011).
RN [19]
RP FUNCTION (PROTEIN 2C), AND INTERACTION WITH HOST BECN1 (PROTEIN 2C).
RX PubMed=22933281; DOI=10.1128/jvi.01610-12;
RA Gladue D.P., O'Donnell V., Baker-Branstetter R., Holinka L.G.,
RA Pacheco J.M., Fernandez-Sainz I., Lu Z., Brocchi E., Baxt B., Piccone M.E.,
RA Rodriguez L., Borca M.V.;
RT "Foot-and-mouth disease virus nonstructural protein 2C interacts with
RT Beclin1, modulating virus replication.";
RL J. Virol. 86:12080-12090(2012).
RN [20]
RP FUNCTION (PROTEIN 2C), AND INTERACTION WITH HOST VIM (PROTEIN 2C).
RX PubMed=23576498; DOI=10.1128/jvi.00448-13;
RA Gladue D.P., O'Donnell V., Baker-Branstetter R., Holinka L.G.,
RA Pacheco J.M., Fernandez Sainz I., Lu Z., Ambroggio X., Rodriguez L.,
RA Borca M.V.;
RT "Foot-and-mouth disease virus modulates cellular vimentin for virus
RT survival.";
RL J. Virol. 87:6794-6803(2013).
RN [21]
RP SUBCELLULAR LOCATION (RNA-DIRECTED RNA POLYMERASE 3D-POL), AND NUCLEAR
RP LOCALIZATIION SIGNAL (RNA-DIRECTED RNA POLYMERASE 3D-POL).
RX PubMed=23886493; DOI=10.1016/j.virol.2013.06.011;
RA Sanchez-Aparicio M.T., Rosas M.F., Sobrino F.;
RT "Characterization of a nuclear localization signal in the foot-and-mouth
RT disease virus polymerase.";
RL Virology 444:203-210(2013).
RN [22]
RP TOPOLOGY (PROTEIN 3A), AND SUBCELLULAR LOCATION (PROTEIN 3A).
RX PubMed=25275544; DOI=10.1371/journal.pone.0106685;
RA Gonzalez-Magaldi M., Martin-Acebes M.A., Kremer L., Sobrino F.;
RT "Membrane topology and cellular dynamics of foot-and-mouth disease virus 3A
RT protein.";
RL PLoS ONE 9:E106685-E106685(2014).
RN [23]
RP FUNCTION (PROTEIN 3A), INTERACTION WITH HOST DCTN3 (PROTEIN 3A), AND
RP SUBCELLULAR LOCATION (PROTEIN 3A).
RX PubMed=24352458; DOI=10.1128/jvi.03059-13;
RA Gladue D.P., O'Donnell V., Baker-Bransetter R., Pacheco J.M., Holinka L.G.,
RA Arzt J., Pauszek S., Fernandez-Sainz I., Fletcher P., Brocchi E., Lu Z.,
RA Rodriguez L.L., Borca M.V.;
RT "Interaction of foot-and-mouth disease virus nonstructural protein 3A with
RT host protein DCTN3 is important for viral virulence in cattle.";
RL J. Virol. 88:2737-2747(2014).
RN [24]
RP FUNCTION (PROTEIN 2B), SUBUNIT (PROTEIN 2B), SUBCELLULAR LOCATION (PROTEIN
RP 2B), AND TOPOLOGY (PROTEIN 2B).
RX PubMed=25946195; DOI=10.1371/journal.pone.0125828;
RA Ao D., Guo H.C., Sun S.Q., Sun D.H., Fung T.S., Wei Y.Q., Han S.C.,
RA Yao X.P., Cao S.Z., Liu D.X., Liu X.T.;
RT "Viroporin Activity of the Foot-and-Mouth Disease Virus Non-Structural 2B
RT Protein.";
RL PLoS ONE 10:E0125828-E0125828(2015).
RN [25]
RP FUNCTION (CAPSID PROTEIN VP1), AND INTERACTION WITH HOST ITGAV/ITGB6
RP (CAPSID PROTEIN VP1).
RX PubMed=28534487; DOI=10.1038/ncomms15408;
RA Kotecha A., Wang Q., Dong X., Ilca S.L., Ondiviela M., Zihe R., Seago J.,
RA Charleston B., Fry E.E., Abrescia N.G.A., Springer T.A., Huiskonen J.T.,
RA Stuart D.I.;
RT "Rules of engagement between alphavbeta6 integrin and foot-and-mouth
RT disease virus.";
RL Nat. Commun. 8:15408-15408(2017).
