ID   POLG_POL1M              Reviewed;        2209 AA.
AC   P03300; A0A142KD04; P03299; Q84879; Q84880; Q89679;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 232.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=P1;
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=P2;
DE   Contains:
DE     RecName: Full=Protease 2A;
DE              Short=P2A;
DE              EC=3.4.22.29 {ECO:0000269|PubMed:1649327};
DE     AltName: Full=Picornain 2A;
DE     AltName: Full=Protein 2A;
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 {ECO:0000269|PubMed:19520852, ECO:0000269|PubMed:30231078, ECO:0000269|PubMed:7730315, ECO:0000269|PubMed:8385138};
DE   Contains:
DE     RecName: Full=P3;
DE   Contains:
DE     RecName: Full=Protein 3AB;
DE   Contains:
DE     RecName: Full=Protein 3A;
DE              Short=P3A;
DE   Contains:
DE     RecName: Full=Viral protein genome-linked;
DE              Short=VPg;
DE     AltName: Full=Protein 3B;
DE              Short=P3B;
DE   Contains:
DE     RecName: Full=Protein 3CD;
DE              EC=3.4.22.28;
DE   Contains:
DE     RecName: Full=Protease 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE              EC=3.4.22.28 {ECO:0000255|PROSITE-ProRule:PRU01222, ECO:0000269|PubMed:8097606};
DE     AltName: Full=Picornain 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE              Short=P3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase {ECO:0000255|PROSITE-ProRule:PRU00539};
DE              Short=RdRp;
DE              EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE     AltName: Full=3D polymerase;
DE              Short=3Dpol;
DE     AltName: Full=Protein 3D;
DE              Short=3D;
OS   Poliovirus type 1 (strain Mahoney).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Ensavirinae; Enterovirus; Enterovirus C.
OX   NCBI_TaxID=12081;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6264310; DOI=10.1038/291547a0;
RA   Kitamura N., Semler B.L., Rothberg P.G., Larsen G.R., Adler C.J.,
RA   Dorner A.J., Emini E.A., Hanecak R., Lee J.J., van der Werf S.,
RA   Anderson C.W., Wimmer E.;
RT   "Primary structure, gene organization and polypeptide expression of
RT   poliovirus RNA.";
RL   Nature 291:547-553(1981).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6272282; DOI=10.1073/pnas.78.8.4887;
RA   Racaniello V.R., Baltimore D.;
RT   "Molecular cloning of poliovirus cDNA and determination of the complete
RT   nucleotide sequence of the viral genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 78:4887-4891(1981).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 2-69.
RX   PubMed=6284987; DOI=10.1128/jvi.42.3.1017-1028.1982;
RA   Dorner A.J., Dorner L.F., Larsen G.R., Wimmer E., Anderson C.W.;
RT   "Identification of the initiation site of poliovirus polyprotein
RT   synthesis.";
RL   J. Virol. 42:1017-1028(1982).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1539-1574, AND FUNCTION (VIRAL PROTEIN
RP   GENOME-LINKED).
RX   PubMed=6250717; DOI=10.1016/0092-8674(80)90137-3;
RA   Kitamura N., Adler C.J., Rothberg P.G., Martinko J., Nathenson S.G.,
RA   Wimmer E.;
RT   "The genome-linked protein of picornaviruses. VII. Genetic mapping of
RT   poliovirus VPg by protein and RNA sequence studies.";
RL   Cell 21:295-302(1980).
RN   [6]
RP   SUBCELLULAR LOCATION (VIRAL PROTEIN GENOME-LINKED).
RX   PubMed=202952; DOI=10.1073/pnas.74.12.5345;
RA   Nomoto A., Kitamura N., Golini F., Wimmer E.;
RT   "The 5'-terminal structures of poliovirion RNA and poliovirus mRNA differ
RT   only in the genome-linked protein VPg.";
RL   Proc. Natl. Acad. Sci. U.S.A. 74:5345-5349(1977).
RN   [7]
RP   FUNCTION (VIRAL PROTEIN GENOME-LINKED), AND COVALENT RNA LINKAGE AT
RP   TYR-1546 (VIRAL PROTEIN GENOME-LINKED).
RX   PubMed=209034; DOI=10.1016/s0021-9258(17)30361-7;
RA   Ambros V., Baltimore D.;
RT   "Protein is linked to the 5' end of poliovirus RNA by a phosphodiester
RT   linkage to tyrosine.";
RL   J. Biol. Chem. 253:5263-5266(1978).
RN   [8]
RP   FUNCTION (RNA-DIRECTED RNA POLYMERASE).
RX   PubMed=2535728; DOI=10.1128/jvi.63.1.216-225.1989;
RA   Plotch S.J., Palant O., Gluzman Y.;
RT   "Purification and properties of poliovirus RNA polymerase expressed in
RT   Escherichia coli.";
RL   J. Virol. 63:216-225(1989).
RN   [9]
RP   ACTIVE SITE (RNA-DIRECTED RNA POLYMERASE).
RX   PubMed=2196557; DOI=10.1093/protein/3.6.461;
RA   Delarue M., Poch O., Tordo N., Moras D., Argos P.;
RT   "An attempt to unify the structure of polymerases.";
RL   Protein Eng. 3:461-467(1990).
RN   [10]
RP   MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF ALA-3.
RX   PubMed=1850017; DOI=10.1128/jvi.65.5.2372-2380.1991;
RA   Moscufo N., Simons J., Chow M.;
RT   "Myristoylation is important at multiple stages in poliovirus assembly.";
RL   J. Virol. 65:2372-2380(1991).
RN   [11]
RP   CATALYTIC ACTIVITY (PROTEASE 2A), FUNCTION (PROTEASE 2A), MUTAGENESIS OF
RP   HIS-901; ASP-919; CYS-990; HIS-997 AND HIS-998, AND ACTIVE SITE (PROTEASE
RP   2A).
RX   PubMed=1649327; DOI=10.1128/jvi.65.8.4226-4231.1991;
RA   Hellen C.U., Faecke M., Kraeusslich H.G., Lee C.K., Wimmer E.;
RT   "Characterization of poliovirus 2A proteinase by mutational analysis:
RT   residues required for autocatalytic activity are essential for induction of
RT   cleavage of eukaryotic initiation factor 4F polypeptide p220.";
RL   J. Virol. 65:4226-4231(1991).
RN   [12]
RP   FUNCTION (CAPSID PROTEIN VP0), MYRISTOYLATION AT GLY-2, MUTAGENESIS OF
RP   GLY-2, SUBCELLULAR LOCATION (CAPSID PROTEIN VP1), SUBCELLULAR LOCATION
RP   (CAPSID PROTEIN VP2), AND SUBCELLULAR LOCATION (CAPSID PROTEIN VP3).
RX   PubMed=1851815; DOI=10.1099/0022-1317-72-5-1151;
RA   Marc D., Girard M., van der Werf S.;
RT   "A Gly1 to Ala substitution in poliovirus capsid protein VP0 blocks its
RT   myristoylation and prevents viral assembly.";
RL   J. Gen. Virol. 72:1151-1157(1991).
RN   [13]
RP   FUNCTION (PROTEIN 3CD).
RX   PubMed=1331532; DOI=10.1128/jvi.66.12.7481-7489.1992;
RA   Harris K.S., Reddigari S.R., Nicklin M.J., Haemmerle T., Wimmer E.;
RT   "Purification and characterization of poliovirus polypeptide 3CD, a
RT   proteinase and a precursor for RNA polymerase.";
RL   J. Virol. 66:7481-7489(1992).
RN   [14]
RP   MUTAGENESIS OF CYS-936; CYS-938; CYS-945; CYS-996 AND HIS-998.
RX   PubMed=1310193; DOI=10.1016/0042-6822(92)90039-r;
RA   Yu S.F., Lloyd R.E.;
RT   "Characterization of the roles of conserved cysteine and histidine residues
RT   in poliovirus 2A protease.";
RL   Virology 186:725-735(1992).
RN   [15]
RP   FUNCTION (PROTEIN 2C), SUBUNIT (PROTEIN 2C), AND CATALYTIC ACTIVITY
RP   (PROTEIN 2C).
RX   PubMed=8385138; DOI=10.1016/s0021-9258(18)53068-4;
RA   Rodriguez P.L., Carrasco L.;
RT   "Poliovirus protein 2C has ATPase and GTPase activities.";
RL   J. Biol. Chem. 268:8105-8110(1993).
RN   [16]
RP   FUNCTION (PROTEASE 3C), PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN),
RP   CATALYTIC ACTIVITY (PROTEASE 3C), ACTIVE SITE (PROTEASE 3C), AND
RP   MUTAGENESIS OF GLU-1636 AND CYS-1712.
RX   PubMed=8097606; DOI=10.1006/viro.1993.1268;
RA   Kean K.M., Howell M.T., Gruenert S., Girard M., Jackson R.J.;
RT   "Substitution mutations at the putative catalytic triad of the poliovirus
RT   3C protease have differential effects on cleavage at different sites.";
RL   Virology 194:360-364(1993).
RN   [17]
RP   INTERACTION WITH PROTEIN 3CD (PROTEIN 3AB), AND INTERACTION WITH PROTEIN
RP   3AB (PROTEIN 3CD).
RX   PubMed=7929441; DOI=10.1016/s0021-9258(18)47118-9;
RA   Harris K.S., Xiang W., Alexander L., Lane W.S., Paul A.V., Wimmer E.;
RT   "Interaction of poliovirus polypeptide 3CDpro with the 5' and 3' termini of
RT   the poliovirus genome. Identification of viral and cellular cofactors
RT   needed for efficient binding.";
RL   J. Biol. Chem. 269:27004-27014(1994).
RN   [18]
RP   RNA-BINDING (PROTEIN 2C), DOMAIN (PROTEIN 2C), CATALYTIC ACTIVITY (PROTEIN
RP   2C), AND FUNCTION (PROTEIN 2C).
RX   PubMed=7730315; DOI=10.1074/jbc.270.17.10105;
RA   Rodriguez P.L., Carrasco L.;
RT   "Poliovirus protein 2C contains two regions involved in RNA binding
RT   activity.";
RL   J. Biol. Chem. 270:10105-10112(1995).
RN   [19]
RP   FUNCTION (PROTEIN 2B).
RX   PubMed=9151862; DOI=10.1128/jvi.71.6.4679-4693.1997;
RA   Sandoval I.V., Carrasco L.;
RT   "Poliovirus infection and expression of the poliovirus protein 2B provoke
RT   the disassembly of the Golgi complex, the organelle target for the
RT   antipoliovirus drug Ro-090179.";
RL   J. Virol. 71:4679-4693(1997).
RN   [20]
RP   FUNCTION (PROTEASE 2A).
RX   PubMed=9755863; DOI=10.1016/s0014-5793(98)01027-8;
RA   Ventoso I., MacMillan S.E., Hershey J.W., Carrasco L.;
RT   "Poliovirus 2A proteinase cleaves directly the eIF-4G subunit of eIF-4F
RT   complex.";
RL   FEBS Lett. 435:79-83(1998).
RN   [21]
RP   DOMAIN (PROTEIN 2C).
RX   PubMed=9696129; DOI=10.1016/s0168-1702(98)00016-1;
RA   Echeverri A., Banerjee R., Dasgupta A.;
RT   "Amino-terminal region of poliovirus 2C protein is sufficient for membrane
RT   binding.";
RL   Virus Res. 54:217-223(1998).
RN   [22]
RP   MUTAGENESIS OF HIS-264, AND PROTEOLYTIC CLEAVAGE (CAPSID PROTEIN VP0).
RX   PubMed=10516013; DOI=10.1128/jvi.73.11.9072-9079.1999;
RA   Hindiyeh M., Li Q.H., Basavappa R., Hogle J.M., Chow M.;
RT   "Poliovirus mutants at histidine 195 of VP2 do not cleave VP0 into VP2 and
RT   VP4.";
RL   J. Virol. 73:9072-9079(1999).
RN   [23]
RP   FUNCTION (PROTEIN 3CD).
RX   PubMed=10666252; DOI=10.1128/jvi.74.5.2219-2226.2000;
RA   Gamarnik A.V., Andino R.;
RT   "Interactions of viral protein 3CD and poly(rC) binding protein with the 5'
RT   untranslated region of the poliovirus genome.";
RL   J. Virol. 74:2219-2226(2000).
RN   [24]
RP   FUNCTION (VIRAL PROTEIN GENOME-LINKED), COVALENT RNA-LINKAGE AT TYR-1546
RP   (VIRAL PROTEIN GENOME-LINKED), AND URIDYLYLATION AT TYR-1546.
RX   PubMed=12502805; DOI=10.1128/jvi.77.2.891-904.2003;
RA   Paul A.V., Peters J., Mugavero J., Yin J., van Boom J.H., Wimmer E.;
RT   "Biochemical and genetic studies of the VPg uridylylation reaction
RT   catalyzed by the RNA polymerase of poliovirus.";
RL   J. Virol. 77:891-904(2003).
RN   [25]
RP   SUBUNIT (PROTEIN 3A).
RX   PubMed=12823963; DOI=10.1016/s0022-2836(03)00577-1;
RA   Strauss D.M., Glustrom L.W., Wuttke D.S.;
RT   "Towards an understanding of the poliovirus replication complex: the
RT   solution structure of the soluble domain of the poliovirus 3A protein.";
RL   J. Mol. Biol. 330:225-234(2003).
RN   [26]
RP   SUBCELLULAR LOCATION (PROTEIN 3CD).
RX   PubMed=15016543; DOI=10.1016/j.virol.2003.10.020;
RA   Sharma R., Raychaudhuri S., Dasgupta A.;
RT   "Nuclear entry of poliovirus protease-polymerase precursor 3CD:
RT   implications for host cell transcription shut-off.";
RL   Virology 320:195-205(2004).
RN   [27]
RP   SUBUNIT (PROTEIN 3A), AND CAUTION.
RX   PubMed=16138011; DOI=10.4161/cc.4.10.2041;
RA   Kondratova A.A., Neznanov N., Kondratov R.V., Gudkov A.V.;
RT   "Poliovirus protein 3A binds and inactivates LIS1, causing block of
RT   membrane protein trafficking and deregulation of cell division.";
RL   Cell Cycle 4:1403-1410(2005).
RN   [28]
RP   FUNCTION (PROTEIN 3A).
RX   PubMed=15914217; DOI=10.1016/j.virol.2005.03.036;
RA   Choe S.S., Dodd D.A., Kirkegaard K.;
RT   "Inhibition of cellular protein secretion by picornaviral 3A proteins.";
RL   Virology 337:18-29(2005).
RN   [29]
RP   ACTIVITY REGULATION (RNA-DIRECTED RNA POLYMERASE).
RX   PubMed=15649563; DOI=10.1016/j.virusres.2004.11.007;
RA   Vignuzzi M., Stone J.K., Andino R.;
RT   "Ribavirin and lethal mutagenesis of poliovirus: molecular mechanisms,
RT   resistance and biological implications.";
RL   Virus Res. 107:173-181(2005).
RN   [30]
RP   FUNCTION (VIRAL PROTEIN GENOME-LINKED), COVALENT RNA-LINKAGE AT TYR-1546
RP   (VIRAL PROTEIN GENOME-LINKED), AND URIDYLYLATION AT TYR-1546.
RX   PubMed=16840321; DOI=10.1128/jvi.02533-05;
RA   Richards O.C., Spagnolo J.F., Lyle J.M., Vleck S.E., Kuchta R.D.,
RA   Kirkegaard K.;
RT   "Intramolecular and intermolecular uridylylation by poliovirus RNA-
RT   dependent RNA polymerase.";
RL   J. Virol. 80:7405-7415(2006).
RN   [31]
RP   INTERACTION WITH HOST GBF1 (PROTEIN 3A).
RX   PubMed=17005635; DOI=10.1128/jvi.01225-06;
RA   Wessels E., Duijsings D., Lanke K.H., van Dooren S.H., Jackson C.L.,
RA   Melchers W.J., van Kuppeveld F.J.;
RT   "Effects of picornavirus 3A Proteins on Protein Transport and GBF1-
RT   dependent COP-I recruitment.";
RL   J. Virol. 80:11852-11860(2006).
RN   [32]
RP   INTERACTION WITH HOST RTN3 (PROTEIN 2C).
RX   PubMed=17182608; DOI=10.1074/jbc.m611145200;
RA   Tang W.-F., Yang S.-Y., Wu B.-W., Jheng J.-R., Chen Y.-L., Shih C.-H.,
RA   Lin K.-H., Lai H.-C., Tang P., Horng J.-T.;
RT   "Reticulon 3 binds the 2C protein of enterovirus 71 and is required for
RT   viral replication.";
RL   J. Biol. Chem. 282:5888-5898(2007).
RN   [33]
RP   FUNCTION (PROTEIN 3A).
RX   PubMed=17079330; DOI=10.1128/jvi.01820-06;
RA   Belov G.A., Altan-Bonnet N., Kovtunovych G., Jackson C.L.,
RA   Lippincott-Schwartz J., Ehrenfeld E.;
RT   "Hijacking components of the cellular secretory pathway for replication of
RT   poliovirus RNA.";
RL   J. Virol. 81:558-567(2007).
RN   [34]
RP   FUNCTION (PROTEASE 3C).
RX   PubMed=18005751; DOI=10.1016/j.chom.2007.08.006;
RA   White J.P., Cardenas A.M., Marissen W.E., Lloyd R.E.;
RT   "Inhibition of cytoplasmic mRNA stress granule formation by a viral
RT   proteinase.";
RL   Cell Host Microbe 2:295-305(2007).
RN   [35]
RP   FUNCTION (CAPSID PROTEIN VP1).
RX   PubMed=17622193; DOI=10.1371/journal.pbio.0050183;
RA   Brandenburg B., Lee L.Y., Lakadamyali M., Rust M.J., Zhuang X., Hogle J.M.;
RT   "Imaging poliovirus entry in live cells.";
RL   PLoS Biol. 5:E183-E183(2007).
RN   [36]
RP   FUNCTION (CAPSID PROTEIN VP1).
RC   STRAIN=Sabin 2;
RX   PubMed=17717529; DOI=10.1038/sj.emboj.7601831;
RA   Coyne C.B., Kim K.S., Bergelson J.M.;
RT   "Poliovirus entry into human brain microvascular cells requires receptor-
RT   induced activation of SHP-2.";
RL   EMBO J. 26:4016-4028(2007).
RN   [37]
RP   INTERACTION WITH RNA-DIRECTED RNA POLYMERASE (PROTEIN 3B), AND INTERACTION
RP   WITH PROTEIN 3B (RNA-DIRECTED RNA POLYMERASE).
RX   PubMed=17409142; DOI=10.1128/jvi.02252-06;
RA   Strauss D.M., Wuttke D.S.;
RT   "Characterization of protein-protein interactions critical for poliovirus
RT   replication: analysis of 3AB and VPg binding to the RNA-dependent RNA
RT   polymerase.";
RL   J. Virol. 81:6369-6378(2007).
RN   [38]
RP   TOPOLOGY (PROTEIN 3A), AND TOPOLOGY (PROTEIN 3AB).
RX   PubMed=17417822; DOI=10.1021/bi6024758;
RA   Fujita K., Krishnakumar S.S., Franco D., Paul A.V., London E., Wimmer E.;
RT   "Membrane topography of the hydrophobic anchor sequence of poliovirus 3A
RT   and 3AB proteins and the functional effect of 3A/3AB membrane association
RT   upon RNA replication.";
RL   Biochemistry 46:5185-5199(2007).
RN   [39]
RP   FUNCTION (PROTEASE 3C).
RX   PubMed=18632855; DOI=10.1128/jvi.00006-08;
RA   Bonderoff J.M., Larey J.L., Lloyd R.E.;
RT   "Cleavage of poly(A)-binding protein by poliovirus 3C proteinase inhibits
RT   viral internal ribosome entry site-mediated translation.";
RL   J. Virol. 82:9389-9399(2008).
RN   [40]
RP   FUNCTION (PROTEASE 3C).
RX   PubMed=18572216; DOI=10.1016/j.virol.2008.05.019;
RA   de Breyne S., Bonderoff J.M., Chumakov K.M., Lloyd R.E., Hellen C.U.;
RT   "Cleavage of eukaryotic initiation factor eIF5B by enterovirus 3C
RT   proteases.";
RL   Virology 378:118-122(2008).