RN [26]
RP FUNCTION (LEADER PROTEASE), AND INTERACTION WITH HOST ISG15 (LEADER
RP PROTEASE).
RX PubMed=29463763; DOI=10.1073/pnas.1710617115;
RA Swatek K.N., Aumayr M., Pruneda J.N., Visser L.J., Berryman S., Kueck A.F.,
RA Geurink P.P., Ovaa H., van Kuppeveld F.J.M., Tuthill T.J., Skern T.,
RA Komander D.;
RT "Irreversible inactivation of ISG15 by a viral leader protease enables
RT alternative infection detection strategies.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:2371-2376(2018).
RN [27]
RP FUNCTION (PROTEIN 3A), AND SUBCELLULAR LOCATION (PROTEIN 3A).
RX PubMed=29536193; DOI=10.1007/s00705-018-3795-9;
RA Lotufo C.M., Wilda M., Giraldez A.N., Grigera P.R., Mattion N.M.;
RT "Relevance of the N-terminal and major hydrophobic domains of non-
RT structural protein 3A in the replicative process of a DNA-launched foot-
RT and-mouth disease virus replicon.";
RL Arch. Virol. 163:1769-1778(2018).
RN [28]
RP FUNCTION (CAPSID PROTEIN VP1), AND INTERACTION WITH HOST MAVS (CAPSID
RP PROTEIN VP1).
RX PubMed=33232374; DOI=10.1371/journal.ppat.1009057;
RA Ekanayaka P., Lee S.Y., Herath T.U.B., Kim J.H., Kim T.H., Lee H.,
RA Chathuranga K., Chathuranga W.A.G., Park J.H., Lee J.S.;
RT "Foot-and-mouth disease virus VP1 target the MAVS to inhibit type-I
RT interferon signaling and VP1 E83K mutation results in virus attenuation.";
RL PLoS Pathog. 16:e1009057-e1009057(2020).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), FUNCTION (CAPSID PROTEIN VP2),
RP FUNCTION (CAPSID PROTEIN VP3), FUNCTION (CAPSID PROTEIN VP1), SUBCELLULAR
RP LOCATION (CAPSID PROTEIN VP2), SUBCELLULAR LOCATION (CAPSID PROTEIN VP3),
RP AND SUBCELLULAR LOCATION (CAPSID PROTEIN VP1).
RX PubMed=2537470; DOI=10.1038/337709a0;
RA Acharya R., Fry E., Stuart D., Fox G., Rowlands D., Brown F.;
RT "The three-dimensional structure of foot-and-mouth disease virus at 2.9-A
RT resolution.";
RL Nature 337:709-716(1989).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 29-201 OF MUTANT ALA-51.
RX PubMed=9857201; DOI=10.1093/emboj/17.24.7469;
RA Guarne A., Tormo J., Kirchweger R., Pfistermueller D., Fita I., Skern T.;
RT "Structure of the foot-and-mouth disease virus leader protease: a papain-
RT like fold adapted for self-processing and eIF4G recognition.";
RL EMBO J. 17:7469-7479(1998).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 202-286; 287-504 AND 505-724.
RX PubMed=9927414; DOI=10.1093/emboj/18.3.543;
RA Fry E.E., Lea S.M., Jackson T., Newman J.W., Ellard F.M., Blakemore W.E.,
RA Abu-Ghazaleh R., Samuel A., King A.M., Stuart D.I.;
RT "The structure and function of a foot-and-mouth disease virus-
RT oligosaccharide receptor complex.";
RL EMBO J. 18:543-554(1999).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-195 OF MUTANT ALA-51/SER-133.
RX PubMed=11183785; DOI=10.1006/jmbi.2000.4115;
RA Guarne A., Hampoelz B., Glaser W., Carpena X., Tormo J., Fita I., Skern T.;
RT "Structural and biochemical features distinguish the foot-and-mouth disease
RT virus leader proteinase from other papain-like enzymes.";
RL J. Mol. Biol. 302:1227-1240(2000).
RN [33]
RP STRUCTURE BY NMR OF 29-195.