RN   [41]
RP   FUNCTION (CAPSID PROTEIN VP1), FUNCTION (CAPSID PROTEIN VP2), AND FUNCTION
RP   (CAPSID PROTEIN VP3).
RX   PubMed=18191571; DOI=10.1016/j.tim.2007.12.004;
RA   Bergelson J.M.;
RT   "New (fluorescent) light on poliovirus entry.";
RL   Trends Microbiol. 16:44-47(2008).
RN   [42]
RP   REVIEW (PROTEIN 2B).
RX   PubMed=18216106; DOI=10.1128/jvi.02076-07;
RA   de Jong A.S., de Mattia F., Van Dommelen M.M., Lanke K., Melchers W.J.,
RA   Willems P.H., van Kuppeveld F.J.;
RT   "Functional analysis of picornavirus 2B proteins: effects on calcium
RT   homeostasis and intracellular protein trafficking.";
RL   J. Virol. 82:3782-3790(2008).
RN   [43]
RP   FUNCTION (PROTEASE 3C).
RX   PubMed=17993457; DOI=10.1074/jbc.m707907200;
RA   Shen M., Reitman Z.J., Zhao Y., Moustafa I., Wang Q., Arnold J.J.,
RA   Pathak H.B., Cameron C.E.;
RT   "Picornavirus genome replication. Identification of the surface of the
RT   poliovirus (PV) 3C dimer that interacts with PV 3Dpol during VPg
RT   uridylylation and construction of a structural model for the PV 3C2-3Dpol
RT   complex.";
RL   J. Biol. Chem. 283:875-888(2008).
RN   [44]
RP   FUNCTION (PROTEIN 2A).
RX   PubMed=19789179; DOI=10.1242/jcs.055988;
RA   Castello A., Izquierdo J.M., Welnowska E., Carrasco L.;
RT   "RNA nuclear export is blocked by poliovirus 2A protease and is concomitant
RT   with nucleoporin cleavage.";
RL   J. Cell Sci. 122:3799-3809(2009).
RN   [45]
RP   FUNCTION (PROTEIN 2C), CATALYTIC ACTIVITY (PROTEIN 2C), SUBUNIT (PROTEIN
RP   2C), AND DOMAIN (PROTEIN 2C).
RX   PubMed=19520852; DOI=10.1074/jbc.m109.031807;
RA   Adams P., Kandiah E., Effantin G., Steven A.C., Ehrenfeld E.;
RT   "Poliovirus 2C protein forms homo-oligomeric structures required for ATPase
RT   activity.";
RL   J. Biol. Chem. 284:22012-22021(2009).
RN   [46]
RP   REVIEW (RNA-DIRECTED RNA POLYMERASE).
RX   PubMed=18487072; DOI=10.1016/j.biocel.2008.03.019;
RA   Kok C.C., McMinn P.C.;
RT   "Picornavirus RNA-dependent RNA polymerase.";
RL   Int. J. Biochem. Cell Biol. 41:498-502(2009).
RN   [47]
RP   INTERACTION WITH PROTEIN 2C (CAPSID PROTEIN VP3), FUNCTION (CAPSID PROTEIN
RP   VP3), AND INTERACTION WITH CAPSID PROTEIN VP3 (PROTEIN 2C).
RX   PubMed=20865167; DOI=10.1371/journal.ppat.1001066;
RA   Liu Y., Wang C., Mueller S., Paul A.V., Wimmer E., Jiang P.;
RT   "Direct interaction between two viral proteins, the nonstructural protein
RT   2C and the capsid protein VP3, is required for enterovirus morphogenesis.";
RL   PLoS Pathog. 6:E1001066-E1001066(2010).
RN   [48]
RP   FUNCTION (VIRAL PROTEIN GENOME-LINKED).
RX   PubMed=20441784; DOI=10.1016/j.peptides.2010.04.021;
RA   Schein C.H., Oezguen N., van der Heden van Noort G.J., Filippov D.V.,
RA   Paul A., Kumar E., Braun W.;
RT   "NMR solution structure of poliovirus uridylyated peptide linked to the
RT   genome (VPgpU).";
RL   Peptides 31:1441-1448(2010).
RN   [49]
RP   FUNCTION (PROTEIN 3AB).
RX   PubMed=21045553; DOI=10.4161/rna.7.6.13781;
RA   Gangaramani D.R., Eden E.L., Shah M., Destefano J.J.;
RT   "The twenty-nine amino acid C-terminal cytoplasmic domain of poliovirus 3AB
RT   is critical for nucleic acid chaperone activity.";
RL   RNA Biol. 7:820-829(2010).
RN   [50]
RP   TOPOLOGY (PROTEIN 2B), AND FUNCTION (PROTEIN 2B).
RX   PubMed=21835803; DOI=10.1128/jvi.05421-11;
RA   Martinez-Gil L., Bano-Polo M., Redondo N., Sanchez-Martinez S., Nieva J.L.,
RA   Carrasco L., Mingarro I.;
RT   "Membrane integration of poliovirus 2B viroporin.";
RL   J. Virol. 85:11315-11324(2011).
RN   [51]
RP   INTERACTION WITH HOST GBF1 (PROTEIN 3A).
RX   PubMed=21345960; DOI=10.1128/jvi.02398-10;
RA   Teterina N.L., Pinto Y., Weaver J.D., Jensen K.S., Ehrenfeld E.;
RT   "Analysis of poliovirus protein 3A interactions with viral and cellular
RT   proteins in infected cells.";
RL   J. Virol. 85:4284-4296(2011).
RN   [52]
RP   FUNCTION (VIRAL PROTEIN GENOME-LINKED).
RX   PubMed=22908287; DOI=10.1073/pnas.1208096109;
RA   Virgen-Slane R., Rozovics J.M., Fitzgerald K.D., Ngo T., Chou W.,
RA   van der Heden van Noort G.J., Filippov D.V., Gershon P.D., Semler B.L.;
RT   "An RNA virus hijacks an incognito function of a DNA repair enzyme.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:14634-14639(2012).
RN   [53]
RP   FUNCTION (PROTEIN 2C).
RX   PubMed=22761387; DOI=10.1128/jvi.00914-12;
RA   Wang C., Jiang P., Sand C., Paul A.V., Wimmer E.;
RT   "Alanine scanning of poliovirus 2CATPase reveals new genetic evidence that
RT   capsid protein/2CATPase interactions are essential for morphogenesis.";
RL   J. Virol. 86:9964-9975(2012).
RN   [54]
RP   INTERACTION WITH HOST ACBD3 (PROTEIN 3A).
RX   PubMed=22258260; DOI=10.1128/jvi.06778-11;
RA   Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., Derisi J.L.;
RT   "The 3A protein from multiple picornaviruses utilizes the golgi adaptor
RT   protein ACBD3 to recruit PI4KIIIbeta.";
RL   J. Virol. 86:3605-3616(2012).
RN   [55]
RP   CHARACTERIZATION OF N-TERMINUS (CAPSID PROTEIN VP1).
RX   PubMed=23085162; DOI=10.1016/j.jmgm.2012.06.009;
RA   Roberts J.A., Kuiper M.J., Thorley B.R., Smooker P.M., Hung A.;
RT   "Investigation of a predicted N-terminal amphipathic alpha-helix using
RT   atomistic molecular dynamics simulation of a complete prototype poliovirus
RT   virion.";
RL   J. Mol. Graph. Model. 38:165-173(2012).
RN   [56]
RP   FUNCTION (CAPSID PROTEIN VP1), AND FUNCTION (CAPSID PROTEIN VP4).
RX   PubMed=23365424; DOI=10.1128/jvi.03209-12;
RA   Strauss M., Levy H.C., Bostina M., Filman D.J., Hogle J.M.;
RT   "RNA transfer from poliovirus 135S particles across membranes is mediated
RT   by long umbilical connectors.";
RL   J. Virol. 87:3903-3914(2013).
RN   [57]
RP   MULTIMERIZATION (RNA-DIRECTED RNA POLYMERASE).
RX   PubMed=23583774; DOI=10.1016/j.jmb.2013.04.007;
RA   Wang J., Lyle J.M., Bullitt E.;
RT   "Surface for catalysis by poliovirus RNA-dependent RNA polymerase.";
RL   J. Mol. Biol. 425:2529-2540(2013).
RN   [58]
RP   FUNCTION (PROTEASE 2A), AND FUNCTION (PROTEASE 3C).
RX   PubMed=24390337; DOI=10.1128/jvi.02712-13;
RA   Feng Q., Langereis M.A., Lork M., Nguyen M., Hato S.V., Lanke K., Emdad L.,
RA   Bhoopathi P., Fisher P.B., Lloyd R.E., van Kuppeveld F.J.;
RT   "Enterovirus 2Apro targets MDA5 and MAVS in infected cells.";
RL   J. Virol. 88:3369-3378(2014).
RN   [59]
RP   FUNCTION (PROTEASE 3C).
RX   PubMed=26610553; DOI=10.3390/v7122922;
RA   Dougherty J.D., Tsai W.C., Lloyd R.E.;
RT   "Multiple Poliovirus Proteins Repress Cytoplasmic RNA Granules.";
RL   Viruses 7:6127-6140(2015).
RN   [60]
RP   FUNCTION (PROTEIN 3A).
RX   PubMed=30755512; DOI=10.1128/mbio.02742-18;
RA   Lyoo H., van der Schaar H.M., Dorobantu C.M., Rabouw H.H.,
RA   Strating J.R.P.M., van Kuppeveld F.J.M.;
RT   "ACBD3 is an essential pan-enterovirus host factor that mediates the
RT   interaction between viral 3A protein and cellular protein PI4KB.";
RL   MBio 10:0-0(2019).
RN   [61]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-881, INTERACTION WITH CAPSID
RP   PROTEIN VP0 (CAPSID PROTEIN VP1), INTERACTION WITH CAPSID PROTEIN VP4
RP   (CAPSID PROTEIN VP1), INTERACTION WITH CAPSID PROTEIN VP1 (CAPSID PROTEIN
RP   VP0), INTERACTION WITH CAPSID PROTEIN VP3 (CAPSID PROTEIN VP0), INTERACTION
RP   WITH CAPSID PROTEIN VP1 (CAPSID PROTEIN VP2), INTERACTION WITH CAPSID
RP   PROTEIN VP3 (CAPSID PROTEIN VP2), INTERACTION WITH CAPSID PROTEIN VP1
RP   (CAPSID PROTEIN VP3), INTERACTION WITH CAPSID PROTEIN VP0 (CAPSID PROTEIN
RP   VP3), INTERACTION WITH CAPSID PROTEIN VP1 (CAPSID PROTEIN VP4), INTERACTION
RP   WITH CAPSID PROTEIN VP3 (CAPSID PROTEIN VP4), INTERACTION WITH CAPSID
RP   PROTEIN VP4 (CAPSID PROTEIN VP3), INTERACTION WITH CAPSID PROTEIN VP2
RP   (CAPSID PROTEIN VP3), FUNCTION (CAPSID PROTEIN VP1), FUNCTION (CAPSID
RP   PROTEIN VP2), AND FUNCTION (CAPSID PROTEIN VP3).
RX   PubMed=2994218; DOI=10.1126/science.2994218;
RA   Hogle J.M., Chow M., Filman D.J.;
RT   "Three-dimensional structure of poliovirus at 2.9-A resolution.";
RL   Science 229:1358-1365(1985).
RN   [62]
RP   X-RAY CRYSTALLOGRAPHY (2.88 ANGSTROMS) OF 2-880.
RX   PubMed=2548847; DOI=10.1002/j.1460-2075.1989.tb03541.x;
RA   Filman D.J., Syed R., Chow M., Macadam A.J., Minor P.D., Hogle J.M.;
RT   "Structural factors that control conformational transitions and serotype
RT   specificity in type 3 poliovirus.";
RL   EMBO J. 8:1567-1579(1989).
RN   [63]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-880, AND FUNCTION (CAPSID
RP   PROTEIN VP0).
RX   PubMed=7849583; DOI=10.1002/pro.5560031005;
RA   Basavappa R., Syed R., Flore O., Icenogle J.P., Filman D.J., Hogle J.M.;
RT   "Role and mechanism of the maturation cleavage of VP0 in poliovirus
RT   assembly: structure of the empty capsid assembly intermediate at 2.9 A
RT   resolution.";
RL   Protein Sci. 3:1651-1669(1994).
RN   [64]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-881.
RX   PubMed=7820548; DOI=10.1016/s0960-9822(00)00176-7;
RA   Grant R.A., Hiremath C.N., Filman D.J., Syed R., Andries K., Hogle J.M.;
RT   "Structures of poliovirus complexes with anti-viral drugs: implications for
RT   viral stability and drug design.";
RL   Curr. Biol. 4:784-797(1994).
RN   [65]
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.0 ANGSTROMS) OF 1-881, MYRISTOYLATION
RP   AT GLY-2, AND INTERACTION WITH HOST PVR (CAPSID PROTEIN VP1).
RX   PubMed=10618374; DOI=10.1073/pnas.97.1.79;
RA   He Y., Bowman V.D., Mueller S., Bator C.M., Bella J., Peng X., Baker T.S.,
RA   Wimmer E., Kuhn R.J., Rossmann M.G.;
RT   "Interaction of the poliovirus receptor with poliovirus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:79-84(2000).
RN   [66]
RP   STRUCTURE BY ELECTRON MICROSCOPY (15.0 ANGSTROMS) OF 2-881.
RX   PubMed=12663789; DOI=10.1128/jvi.77.8.4827-4835.2003;
RA   He Y., Mueller S., Chipman P.R., Bator C.M., Peng X., Bowman V.D.,
RA   Mukhopadhyay S., Wimmer E., Kuhn R.J., Rossmann M.G.;
RT   "Complexes of poliovirus serotypes with their common cellular receptor,
RT   CD155.";
RL   J. Virol. 77:4827-4835(2003).
RN   [67]
RP   STRUCTURE BY ELECTRON MICROSCOPY (11.0 ANGSTROMS) OF 97-880.
RX   PubMed=15919927; DOI=10.1128/jvi.79.12.7745-7755.2005;
RA   Bubeck D., Filman D.J., Cheng N., Steven A.C., Hogle J.M., Belnap D.M.;
RT   "The structure of the poliovirus 135S cell entry intermediate at 10-
RT   angstrom resolution reveals the location of an externalized polypeptide
RT   that binds to membranes.";
RL   J. Virol. 79:7745-7755(2005).
RN   [68]
RP   STRUCTURE BY ELECTRON MICROSCOPY (8.0 ANGSTROMS) OF 2-881.
RX   PubMed=19011098; DOI=10.1073/pnas.0807848105;
RA   Zhang P., Mueller S., Morais M.C., Bator C.M., Bowman V.D., Hafenstein S.,
RA   Wimmer E., Rossmann M.G.;
RT   "Crystal structure of CD155 and electron microscopic studies of its
RT   complexes with polioviruses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:18284-18289(2008).
RN   [69]
RP   STRUCTURE BY ELECTRON MICROSCOPY OF 97-341 AND 647-881.
RX   PubMed=20181687; DOI=10.1128/jvi.02393-09;
RA   Levy H.C., Bostina M., Filman D.J., Hogle J.M.;
RT   "Catching a virus in the act of RNA release: a novel poliovirus uncoating
RT   intermediate characterized by cryo-electron microscopy.";
RL   J. Virol. 84:4426-4441(2010).
RN   [70] {ECO:0007744|PDB:3OL7}
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1749-2209 IN COMPLEX WITH
RP   MAGNESIUM AND CTP, AND COFACTOR (RNA-DIRECTED RNA POLYMERASE).
RX   PubMed=21148772; DOI=10.1073/pnas.1007626107;
RA   Gong P., Peersen O.B.;
RT   "Structural basis for active site closure by the poliovirus RNA-dependent
RT   RNA polymerase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:22505-22510(2010).
RN   [71] {ECO:0007744|PDB:4K4S, ECO:0007744|PDB:4K4T, ECO:0007744|PDB:4K4U, ECO:0007744|PDB:4K4V, ECO:0007744|PDB:4K4W}
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1749-2209 IN COMPLEX WITH ZINC,
RP   AND ZINC-BINDING.
RX   PubMed=23667424; DOI=10.1371/journal.pone.0060272;
RA   Gong P., Kortus M.G., Nix J.C., Davis R.E., Peersen O.B.;
RT   "Structures of coxsackievirus, rhinovirus, and poliovirus polymerase
RT   elongation complexes solved by engineering RNA mediated crystal contacts.";
RL   PLoS ONE 8:E60272-E60272(2013).
RN   [72] {ECO:0007744|PDB:3J8F, ECO:0007744|PDB:3J9F}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS) OF 2-881 IN COMPLEX WITH
RP   THE PVR RECEPTOR, FUNCTION (CAPSID PROTEIN VP1), AND FUNCTION (CAPSID
RP   PROTEIN VP4).
RX   PubMed=25631086; DOI=10.1128/jvi.03101-14;
RA   Strauss M., Filman D.J., Belnap D.M., Cheng N., Noel R.T., Hogle J.M.;
RT   "Nectin-like interactions between poliovirus and its receptor trigger
RT   conformational changes associated with cell entry.";
RL   J. Virol. 89:4143-4157(2015).
RN   [73] {ECO:0007744|PDB:5Z3Q}
RP   X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 1243-1456 IN COMPLEX WITH ZINC,
RP   SUBUNIT (PROTEIN 2C), CATALYTIC ACTIVITY (PROTEIN 2C), ZINC-FINGER (PROTEIN
RP   2C), DOMAIN (PROTEIN 2C), FUNCTION (PROTEIN 2C), MUTAGENESIS OF LYS-1262;
RP   LEU-1268; ALA-1272; ASP-1304; ASN-1350; ARG-1368; CYS-1396; CYS-1399;
RP   PHE-1405; CYS-1408; LEU-1411; CYS-1413; CYS-1450; MET-1451; LEU-1454 AND
RP   PHE-1455, AND BIOPHYSICOCHEMICAL PROPERTIES (PROTEIN 2C).
RX   PubMed=30231078; DOI=10.1371/journal.ppat.1007304;
RA   Guan H., Tian J., Zhang C., Qin B., Cui S.;
RT   "Crystal structure of a soluble fragment of poliovirus 2CATPase.";
RL   PLoS Pathog. 14:e1007304-e1007304(2018).
RN   [74] {ECO:0007744|PDB:6HLV}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1457-1514, INTERACTION WITH HOST
RP   ACBD3 (PROTEIN 3A), FUNCTION (PROTEIN 3A), AND SUBUNIT (PROTEIN 3A).
RX   PubMed=31381608; DOI=10.1371/journal.ppat.1007962;
RA   Horova V., Lyoo H., Rozycki B., Chalupska D., Smola M., Humpolickova J.,
RA   Strating J.R.P.M., van Kuppeveld F.J.M., Boura E., Klima M.;
RT   "Convergent evolution in the mechanisms of ACBD3 recruitment to
RT   picornavirus replication sites.";
RL   PLoS Pathog. 15:E1007962-E1007962(2019).
CC   -!- FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo
CC       T=3 symmetry with capsid proteins VP2 and VP3 (PubMed:2994218). The
CC       capsid is 300 Angstroms in diameter, composed of 60 copies of each
CC       capsid protein and enclosing the viral positive strand RNA genome
CC       (PubMed:2994218). Capsid protein VP1 mainly forms the vertices of the
CC       capsid (PubMed:23365424). Capsid protein VP1 interacts with host cell
CC       receptor PVR to provide virion attachment to target host epithelial
CC       cells (PubMed:25631086). This attachment induces virion internalization
CC       predominantly through clathrin- and caveolin-independent endocytosis in
CC       Hela cells and through caveolin-mediated endocytosis in brain
CC       microvascular endothelial cells (PubMed:17717529, PubMed:18191571,
CC       PubMed:17622193). Tyrosine kinases are probably involved in the entry
CC       process (PubMed:17717529). Virus binding to PVR induces increased
CC       junctional permeability and rearrangement of junctional proteins
CC       (PubMed:17717529). Modulation of endothelial tight junctions, as well
CC       as cytolytic infection of endothelial cells themselves, may result in
CC       loss of endothelial integrity which may help the virus to reach the CNS
CC       (PubMed:17717529). After binding to its receptor, the capsid undergoes
CC       conformational changes (PubMed:25631086). Capsid protein VP1 N-terminus
CC       (that contains an amphipathic alpha-helix) and capsid protein VP4 are
CC       externalized (PubMed:25631086). Together, they shape a pore in the host
CC       membrane through which viral genome is translocated to host cell
CC       cytoplasm (PubMed:25631086). {ECO:0000269|PubMed:17622193,
CC       ECO:0000269|PubMed:17717529, ECO:0000269|PubMed:18191571,
CC       ECO:0000269|PubMed:23365424, ECO:0000269|PubMed:25631086,
CC       ECO:0000269|PubMed:2994218}.