RX PubMed=17897674; DOI=10.1016/j.jmb.2007.08.061;
RA Cencic R., Mayer C., Juliano M.A., Juliano L., Konrat R., Kontaxis G.,
RA Skern T.;
RT "Investigating the substrate specificity and oligomerisation of the leader
RT protease of foot and mouth disease virus using NMR.";
RL J. Mol. Biol. 373:1071-1087(2007).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 29-195, FUNCTION (LEADER
RP PROTEASE), AND ACTIVE SITE (LEADER PROTEASE).
RX PubMed=25240326; DOI=10.1016/j.virol.2014.08.023;
RA Steinberger J., Grishkovskaya I., Cencic R., Juliano L., Juliano M.A.,
RA Skern T.;
RT "Foot-and-mouth disease virus leader proteinase: structural insights into
RT the mechanism of intermolecular cleavage.";
RL Virology 468:397-408(2014).
CC -!- FUNCTION: [Leader protease]: Autocatalytically cleaves itself from the
CC polyprotein at the L/VP0 junction. Cleaves also the host translation
CC initiation factors EIF4G1 and EIF4G3, in order to shutoff the capped
CC cellular mRNA transcription. Plays a role in counteracting host innate
CC antiviral response using diverse mechanisms. Possesses a deubiquitinase
CC activity acting on both 'Lys'-48 and 'Lys'-63-linked polyubiquitin
CC chains. In turn, inhibits the ubiquitination and subsequent activation
CC of key signaling molecules of type I IFN response such as host DDX58,
CC TBK1, TRAF3 and TRAF6. Inhibits host NF-kappa-B activity by inducing a
CC decrease in RELA mRNA levels. Cleaves a peptide bond in the C-terminus
CC of host ISG15, resulting in the damaging of this mofidier that can no
CC longer be attached to target proteins. Cleaves also host G3BP1 and
CC G3BP2 in order to inhibit cytoplasmic stress granules assembly.
CC {ECO:0000250|UniProtKB:P03308, ECO:0000269|PubMed:11034318,
CC ECO:0000269|PubMed:15016848, ECO:0000269|PubMed:17881445,
CC ECO:0000269|PubMed:21307201, ECO:0000269|PubMed:29463763,
CC ECO:0000269|PubMed:8386879}.
CC -!- FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid
CC shell. After binding to the host receptor, the capsid undergoes
CC conformational changes. Capsid protein VP4 is released, capsid protein
CC VP1 N-terminus is externalized, and together, they shape a pore in the
CC host membrane through which the viral genome is translocated into the
CC host cell cytoplasm. After genome has been released, the channel
CC shrinks. {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP1 and VP3. The capsid is composed
CC of 60 copies of each capsid protein organized in the form of twelve
CC pentamers and encloses the viral positive strand RNA genome.
CC {ECO:0000269|PubMed:2537470}.
CC -!- FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3. The capsid is composed
CC of 60 copies of each capsid protein organized in the form of twelve
CC pentamers and encloses the viral positive strand RNA genome. Mediates
CC cell entry by attachment to an integrin receptor, usually host
CC ITGAV/ITGB6, via a conserved arginine-glycine-aspartic acid (R-G-D)
CC motif. In addition, targets host MAVS to suppress type I IFN pathway
CC (PubMed:33232374). {ECO:0000269|PubMed:18045932,
CC ECO:0000269|PubMed:2537470, ECO:0000269|PubMed:2543752,
CC ECO:0000269|PubMed:28534487, ECO:0000269|PubMed:33232374}.
CC -!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP0 and VP3. The capsid is composed
CC of 60 copies of each capsid protein organized in the form of twelve
CC pentamers and encloses the viral positive strand RNA genome.
CC {ECO:0000269|PubMed:2537470}.
CC -!- FUNCTION: [Protein 2A]: Mediates self-processing of the polyprotein by
CC a translational effect termed 'ribosome skipping'. Mechanistically, 2A-
CC mediated cleavage occurs between the C-terminal glycine and the proline
CC of the downstream protein 2B. In the case of foot-and-mouth disease
CC virus, the 2A oligopeptide is post-translationally 'trimmed' from the
CC C-terminus of the upstream protein 1D by 3C proteinase.
CC {ECO:0000269|PubMed:1658199}.
CC -!- FUNCTION: [Protein 2B]: Plays an essential role in the virus
CC replication cycle by acting as a viroporin. Creates a pore in the host
CC reticulum endoplasmic and as a consequence releases Ca2+ in the
CC cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium
CC may trigger membrane trafficking and transport of viral ER-associated
CC proteins to viroplasms, sites of viral genome replication.
CC {ECO:0000269|PubMed:25946195}.
CC -!- FUNCTION: [Protein 2C]: Associates with and induces structural
CC rearrangements of intracellular membranes. Triggers host autophagy by
CC interacting with host BECN1 and thereby promotes viral replication.
CC Participates in viral replication and interacts with host DHX9.
CC Displays RNA-binding, nucleotide binding and NTPase activities. May
CC play a role in virion morphogenesis and viral RNA encapsidation by
CC interacting with the capsid protein VP3. {ECO:0000269|PubMed:20507978,
CC ECO:0000269|PubMed:21307201, ECO:0000269|PubMed:22933281,
CC ECO:0000269|PubMed:23576498}.
CC -!- FUNCTION: [Protein 3A]: Plays important roles in virus replication,
CC virulence and host range. {ECO:0000269|PubMed:24352458,
CC ECO:0000269|PubMed:29536193}.
CC -!- FUNCTION: [Protein 3B-1]: Covalently linked to the 5'-end of both the
CC positive-strand and negative-strand genomic RNAs. Acts as a genome-
CC linked replication primer. {ECO:0000269|PubMed:15919922}.
CC -!- FUNCTION: [Protein 3B-2]: Covalently linked to the 5'-end of both the
CC positive-strand and negative-strand genomic RNAs. Acts as a genome-
CC linked replication primer. {ECO:0000269|PubMed:15919922}.
CC -!- FUNCTION: [Protein 3B-3]: Covalently linked to the 5'-end of both the
CC positive-strand and negative-strand genomic RNAs. Acts as a genome-
CC linked replication primer. {ECO:0000269|PubMed:15919922}.
CC -!- FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral
CC proteins from the precursor polyprotein. In addition to its proteolytic
CC activity, binds to viral RNA and thus influences viral genome
CC replication. RNA and substrate bind cooperatively to the protease.
CC {ECO:0000269|PubMed:3041041}.
CC -!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic and
CC antigenomic RNA by recognizing replications specific signals.
CC Covalently attaches UMP to a tyrosine of VPg, which is used to prime
CC RNA synthesis. The positive stranded RNA genome is first replicated at
CC virus induced membranous vesicles, creating a dsRNA genomic replication
CC form. This dsRNA is then used as template to synthesize positive
CC stranded RNA genomes. ss(+)RNA genomes are either translated,
CC replicated or encapsidated. {ECO:0000255|PROSITE-ProRule:PRU00539,
CC ECO:0000269|PubMed:15919922}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Autocatalytically cleaves itself from the polyprotein of the
CC foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but
CC then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-
CC Arg- and -Lys-|-Arg-.; EC=3.4.22.46;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
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=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: [Leader protease]: Interacts with host ISG15
CC (PubMed:29463763). {ECO:0000269|PubMed:29463763}.
CC -!- SUBUNIT: [Capsid protein VP1]: Interacts (via R-G-D motif) with host
CC ITGAV/ITGB6 (PubMed:28534487). Interacts with host MAVS; this
CC interaction inhibits binding of host TRAF3 to MAVS, thereby suppressing
CC interferon-mediated responses (PubMed:33232374).
CC {ECO:0000269|PubMed:28534487, ECO:0000269|PubMed:33232374}.
CC -!- SUBUNIT: [Protein 2B]: Forms homooligomers. {ECO:0000305}.
CC -!- SUBUNIT: [Protein 2C]: Interacts with host VIM (PubMed:23576498).
CC Interacts with host BECN1 (PubMed:22933281).
CC {ECO:0000269|PubMed:22933281, ECO:0000269|PubMed:23576498}.
CC -!- SUBUNIT: [Protein 3A]: Interacts with host DCTN3 (PubMed:24352458).
CC {ECO:0000269|PubMed:24352458}.
CC -!- SUBCELLULAR LOCATION: [Leader protease]: Host nucleus
CC {ECO:0000269|PubMed:17881445}. Host cytoplasm
CC {ECO:0000269|PubMed:17881445}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion
CC {ECO:0000269|PubMed:2537470}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
CC {ECO:0000269|PubMed:2537470}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC {ECO:0000269|PubMed:2537470}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein 2B]: Host endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:25946195}.