CC   -!- FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo
CC       T=3 symmetry with capsid proteins VP1 and VP3 (PubMed:2994218). The
CC       capsid is 300 Angstroms in diameter, composed of 60 copies of each
CC       capsid protein and enclosing the viral positive strand RNA genome
CC       (PubMed:18191571). {ECO:0000269|PubMed:18191571,
CC       ECO:0000269|PubMed:2994218}.
CC   -!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
CC       T=3 symmetry with capsid proteins VP2 and VP1 (PubMed:2994218). The
CC       capsid is 300 Angstroms in diameter, composed of 60 copies of each
CC       capsid protein and enclosing the viral positive strand RNA genome
CC       (PubMed:18191571). {ECO:0000269|PubMed:18191571,
CC       ECO:0000269|PubMed:2994218}.
CC   -!- FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid
CC       shell (PubMed:25631086). After binding to the host receptor, the capsid
CC       undergoes conformational changes (PubMed:25631086). Capsid protein VP4
CC       is released, Capsid protein VP1 N-terminus is externalized, and
CC       together, they shape a pore in the host membrane through which the
CC       viral genome is translocated into the host cell cytoplasm
CC       (PubMed:25631086, PubMed:23365424). {ECO:0000269|PubMed:23365424,
CC       ECO:0000269|PubMed:25631086}.
CC   -!- FUNCTION: [Capsid protein VP0]: Component of immature procapsids, which
CC       is cleaved into capsid proteins VP4 and VP2 after maturation
CC       (PubMed:7849583). Allows the capsid to remain inactive before the
CC       maturation step (PubMed:1851815). {ECO:0000269|PubMed:1851815,
CC       ECO:0000269|PubMed:7849583}.
CC   -!- FUNCTION: [Protease 2A]: Cysteine protease that cleaves viral
CC       polyprotein and specific host proteins (PubMed:1649327). It is
CC       responsible for the autocatalytic cleavage between the P1 and P2
CC       regions, which is the first cleavage occurring in the polyprotein
CC       (PubMed:1649327). Cleaves also the host translation initiation factor
CC       EIF4G1, in order to shut down the capped cellular mRNA translation
CC       (PubMed:9755863). Inhibits the host nucleus-cytoplasm protein and RNA
CC       trafficking by cleaving host members of the nuclear pores including
CC       NUP98, NUP62 and NUP153 (PubMed:19789179). Counteracts stress granule
CC       formation probably by antagonizing its assembly or promoting its
CC       dissassembly (By similarity). Cleaves and inhibits host IFIH1/MDA5,
CC       thereby inhibiting the type-I IFN production and the establishment of
CC       the antiviral state (PubMed:24390337). Cleaves and inhibits host MAVS,
CC       thereby inhibiting the type-I IFN production and the establishment of
CC       the antiviral state (PubMed:24390337). {ECO:0000250|UniProtKB:P03301,
CC       ECO:0000269|PubMed:1649327, ECO:0000269|PubMed:19789179,
CC       ECO:0000269|PubMed:24390337, ECO:0000269|PubMed:9755863}.
CC   -!- FUNCTION: [Protein 2B]: Plays an essential role in the virus
CC       replication cycle by acting as a viroporin (PubMed:21835803). Creates a
CC       pore in the host reticulum endoplasmic and as a consequence releases
CC       Ca2+ in the cytoplasm of infected cell. In turn, high levels of
CC       cytoplasmic calcium may trigger membrane trafficking and transport of
CC       viral ER-associated proteins to viroplasms, sites of viral genome
CC       replication (PubMed:9151862). {ECO:0000269|PubMed:21835803,
CC       ECO:0000269|PubMed:9151862}.
CC   -!- FUNCTION: [Protein 2C]: Induces and associates with structural
CC       rearrangements of intracellular membranes. Displays RNA-binding,
CC       nucleotide binding and NTPase activities (PubMed:7730315,
CC       PubMed:19520852, PubMed:8385138, PubMed:30231078). May play a role in
CC       virion morphogenesis and viral RNA encapsidation by interacting with
CC       the capsid protein VP3 (PubMed:22761387). {ECO:0000269|PubMed:19520852,
CC       ECO:0000269|PubMed:22761387, ECO:0000269|PubMed:30231078,
CC       ECO:0000269|PubMed:7730315, ECO:0000269|PubMed:8385138}.
CC   -!- FUNCTION: [Protein 3AB]: Localizes the viral replication complex to the
CC       surface of membranous vesicles. Together with protein 3CD binds the
CC       Cis-Active RNA Element (CRE) which is involved in RNA synthesis
CC       initiation. Acts as a cofactor to stimulate the activity of 3D
CC       polymerase, maybe through a nucleid acid chaperone activity.
CC       {ECO:0000269|PubMed:21045553}.
CC   -!- FUNCTION: [Protein 3A]: Localizes the viral replication complex to the
CC       surface of membranous vesicles. It inhibits host cell endoplasmic
CC       reticulum-to-Golgi apparatus transport and causes the disassembly of
CC       the Golgi complex, possibly through GBF1 interaction (PubMed:17079330,
CC       PubMed:15914217). This would result in depletion of MHC, trail
CC       receptors and IFN receptors at the host cell surface (PubMed:17079330,
CC       PubMed:15914217). Plays an essential role in viral RNA replication by
CC       recruiting ACBD3 and PI4KB at the viral replication sites, thereby
CC       allowing the formation of the rearranged membranous structures where
CC       viral replication takes place (Probable) (PubMed:31381608).
CC       {ECO:0000269|PubMed:15914217, ECO:0000269|PubMed:17079330,
CC       ECO:0000269|PubMed:31381608, ECO:0000305|PubMed:30755512}.
CC   -!- FUNCTION: [Viral protein genome-linked]: Acts as a primer for viral RNA
CC       replication and remains covalently bound to viral genomic RNA
CC       (PubMed:12502805, PubMed:20441784, PubMed:16840321, PubMed:209034,
CC       PubMed:6250717). VPg is uridylylated prior to priming replication into
CC       VPg-pUpU (PubMed:12502805, PubMed:20441784, PubMed:16840321). The oriI
CC       viral genomic sequence may act as a template for this. The VPg-pUpU is
CC       then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA
CC       polymerase to replicate the viral genome (PubMed:12502805,
CC       PubMed:16840321). Following genome release from the infecting virion in
CC       the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2
CC       (PubMed:22908287). During the late stage of the replication cycle, host
CC       TDP2 is excluded from sites of viral RNA synthesis and encapsidation,
CC       allowing for the generation of progeny virions (PubMed:22908287).
CC       {ECO:0000269|PubMed:12502805, ECO:0000269|PubMed:16840321,
CC       ECO:0000269|PubMed:20441784, ECO:0000269|PubMed:209034,
CC       ECO:0000269|PubMed:22908287, ECO:0000269|PubMed:6250717}.
CC   -!- FUNCTION: [Protein 3CD]: Involved in the viral replication complex and
CC       viral polypeptide maturation (PubMed:1331532, PubMed:10666252). It
CC       exhibits protease activity with a specificity and catalytic efficiency
CC       that is different from protease 3C (PubMed:1331532). Protein 3CD binds
CC       to the 5'UTR of the viral genome (PubMed:10666252).
CC       {ECO:0000269|PubMed:10666252, ECO:0000269|PubMed:1331532}.
CC   -!- FUNCTION: [Protease 3C]: Major viral protease that mediates proteolytic
CC       processing of the polyprotein (PubMed:8097606). Cleaves host EIF5B,
CC       contributing to host translation shutoff (PubMed:18572216). Cleaves
CC       also host PABPC1, contributing to host translation shutoff
CC       (PubMed:18632855). Cleaves host RIGI and thus contributes to the
CC       inhibition of type I interferon production (PubMed:24390337). Cleaves
CC       host NLRP1, triggers host N-glycine-mediated degradation of the
CC       autoinhibitory NLRP1 N-terminal fragment (By similarity). Inhibits the
CC       integrated stress response (ISR) in the infected cell by cleaving host
CC       G3BP1 (PubMed:18005751, PubMed:26610553). Stress granule formation is
CC       thus inhibited, which allows protein synthesis and viral replication
CC       (PubMed:18005751, PubMed:26610553). {ECO:0000250|UniProtKB:P03303,
CC       ECO:0000269|PubMed:18005751, ECO:0000269|PubMed:18572216,
CC       ECO:0000269|PubMed:18632855, ECO:0000269|PubMed:24390337,
CC       ECO:0000269|PubMed:26610553, ECO:0000269|PubMed:8097606}.
CC   -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genomic
CC       RNA on the surface of intracellular membranes. May form linear arrays
CC       of subunits that propagate along a strong head-to-tail interaction
CC       called interface-I. Covalently attaches UMP to a tyrosine of VPg, which
CC       is used to prime RNA synthesis. The positive stranded RNA genome is
CC       first replicated at virus induced membranous vesicles, creating a dsRNA
CC       genomic replication form. This dsRNA is then used as template to
CC       synthesize positive stranded RNA genomes. ss(+)RNA genomes are either
CC       translated, replicated or encapsidated. {ECO:0000269|PubMed:2535728}.
CC   -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
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: [Protease 2A]:
CC       Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus
CC         polyprotein.; EC=3.4.22.29; Evidence={ECO:0000269|PubMed:1649327};
CC   -!- CATALYTIC ACTIVITY: [Protein 2C]:
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         Evidence={ECO:0000269|PubMed:19520852, ECO:0000269|PubMed:30231078,
CC         ECO:0000269|PubMed:7730315, ECO:0000269|PubMed:8385138};
CC   -!- CATALYTIC ACTIVITY: [Protease 3C]:
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         ECO:0000269|PubMed:8097606};
CC   -!- COFACTOR: [RNA-directed RNA polymerase]:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:21148772};
CC       Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal
CC       center (PubMed:21148772). The magnesium ions are not prebound but only
CC       present for catalysis (PubMed:21148772). Requires the presence of
CC       3CDpro or 3CPro (By similarity). {ECO:0000250|UniProtKB:P03313,
CC       ECO:0000269|PubMed:21148772};
CC   -!- ACTIVITY REGULATION: [RNA-directed RNA polymerase]: Replication or
CC       transcription is subject to high level of random mutations by the
CC       nucleotide analog ribavirin. {ECO:0000269|PubMed:15649563}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=642 uM for ATP {ECO:0000269|PubMed:30231078};
CC         Note=For protein 2C ATPase activity. {ECO:0000269|PubMed:30231078};
CC   -!- SUBUNIT: [Capsid protein VP0]: Interacts with capsid protein VP1 and
CC       capsid protein VP3 to form heterotrimeric protomers.
CC       {ECO:0000269|PubMed:2994218}.
CC   -!- SUBUNIT: [Capsid protein VP1]: Interacts with capsid protein VP0, and
CC       capsid protein VP3 to form heterotrimeric protomers (PubMed:2994218).
CC       Five protomers subsequently associate to form pentamers which serve as
CC       building blocks for the capsid (PubMed:2994218). Interacts with capsid
CC       protein VP2, capsid protein VP3 and capsid protein VP4 following
CC       cleavage of capsid protein VP0 (PubMed:10618374, PubMed:2994218).
CC       Interacts with human PVR (PubMed:10618374).
CC       {ECO:0000269|PubMed:10618374, ECO:0000269|PubMed:2994218}.
CC   -!- SUBUNIT: [Capsid protein VP2]: Interacts with capsid protein VP1 and
CC       capsid protein VP3 in the mature capsid. {ECO:0000269|PubMed:2994218}.
CC   -!- SUBUNIT: [Capsid protein VP3]: Interacts with capsid protein VP0 and
CC       capsid protein VP1 to form heterotrimeric protomers (PubMed:2994218).
CC       Five protomers subsequently associate to form pentamers which serve as
CC       building blocks for the capsid (PubMed:2994218). Interacts with capsid
CC       protein VP4 in the mature capsid (PubMed:2994218). Interacts with
CC       protein 2C; this interaction may be important for virion morphogenesis
CC       (PubMed:20865167). {ECO:0000269|PubMed:20865167,
CC       ECO:0000269|PubMed:2994218}.
CC   -!- SUBUNIT: [Capsid protein VP4]: Interacts with capsid protein VP1 and
CC       capsid protein VP3. {ECO:0000269|PubMed:2994218}.
CC   -!- SUBUNIT: [Protease 2A]: Homodimer. {ECO:0000250|UniProtKB:P04936}.
CC   -!- SUBUNIT: [Protein 2C]: Homohexamer; forms a hexameric ring structure
CC       with 6-fold symmetry characteristic of AAA+ ATPases (Probable).
CC       Interacts (via N-terminus) with host RTN3 (via reticulon domain); this
CC       interaction is important for viral replication (PubMed:17182608).
CC       Interacts with capsid protein VP3; this interaction may be important
CC       for virion morphogenesis (PubMed:20865167).
CC       {ECO:0000269|PubMed:17182608, ECO:0000269|PubMed:20865167,
CC       ECO:0000305|PubMed:19520852, ECO:0000305|PubMed:30231078}.
CC   -!- SUBUNIT: [Protein 3AB]: Interacts with protein 3CD.
CC       {ECO:0000269|PubMed:7929441}.
CC   -!- SUBUNIT: [Protein 3A]: Homodimer (PubMed:31381608, PubMed:12823963).
CC       Interacts with host GBF1 (PubMed:17005635, PubMed:21345960). Interacts
CC       (via GOLD domain) with host ACBD3 (via GOLD domain); this interaction
CC       allows the formation of a viral protein 3A/ACBD3 heterotetramer with a
CC       2:2 stoichiometry, which will stimulate the recruitment of host PI4KB
CC       in order to synthesize PI4P at the viral RNA replication sites
CC       (PubMed:22258260, PubMed:31381608). {ECO:0000269|PubMed:12823963,
CC       ECO:0000269|PubMed:17005635, ECO:0000269|PubMed:21345960,
CC       ECO:0000269|PubMed:22258260, ECO:0000269|PubMed:31381608}.
CC   -!- SUBUNIT: [Viral protein genome-linked]: Interacts with RNA-directed RNA
CC       polymerase. {ECO:0000269|PubMed:17409142}.
CC   -!- SUBUNIT: [Protein 3CD]: Interacts with protein 3AB and with RNA-
CC       directed RNA polymerase. {ECO:0000269|PubMed:7929441}.
CC   -!- SUBUNIT: [RNA-directed RNA polymerase]: Interacts with Viral protein
CC       genome-linked and with protein 3CD. {ECO:0000269|PubMed:17409142}.
CC   -!- INTERACTION:
CC       PRO_0000424692; Q9H3P7: ACBD3; Xeno; NbExp=12; IntAct=EBI-21242141, EBI-1791792;
CC       PRO_0000424692; Q92538: GBF1; Xeno; NbExp=8; IntAct=EBI-21242141, EBI-359050;
CC       PRO_0000424692; Q9UBF8: PI4KB; Xeno; NbExp=9; IntAct=EBI-21242141, EBI-1053214;
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion
CC       {ECO:0000269|PubMed:1851815}. Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
CC       {ECO:0000269|PubMed:1851815}. Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC       {ECO:0000269|PubMed:1851815}. Host cytoplasm {ECO:0000305}.
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 derived from
CC       the endoplasmic reticulum.
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.
CC   -!- SUBCELLULAR LOCATION: [Protein 3A]: 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.
CC   -!- SUBCELLULAR LOCATION: [Protein 3AB]: 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.
CC   -!- SUBCELLULAR LOCATION: [Viral protein genome-linked]: Virion
CC       {ECO:0000305|PubMed:202952}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:Q66478}.
CC   -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm.
CC   -!- SUBCELLULAR LOCATION: [Protein 3CD]: Host nucleus
CC       {ECO:0000269|PubMed:15016543}. Host cytoplasm
CC       {ECO:0000269|PubMed:15016543}. 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.
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 derived from the endoplasmic reticulum.
CC   -!- DOMAIN: [Protein 2C]: The N-terminus has membrane-binding
CC       (PubMed:9696129). The N-terminus also displays RNA-binding properties
CC       (PubMed:7730315). The N-terminus is involved in oligomerization
CC       (PubMed:19520852). The central part contains an ATPase domain and a C4-
CC       type zinc-finger (PubMed:30231078). The C-terminus is involved in RNA-
CC       binding (PubMed:7730315). The extreme C-terminus contains a region
CC       involved in oligomerization (PubMed:30231078).
CC       {ECO:0000269|PubMed:19520852, ECO:0000269|PubMed:30231078,
CC       ECO:0000269|PubMed:7730315, ECO:0000269|PubMed:9696129}.
CC   -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the
CC       viral proteases yield processing intermediates and the mature proteins.
CC       {ECO:0000269|PubMed:8097606}.
CC   -!- PTM: [Capsid protein VP0]: Myristoylation is required for the formation
CC       of pentamers during virus assembly (PubMed:1850017, PubMed:1851815).
CC       Further assembly of 12 pentamers and a molecule of genomic RNA
CC       generates the provirion. {ECO:0000269|PubMed:1850017,
CC       ECO:0000269|PubMed:1851815}.
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 it is followed by a conformational
CC       change infectious virion. {ECO:0000269|PubMed:10516013}.
CC   -!- PTM: [Capsid protein VP4]: Myristoylation is required during RNA
CC       encapsidation and formation of the mature virus particle.
CC       {ECO:0000269|PubMed:1850017}.
CC   -!- PTM: [Viral protein genome-linked]: VPg is uridylylated by the
CC       polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for
CC       the genomic RNA replication. {ECO:0000269|PubMed:12502805,
CC       ECO:0000269|PubMed:16840321}.
CC   -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC       {ECO:0000305}.
CC   -!- CAUTION: [Protein 3A]: Has been proposed to interact with host LIS1/NUF
CC       (PubMed:16138011), but this has not been confirmed by other studies
CC       (PubMed:21345960). {ECO:0000305|PubMed:16138011,
CC       ECO:0000305|PubMed:21345960}.
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure associated with cellular receptor;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1dgi";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure associated with cellular receptor;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1nn8";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure in complex with R80633, an inhibitor of viral replication;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1po1";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure in complex with R77975, an inhibitor of viral replication;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1po2";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral empty
CC       capsid structure;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1pov";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure complexed with R78206;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1vbd";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2plv";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure of 135S cell entry intermediate;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1xyr";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1hxs";
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DR   EMBL; V01149; CAA24461.1; -; Genomic_RNA.
DR   EMBL; V01148; CAA24446.1; -; Genomic_RNA.
DR   EMBL; KU866422; AMS03992.1; -; Genomic_RNA.
DR   PIR; A03898; GNNY2P.
DR   PIR; A93258; GNNY1P.
DR   RefSeq; NP_041277.1; NC_002058.3.
DR   PDB; 1AL2; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
DR   PDB; 1AR6; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
DR   PDB; 1AR7; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
DR   PDB; 1AR8; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
DR   PDB; 1AR9; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
DR   PDB; 1ASJ; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
DR   PDB; 1DGI; EM; 22.00 A; 1=599-881, 2=74-341, 3=342-576, 4=2-69.
DR   PDB; 1FPT; X-ray; 3.00 A; P=665-682.
DR   PDB; 1HXS; X-ray; 2.20 A; 1=580-881, 2=70-341, 3=342-578, 4=2-69.
DR   PDB; 1L1N; X-ray; 2.10 A; A/B=1566-1748.
DR   PDB; 1NG7; NMR; -; A/B=1457-1515.
DR   PDB; 1NN8; EM; 15.00 A; 1=580-881, 2=70-341, 3=342-576, 4=2-69.