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 derived from
CC the endoplasmic reticulum (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasm
CC {ECO:0000269|PubMed:24352458, ECO:0000269|PubMed:29536193}. Host
CC endoplasmic reticulum membrane {ECO:0000269|PubMed:25275544}.
CC Note=Interacts with host endoplasmic reticulum membranes through its
CC hydrophobic stretch, while its N- and C-terminus face the cytosol being
CC accessible to other viral proteins for viral replication.
CC {ECO:0000269|PubMed:25275544}.
CC -!- SUBCELLULAR LOCATION: [Protein 3B-1]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein 3B-2]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein 3B-3]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase 3D-POL]: Host
CC cytoplasm {ECO:0000269|PubMed:23886493}. Host nucleus
CC {ECO:0000269|PubMed:23886493}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Lab;
CC IsoId=P03305-1; Sequence=Displayed;
CC Name=Lb;
CC IsoId=P03305-2; Sequence=VSP_018982;
CC -!- PTM: [Leader protease]: Removes six residues from its own C-terminus,
CC generating sLb(pro). {ECO:0000269|PubMed:25240326}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the
CC viral proteases yield a variety of precursors and mature proteins. The
CC polyprotein seems to be cotranslationally cleaved at the 2A/2B junction
CC by a ribosomal skip from one codon to the next without formation of a
CC peptide bond. This process would release the L-P1-2A peptide from the
CC translational complex. {ECO:0000269|PubMed:11297676}.
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:P03303}.
CC -!- PTM: [Capsid protein VP4]: Myristoylation is required during RNA
CC encapsidation and formation of the mature virus particle.
CC {ECO:0000250}.
CC -!- PTM: [Protein 3B-1]: Uridylylated by the polymerase and are covalently
CC linked to the 5'-end of genomic RNA. These uridylylated forms act as a
CC nucleotide-peptide primer for the polymerase.
CC {ECO:0000269|PubMed:15919922}.
CC -!- PTM: [Protein 3B-2]: Uridylylated by the polymerase and are covalently
CC linked to the 5'-end of genomic RNA. These uridylylated forms act as a
CC nucleotide-peptide primer for the polymerase.
CC {ECO:0000269|PubMed:15919922}.
CC -!- PTM: [Protein 3B-3]: Uridylylated by the polymerase and are covalently
CC linked to the 5'-end of genomic RNA. These uridylylated forms act as a
CC nucleotide-peptide primer for the polymerase.
CC {ECO:0000269|PubMed:15919922}.
CC -!- MISCELLANEOUS: [Capsid protein VP1]: Contains the main antigenic
CC determinants of the virion; therefore, changes in its sequence must be
CC responsible for the high antigenic variability of the virus.
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=1bbt";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1fod";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure complexed with oligosaccharide receptor;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1qqp";
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DR EMBL; X00871; CAA25416.1; -; Genomic_RNA.
DR EMBL; J02185; AAA42635.1; -; Genomic_RNA.
DR PDB; 1QMY; X-ray; 1.90 A; A/B/C=29-195.
DR PDB; 1QOL; X-ray; 3.00 A; A/B/C/D/E/F/G/H=29-201.
DR PDB; 1QQP; X-ray; 1.90 A; 1=725-937, 2=287-504, 3=505-724, 4=202-286.
DR PDB; 2JQF; NMR; -; R/S=29-201.
DR PDB; 2JQG; NMR; -; R=29-195.
DR PDB; 4QBB; X-ray; 1.60 A; A/B/C=29-195.
DR PDB; 6FFA; X-ray; 1.50 A; A=29-195.
DR PDBsum; 1QMY; -.
DR PDBsum; 1QOL; -.
DR PDBsum; 1QQP; -.
DR PDBsum; 2JQF; -.
DR PDBsum; 2JQG; -.
DR PDBsum; 4QBB; -.
DR PDBsum; 6FFA; -.
DR BMRB; P03305; -.
DR SMR; P03305; -.
DR ELM; P03305; -.
DR MEROPS; C03.008; -.
DR TCDB; 1.A.85.1.8; the poliovirus 2b viroporin (2b viroporin) family.
DR UniLectin; P03305; -.
DR PRIDE; P03305; -.
DR KEGG; ag:CAA25416; -.
DR BRENDA; 3.4.22.46; 2315.
DR EvolutionaryTrace; P03305; -.
DR Proteomes; UP000008765; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
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:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0019785; F:ISG15-specific peptidase activity; IDA:UniProtKB.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
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:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IDA:UniProtKB.