DR   PDB; 1PO1; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
DR   PDB; 1PO2; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
DR   PDB; 1POV; X-ray; 2.80 A; 0=2-341, 1=580-881, 3=342-579.
DR   PDB; 1RA6; X-ray; 2.00 A; A=1749-2209.
DR   PDB; 1RA7; X-ray; 2.35 A; A=1749-2209.
DR   PDB; 1RAJ; X-ray; 2.50 A; A=1817-2209.
DR   PDB; 1RDR; X-ray; 2.40 A; A=1749-2209.
DR   PDB; 1TQL; X-ray; 2.30 A; A=1749-2209.
DR   PDB; 1VBD; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
DR   PDB; 1XYR; EM; 11.00 A; 1=650-881, 2=97-333, 3=391-572, 5=342-353, 6=355-390, 7=82-95, 8=621-631.
DR   PDB; 2BBL; NMR; -; A=1544-1565.
DR   PDB; 2BBP; NMR; -; A=1544-1565.
DR   PDB; 2IJD; X-ray; 3.40 A; 1/2=1566-2208.
DR   PDB; 2IJF; X-ray; 3.00 A; A=1749-2208.
DR   PDB; 2ILY; X-ray; 2.60 A; A=1749-2208.
DR   PDB; 2ILZ; X-ray; 2.50 A; A=1749-2208.
DR   PDB; 2IM0; X-ray; 2.25 A; A=1749-2208.
DR   PDB; 2IM1; X-ray; 2.50 A; A=1749-2208.
DR   PDB; 2IM2; X-ray; 2.35 A; A=1749-2208.
DR   PDB; 2IM3; X-ray; 2.60 A; A=1749-2208.
DR   PDB; 2PLV; X-ray; 2.88 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
DR   PDB; 3EPC; EM; 8.00 A; 1=599-881, 2=74-341, 3=342-576, 4=2-69.
DR   PDB; 3IYB; EM; 10.00 A; 1=647-881, 3=342-572, 4=97-341.
DR   PDB; 3IYC; EM; -; 1=647-881, 4=97-341.
DR   PDB; 3J3O; EM; 11.10 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
DR   PDB; 3J3P; EM; 9.10 A; 1=580-881, 2=70-341, 3=342-579.
DR   PDB; 3J48; EM; 5.50 A; 1=580-881, 2=70-341, 3=342-579.
DR   PDB; 3J8F; EM; 3.70 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
DR   PDB; 3J9F; EM; 9.00 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
DR   PDB; 3JBC; EM; 5.60 A; 1=580-881, 2=70-341, 3=342-578, 4=2-69.
DR   PDB; 3JBD; EM; 4.70 A; 1=580-881, 2=70-341, 3=342-578, 4=2-69.
DR   PDB; 3JBE; EM; 4.20 A; 1=580-881, 2=70-341, 3=342-578, 4=2-69.
DR   PDB; 3JBF; EM; 4.60 A; 1=580-881, 2=70-341, 3=342-578, 4=2-69.
DR   PDB; 3JBG; EM; 3.80 A; 1=580-881, 2=70-341, 3=342-578, 4=2-69.
DR   PDB; 3OL7; X-ray; 2.70 A; A/E/I/M=1749-2209.
DR   PDB; 4DCD; X-ray; 1.69 A; A=1566-1748.
DR   PDB; 4K4S; X-ray; 2.40 A; A/E=1749-2209.
DR   PDB; 4K4T; X-ray; 2.75 A; A/E=1749-2209.
DR   PDB; 4K4U; X-ray; 2.85 A; A/E=1749-2209.
DR   PDB; 4K4V; X-ray; 2.63 A; A/E=1749-2209.
DR   PDB; 4K4W; X-ray; 2.69 A; A/E=1749-2209.
DR   PDB; 4NLO; X-ray; 2.20 A; A=1749-2209.
DR   PDB; 4NLP; X-ray; 2.20 A; A=1749-2209.
DR   PDB; 4NLQ; X-ray; 2.30 A; A=1749-2209.
DR   PDB; 4NLR; X-ray; 2.00 A; A=1749-2209.
DR   PDB; 4NLS; X-ray; 2.00 A; A=1749-2209.
DR   PDB; 4NLT; X-ray; 2.50 A; A=1749-2209.
DR   PDB; 4NLU; X-ray; 2.10 A; A=1749-2209.
DR   PDB; 4NLV; X-ray; 2.30 A; A=1749-2209.
DR   PDB; 4NLW; X-ray; 2.10 A; A=1749-2209.
DR   PDB; 4NLX; X-ray; 2.60 A; A=1749-2209.
DR   PDB; 4NLY; X-ray; 2.30 A; A=1749-2209.
DR   PDB; 4R0E; X-ray; 3.00 A; A=1749-2209.
DR   PDB; 5KTZ; EM; 4.30 A; 1=636-858, 2=70-338, 3=342-572.
DR   PDB; 5KU0; EM; 4.20 A; 1=636-858, 2=70-338, 3=342-572.
DR   PDB; 5KU2; EM; 4.50 A; 1=650-858, 2=70-337, 3=342-571.
DR   PDB; 5KWL; EM; 4.50 A; 1=650-858, 2=70-337, 3=342-571.
DR   PDB; 5Z3Q; X-ray; 2.54 A; A/B/C/D/E/H=1243-1456.
DR   PDB; 6HLV; X-ray; 2.50 A; B=1457-1514.
DR   PDB; 6P9O; EM; 2.90 A; 1=580-881, 2=70-341.
DR   PDB; 6P9W; EM; 3.20 A; 1=580-881, 2=70-341.
DR   PDB; 6PSZ; EM; 3.20 A; 1=580-881, 2=70-341.
DR   PDBsum; 1AL2; -.
DR   PDBsum; 1AR6; -.
DR   PDBsum; 1AR7; -.
DR   PDBsum; 1AR8; -.
DR   PDBsum; 1AR9; -.
DR   PDBsum; 1ASJ; -.
DR   PDBsum; 1DGI; -.
DR   PDBsum; 1FPT; -.
DR   PDBsum; 1HXS; -.
DR   PDBsum; 1L1N; -.
DR   PDBsum; 1NG7; -.
DR   PDBsum; 1NN8; -.
DR   PDBsum; 1PO1; -.
DR   PDBsum; 1PO2; -.
DR   PDBsum; 1POV; -.
DR   PDBsum; 1RA6; -.
DR   PDBsum; 1RA7; -.
DR   PDBsum; 1RAJ; -.
DR   PDBsum; 1RDR; -.
DR   PDBsum; 1TQL; -.
DR   PDBsum; 1VBD; -.
DR   PDBsum; 1XYR; -.
DR   PDBsum; 2BBL; -.
DR   PDBsum; 2BBP; -.
DR   PDBsum; 2IJD; -.
DR   PDBsum; 2IJF; -.
DR   PDBsum; 2ILY; -.
DR   PDBsum; 2ILZ; -.
DR   PDBsum; 2IM0; -.
DR   PDBsum; 2IM1; -.
DR   PDBsum; 2IM2; -.
DR   PDBsum; 2IM3; -.
DR   PDBsum; 2PLV; -.
DR   PDBsum; 3EPC; -.
DR   PDBsum; 3IYB; -.
DR   PDBsum; 3IYC; -.
DR   PDBsum; 3J3O; -.
DR   PDBsum; 3J3P; -.
DR   PDBsum; 3J48; -.
DR   PDBsum; 3J8F; -.
DR   PDBsum; 3J9F; -.
DR   PDBsum; 3JBC; -.
DR   PDBsum; 3JBD; -.
DR   PDBsum; 3JBE; -.
DR   PDBsum; 3JBF; -.
DR   PDBsum; 3JBG; -.
DR   PDBsum; 3OL7; -.
DR   PDBsum; 4DCD; -.
DR   PDBsum; 4K4S; -.
DR   PDBsum; 4K4T; -.
DR   PDBsum; 4K4U; -.
DR   PDBsum; 4K4V; -.
DR   PDBsum; 4K4W; -.
DR   PDBsum; 4NLO; -.
DR   PDBsum; 4NLP; -.
DR   PDBsum; 4NLQ; -.
DR   PDBsum; 4NLR; -.
DR   PDBsum; 4NLS; -.
DR   PDBsum; 4NLT; -.
DR   PDBsum; 4NLU; -.
DR   PDBsum; 4NLV; -.
DR   PDBsum; 4NLW; -.
DR   PDBsum; 4NLX; -.
DR   PDBsum; 4NLY; -.
DR   PDBsum; 4R0E; -.
DR   PDBsum; 5KTZ; -.
DR   PDBsum; 5KU0; -.
DR   PDBsum; 5KU2; -.
DR   PDBsum; 5KWL; -.
DR   PDBsum; 5Z3Q; -.
DR   PDBsum; 6HLV; -.
DR   PDBsum; 6P9O; -.
DR   PDBsum; 6P9W; -.
DR   PDBsum; 6PSZ; -.
DR   BMRB; P03300; -.
DR   EMDB; EMD-20275; -.
DR   EMDB; EMD-20276; -.
DR   EMDB; EMD-20469; -.
DR   EMDB; EMD-27943; -.
DR   EMDB; EMD-8284; -.
DR   EMDB; EMD-8285; -.
DR   EMDB; EMD-8286; -.
DR   SMR; P03300; -.
DR   ELM; P03300; -.
DR   IntAct; P03300; 5.
DR   BindingDB; P03300; -.
DR   ChEMBL; CHEMBL5127; -.
DR   DrugBank; DB08014; (METHYLPYRIDAZINE PIPERIDINE BUTYLOXYPHENYL)ETHYLACETATE.
DR   DrugBank; DB08013; (METHYLPYRIDAZINE PIPERIDINE PROPYLOXYPHENYL)ETHYLACETATE.
DR   DrugBank; DB04137; Guanosine-5'-Triphosphate.
DR   DrugBank; DB08231; Myristic acid.
DR   DrugBank; DB08012; Pirodavir.
DR   DrugBank; DB03963; S-(Dimethylarsenic)Cysteine.
DR   DrugBank; DB03203; Sphingosine.
DR   MEROPS; C03.001; -.
DR   MEROPS; C03.020; -.
DR   MEROPS; N08.001; -.
DR   iPTMnet; P03300; -.
DR   ABCD; P03300; 10 sequenced antibodies.