DR GO; GO:0039525; P:modulation by virus of host chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0039690; P:positive stranded viral RNA replication; ISS:UniProtKB.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR GO; GO:0039579; P:suppression by virus of host ISG15-protein conjugation; IDA:UniProtKB.
DR GO; GO:0039644; P:suppression by virus of host NF-kappaB cascade; IDA:UniProtKB.
DR GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; IDA:UniProtKB.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
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; -; 2.
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; IPR004080; FMDV_VP1_coat.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR008739; Peptidase_C28.
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; PF05408; Peptidase_C28; 1.
DR Pfam; PF00548; Peptidase_C3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00073; Rhv; 3.
DR Pfam; PF00910; RNA_helicase; 1.
DR Pfam; PF08935; VP4_2; 1.
DR PRINTS; PR00918; CALICVIRUSNS.
DR PRINTS; PR01542; FMDVP1COAT.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51887; APHTHOVIRUS_LPRO; 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; Alternative initiation; ATP-binding; Autocatalytic cleavage;
KW Capsid protein;
KW Clathrin- and caveolin-independent endocytosis of virus by host;
KW Clathrin-mediated endocytosis of virus by host;
KW Covalent protein-RNA linkage; Disulfide bond; Helicase; Host cytoplasm;
KW Host cytoplasmic vesicle; Host endoplasmic reticulum; Host membrane;
KW Host nucleus; Host-virus interaction; Hydrolase; Ion channel;
KW Ion transport; Lipoprotein; Membrane;
KW Modulation of host chromatin by virus; Myristate; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Protease; RNA-binding;
KW RNA-directed RNA polymerase; T=pseudo3 icosahedral capsid protein;
KW Thiol protease; Transferase; Translation regulation; Transport;
KW Viral attachment to host cell; Viral ion channel;
KW Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW Virus endocytosis by host; Virus entry into host cell.
FT CHAIN 1..2332
FT /note="Genome polyprotein"
FT /id="PRO_0000039872"
FT CHAIN 1..201
FT /note="Leader protease"
FT /id="PRO_0000039873"
FT CHAIN 202..504
FT /note="Capsid protein VP0"
FT /evidence="ECO:0000255"
FT /id="PRO_0000374076"
FT CHAIN 202..286
FT /note="Capsid protein VP4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039876"
FT CHAIN 287..504
FT /note="Capsid protein VP2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039877"
FT CHAIN 505..724
FT /note="Capsid protein VP3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039878"
FT CHAIN 725..935
FT /note="Capsid protein VP1"
FT /id="PRO_0000039879"
FT CHAIN 936..953
FT /note="Protein 2A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039880"
FT CHAIN 954..1107
FT /note="Protein 2B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000310976"
FT CHAIN 1108..1425
FT /note="Protein 2C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039881"
FT CHAIN 1426..1578
FT /note="Protein 3A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039882"
FT CHAIN 1579..1601
FT /note="Protein 3B-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039883"
FT CHAIN 1602..1625
FT /note="Protein 3B-2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000310977"
FT CHAIN 1626..1649
FT /note="Protein 3B-3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000310978"
FT CHAIN 1650..1862
FT /note="Protease 3C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039884"
FT CHAIN 1863..2332
FT /note="RNA-directed RNA polymerase 3D-POL"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039885"
FT TOPO_DOM 1..1480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1481..1501
FT /evidence="ECO:0000255"
FT TOPO_DOM 1502..2332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..201
FT /note="Peptidase C28"
FT DOMAIN 1189..1353
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1652..1848
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 2096..2214
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 197..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1529..1584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 869..871
FT /note="Cell attachment site"
FT /evidence="ECO:0000269|PubMed:2543752"
FT MOTIF 1879..1886
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:23886493"
FT COMPBIAS 203..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 51
FT /note="For leader protease activity"
FT ACT_SITE 148
FT /note="For leader protease activity"
FT ACT_SITE 163
FT /note="For leader protease activity"
FT ACT_SITE 1695
FT /note="For protease 3C activity; Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1733
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1812
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 2200
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT BINDING 1217..1224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 201..202
FT /note="Cleavage; by leader protease"
FT /evidence="ECO:0000255"
FT SITE 286..287
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 504..505
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000255"
FT SITE 724..725
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000255"
FT SITE 935..936
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000255"
FT SITE 953..954
FT /note="Cleavage; by ribosomal skip"
FT /evidence="ECO:0000255"
FT SITE 1107..1108
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000255"
FT SITE 1425..1426
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000255"
FT SITE 1578..1579
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000255"
FT SITE 1601..1602
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000255"
FT SITE 1625..1626
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000255"
FT SITE 1649..1650
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000255"
FT SITE 1862..1863
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000255"
FT MOD_RES 1581
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 1604
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 1628
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
FT LIPID 202
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT DISULFID 406..858
FT /note="Interchain (between VP2 and VP1 chains)"
FT DISULFID 511
FT /note="Interchain; in VP3 dimer"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform Lb)"
FT /evidence="ECO:0000305"
FT /id="VSP_018982"
FT VARIANT 780
FT /note="I -> V (in strain: Isolate O1BFS)"
FT VARIANT 808
FT /note="G -> R (in strain: Isolate O1BFS)"
FT VARIANT 861
FT /note="N -> S (in strain: Isolate O1BFS)"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:6FFA"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:6FFA"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6FFA"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:6FFA"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1QOL"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:6FFA"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2JQG"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:6FFA"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:6FFA"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:6FFA"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2JQF"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:6FFA"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:6FFA"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2JQG"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:6FFA"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:6FFA"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:6FFA"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:6FFA"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:6FFA"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:6FFA"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:6FFA"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:6FFA"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:1QOL"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:1QQP"
FT HELIX 268..274
FT /evidence="ECO:0007829|PDB:1QQP"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:1QQP"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:1QQP"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:1QQP"
FT HELIX 376..383
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 384..397
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 404..413
FT /evidence="ECO:0007829|PDB:1QQP"
FT HELIX 421..428
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 429..434
FT /evidence="ECO:0007829|PDB:1QQP"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 440..446
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:1QQP"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 463..474
FT /evidence="ECO:0007829|PDB:1QQP"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 483..499
FT /evidence="ECO:0007829|PDB:1QQP"
FT HELIX 548..554
FT /evidence="ECO:0007829|PDB:1QQP"
FT TURN 562..564
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 565..569
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 577..583
FT /evidence="ECO:0007829|PDB:1QQP"
FT HELIX 588..590
FT /evidence="ECO:0007829|PDB:1QQP"
FT HELIX 594..599
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 602..607
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 609..615
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 622..630
FT /evidence="ECO:0007829|PDB:1QQP"
FT HELIX 640..643
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 646..652
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 658..663
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 672..675
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 687..697
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 702..709
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 714..718
FT /evidence="ECO:0007829|PDB:1QQP"
FT HELIX 739..742
FT /evidence="ECO:0007829|PDB:1QQP"
FT HELIX 752..754
FT /evidence="ECO:0007829|PDB:1QQP"
FT HELIX 756..760
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 762..766
FT /evidence="ECO:0007829|PDB:1QQP"
FT HELIX 777..779
FT /evidence="ECO:0007829|PDB:1QQP"
FT HELIX 785..791
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 793..808
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 810..813
FT /evidence="ECO:0007829|PDB:1QQP"
FT HELIX 819..823
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 827..830
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 837..841
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 846..852
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 891..893
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 895..912
FT /evidence="ECO:0007829|PDB:1QQP"
FT STRAND 921..924
FT /evidence="ECO:0007829|PDB:1QQP"
SQ SEQUENCE 2332 AA; 258927 MW; 4A83176F43447D68 CRC64;
MNTTDCFIAL VQAIREIKAL FLSRTTGKME LTLYNGEKKT FYSRPNNHDN CWLNAILQLF
RYVEEPFFDW VYSSPENLTL EAIKQLEDLT GLELHEGGPP ALVIWNIKHL LHTGIGTASR
PSEVCMVDGT DMCLADFHAG IFLKGQEHAV FACVTSNGWY AIDDEDFYPW TPDPSDVLVF
VPYDQEPLNG EWKAKVQRKL KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG
DNAISGGSNE GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI
LTTRNGHTTS TTQSSVGVTY GYATAEDFVS GPNTSGLETR VVQAERFFKT HLFDWVTSDS
FGRCHLLELP TDHKGVYGSL TDSYAYMRNG WDVEVTAVGN QFNGGCLLVA MVPELYSIQK
RELYQLTLFP HQFINPRTNM TAHITVPFVG VNRYDQYKVH KPWTLVVMVV APLTVNTEGA
PQIKVYANIA PTNVHVAGEF PSKEGIFPVA CSDGYGGLVT TDPKTADPVY GKVFNPPRNQ
LPGRFTNLLD VAEACPTFLR FEGGVPYVTT KTDSDRVLAQ FDMSLAAKQM SNTFLAGLAQ
YYTQYSGTIN LHFMFTGPTD AKARYMVAYA PPGMEPPKTP EAAAHCIHAE WDTGLNSKFT
FSIPYLSAAD YAYTASGVAE TTNVQGWVCL FQITHGKADG DALVVLASAG KDFELRLPVD
ARAETTSAGE SADPVTTTVE NYGGETQIQR RQHTDVSFIM DRFVKVTPQN QINILDLMQI
PSHTLVGALL RASTYYFSDL EIAVKHEGDL TWVPNGAPEK ALDNTTNPTA YHKAPLTRLA
LPYTAPHRVL ATVYNGECRY NRNAVPNLRG DLQVLAQKVA RTLPTSFNYG AIKATRVTEL
LYRMKRAETY CPRPLLAIHP TEARHKQKIV APVKQTLNFD LLKLAGDVES NPGPFFFSDV
RSNFSKLVET INQMQEDMST KHGPDFNRLV SAFEELAIGV KAIRTGLDEA KPWYKLIKLL
SRLSCMAAVA ARSKDPVLVA IMLADTGLEI LDSTFVVKKI SDSLSSLFHV PAPVFSFGAP
VLLAGLVKVA SSFFRSTPED LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW
IASEEKFVTM TDLVPGILEK QRDLNDPSKY KEAKEWLDNA RQACLKSGNV HIANLCKVVA
PAPSKSRPEP VVVCLRGKSG QGKSFLANVL AQAISTHFTG RIDSVWYCPP DPDHFDGYNQ
QTVVVMDDLG QNPDGKDFKY FAQMVSTTGF IPPMASLEDK GKPFNSKVII ATTNLYSGFT
PRTMVCPDAL NRRFHFDIDV SAKDGYKINS KLDIIKALED THANPVAMFQ YDCALLNGMA
VEMKRMQQDM FKPQPPLQNV YQLVQEVIDR VELHEKVSSH PIFKQISIPS QKSVLYFLIE
KGQHEAAIEF FEGMVHDSIK EELRPLIQQT SFVKRAFKRL KENFEIVALC LTLLANIVIM
IRETRKRQKM VDDAVNEYIE KANITTDDKT LDEAEKSPLE TSGASTVGFR ERTLPGQKAC
DDVNSEPAQP VEEQPQAEGP YAGPLERQKP LKVRAKLPQQ EGPYAGPMER QKPLKVKAKA
PVVKEGPYEG PVKKPVALKV KAKNLIVTES GAPPTDLQKM VMGNTKPVEL ILDGKTVAIC
CATGVFGTAY LVPRHLFAEK YDKIMVDGRA MTDSDYRVFE FEIKVKGQDM LSDAALMVLH
RGNRVRDITK HFRDTARMKK GTPVVGVINN ADVGRLIFSG EALTYKDIVV CMDGDTMPGL
FAYRAATKAG YCGGAVLAKD GADTFIVGTH SAGGNGVGYC SCVSRSMLLK MKAHIDPEPH
HEGLIVDTRD VEERVHVMRK TKLAPTVAHG VFNPEFGPAA LSNKDPRLNE GVVLDEVIFS
KHKGDTKMSE EDKALFRRCA ADYASRLHSV LGTANAPLSI YEAIKGVDGL DAMEPDTAPG
LPWALQGKRR GALIDFENGT VGPEVEAALK LMEKREYKFV CQTFLKDEIR PLEKVRAGKT
RIVDVLPVEH ILYTRMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD
VDYSAFDANH CSDAMNIMFE EVFRTEFGFH PNAEWILKTL VNTEHAYENK RITVGGGMPS
GCSATSIINT ILNNIYVLYA LRRHYEGVEL DTYTMISYGD DIVVASDYDL DFEALKPHFK
SLGQTITPAD KSDKGFVLGH SITDVTFLKR HFHMDYGTGF YKPVMASKTL EAILSFARRG
TIQEKLISVA GLAVHSGPDE YRRLFEPFQG LFEIPSYRSL YLRWVNAVCG DA