DR   DNASU; 919920; -.
DR   GeneID; 919920; -.
DR   KEGG; vg:919920; -.
DR   EvolutionaryTrace; P03300; -.
DR   Proteomes; UP000000356; Genome.
DR   Proteomes; UP000138192; Genome.
DR   Proteomes; UP000149468; Genome.
DR   GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
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-dependent RNA polymerase activity; IDA:CACAO.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039520; P:induction by virus of host autophagy; IDA:UniProtKB.
DR   GO; GO:0044694; P:pore-mediated entry of viral genome into 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:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR   GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0039606; P:suppression by virus of host translation initiation; IDA: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; IEA:UniProtKB-KW.
DR   GO; GO:0039540; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity; IEA:UniProtKB-KW.
DR   GO; GO:0039545; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039707; P:virus-mediated pore formation in host cell membrane; IEA:UniProtKB-KW.
DR   CDD; cd23213; Enterovirus_RdRp; 1.
DR   CDD; cd00205; rhv_like; 3.
DR   Gene3D; 1.20.960.20; -; 1.
DR   Gene3D; 2.60.120.20; -; 3.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 6.10.20.20; Poliovirus 3A protein-like; 1.
DR   Gene3D; 4.10.880.10; Poliovirus 3D polymerase Domain 1 (Nucleotidyltransferase); 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 4.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR   InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014838; P3A.
DR   InterPro; IPR036203; P3A_soluble_dom.
DR   InterPro; IPR044067; PCV_3C_PRO.
DR   InterPro; IPR000081; Peptidase_C3.
DR   InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR003138; Pico_P1A.
DR   InterPro; IPR002527; Pico_P2B.
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; PF08727; P3A; 1.
DR   Pfam; PF00548; Peptidase_C3; 1.
DR   Pfam; PF02226; Pico_P1A; 1.
DR   Pfam; PF00947; Pico_P2A; 1.
DR   Pfam; PF01552; Pico_P2B; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   Pfam; PF00073; Rhv; 3.
DR   Pfam; PF00910; RNA_helicase; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF88633; Positive stranded ssRNA viruses; 2.
DR   SUPFAM; SSF89043; Soluble domain of poliovirus core protein 3a; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
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; Activation of host autophagy by virus; ATP-binding;
KW   Autocatalytic cleavage; Capsid protein; Covalent protein-RNA linkage;
KW   Direct protein sequencing;
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 MAVS by virus; Inhibition of host MDA5 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; Magnesium; Membrane;
KW   Metal-binding; Myristate; Nucleotide-binding; Nucleotidyltransferase;
KW   Phosphoprotein; Pore-mediated penetration of viral genome into host cell;
KW   Protease; Reference proteome; Repeat; 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;
KW   Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW   Virus endocytosis by host; Virus entry into host cell; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000269|PubMed:1850017"
FT   CHAIN           2..2209
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000424686"
FT   CHAIN           2..881
FT                   /note="P1"
FT                   /id="PRO_0000424687"
FT   CHAIN           2..341
FT                   /note="Capsid protein VP0"
FT                   /id="PRO_0000424688"
FT   CHAIN           2..69
FT                   /note="Capsid protein VP4"
FT                   /id="PRO_0000040080"
FT   CHAIN           70..341
FT                   /note="Capsid protein VP2"
FT                   /id="PRO_0000040081"
FT   CHAIN           342..579
FT                   /note="Capsid protein VP3"
FT                   /id="PRO_0000040082"
FT   CHAIN           580..881
FT                   /note="Capsid protein VP1"
FT                   /id="PRO_0000040083"
FT   CHAIN           882..1456
FT                   /note="P2"
FT                   /id="PRO_0000424689"
FT   CHAIN           882..1030
FT                   /note="Protease 2A"
FT                   /id="PRO_0000040084"
FT   CHAIN           1031..1127
FT                   /note="Protein 2B"
FT                   /id="PRO_0000040085"
FT   CHAIN           1128..1456
FT                   /note="Protein 2C"
FT                   /id="PRO_0000040086"
FT   CHAIN           1457..2209
FT                   /note="P3"
FT                   /id="PRO_0000424690"
FT   CHAIN           1457..1565
FT                   /note="Protein 3AB"
FT                   /id="PRO_0000424691"
FT   CHAIN           1457..1543
FT                   /note="Protein 3A"
FT                   /id="PRO_0000424692"
FT   CHAIN           1544..1565
FT                   /note="Viral protein genome-linked"
FT                   /id="PRO_0000040088"
FT   CHAIN           1566..2209
FT                   /note="Protein 3CD"
FT                   /id="PRO_0000424693"
FT   CHAIN           1566..1748
FT                   /note="Protease 3C"
FT                   /id="PRO_0000040089"
FT   CHAIN           1749..2209
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000040090"
FT   TOPO_DOM        2..1520
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        1521..1536
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1537..2209
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1232..1388
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1566..1744
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          1975..2090
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   ZN_FING         1396..1413
FT                   /note="C4-type"
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   REGION          580..600
FT                   /note="Amphipathic alpha-helix"
FT                   /evidence="ECO:0000255"
FT   REGION          599..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1128..1266
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000269|PubMed:19520852"
FT   REGION          1128..1200
FT                   /note="Membrane-binding"
FT                   /evidence="ECO:0000269|PubMed:9696129"
FT   REGION          1149..1153
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000269|PubMed:7730315"
FT   REGION          1440..1447
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000269|PubMed:7730315"
FT   REGION          1451..1456
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   COMPBIAS        599..615
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        901
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000269|PubMed:1649327"
FT   ACT_SITE        919
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000269|PubMed:1649327"
FT   ACT_SITE        990
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000269|PubMed:1649327"
FT   ACT_SITE        1605
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1636
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222,
FT                   ECO:0000269|PubMed:8097606"
FT   ACT_SITE        1712
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222,
FT                   ECO:0000269|PubMed:8097606"
FT   BINDING         936
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000305|PubMed:1310193"
FT   BINDING         938
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000305|PubMed:1310193"
FT   BINDING         996
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000305|PubMed:1310193"
FT   BINDING         998
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000305|PubMed:1310193"
FT   BINDING         1256..1263
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   BINDING         1396
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   BINDING         1399
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   BINDING         1408
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   BINDING         1413
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   BINDING         1981
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic; for RdRp activity"
FT                   /evidence="ECO:0000269|PubMed:21148772"
FT   BINDING         1981
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic; for RdRp activity"
FT                   /evidence="ECO:0000269|PubMed:21148772"
FT   BINDING         2076
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic; for RdRp activity"
FT                   /evidence="ECO:0000269|PubMed:21148772,
FT                   ECO:0000305|PubMed:2196557"
FT   BINDING         2076
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic; for RdRp activity"
FT                   /evidence="ECO:0000269|PubMed:21148772,
FT                   ECO:0000305|PubMed:2196557"
FT   SITE            69..70
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000269|PubMed:10516013"
FT   SITE            341..342
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            579..580
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            881..882
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1030..1031
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1127..1128
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1152
FT                   /note="Involved in the interaction with host RTN3"
FT                   /evidence="ECO:0000250|UniProtKB:Q66478"
FT   SITE            1456..1457
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1543..1544
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1565..1566
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1748..1749
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   MOD_RES         1546
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000269|PubMed:209034"
FT   MOD_RES         1546
FT                   /note="O-UMP-tyrosine; transient"
FT                   /evidence="ECO:0000269|PubMed:12502805,
FT                   ECO:0000269|PubMed:16840321"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000269|PubMed:10618374,
FT                   ECO:0000269|PubMed:1850017, ECO:0000269|PubMed:1851815"
FT   MUTAGEN         2
FT                   /note="G->A: 100% loss of myristoylation. Impaired viral
FT                   assembly."
FT                   /evidence="ECO:0000269|PubMed:1851815"
FT   MUTAGEN         3
FT                   /note="A->D: 50% loss of myristoylation. Severe reduction
FT                   in specific infectivity."
FT                   /evidence="ECO:0000269|PubMed:1850017"
FT   MUTAGEN         3
FT                   /note="A->G,L,V: No effect on myristoylation and virus
FT                   growth."
FT                   /evidence="ECO:0000269|PubMed:1850017"
FT   MUTAGEN         3
FT                   /note="A->H: No effect on myristoylation. Severe reduction
FT                   in specific infectivity."
FT                   /evidence="ECO:0000269|PubMed:1850017"
FT   MUTAGEN         264
FT                   /note="H->G,T: Complete loss of VP0 cleavage."
FT                   /evidence="ECO:0000269|PubMed:10516013"
FT   MUTAGEN         901
FT                   /note="H->A: Complete loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:1649327"
FT   MUTAGEN         919
FT                   /note="D->A: Complete loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:1649327"
FT   MUTAGEN         936
FT                   /note="C->S: Complete loss of autocatalytic activity of
FT                   protease 2A. Complete loss of polyprotein cleavage."
FT                   /evidence="ECO:0000269|PubMed:1310193"
FT   MUTAGEN         938
FT                   /note="C->S,N,T: Complete loss of autocatalytic activity of
FT                   protease 2A. Complete loss of polyprotein cleavage."
FT                   /evidence="ECO:0000269|PubMed:1310193"
FT   MUTAGEN         945
FT                   /note="C->N,S: Almost no effect on the autocatalytic
FT                   activity of protease 2A. Almost no effect on polyprotein
FT                   cleavage."
FT                   /evidence="ECO:0000269|PubMed:1310193"
FT   MUTAGEN         990
FT                   /note="C->A: Complete loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:1649327"
FT   MUTAGEN         990
FT                   /note="C->S: 90% loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:1649327"
FT   MUTAGEN         996
FT                   /note="C->H,P,S,Y: Complete loss of autocatalytic activity
FT                   of protease 2A. Complete loss of polyprotein cleavage."
FT                   /evidence="ECO:0000269|PubMed:1310193"
FT   MUTAGEN         997
FT                   /note="H->R: No effect on catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:1649327"
FT   MUTAGEN         998
FT                   /note="H->A: 95% loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:1649327"
FT   MUTAGEN         998
FT                   /note="H->Q: Complete loss of autocatalytic activity of
FT                   protease 2A. Complete loss of polyprotein cleavage."
FT                   /evidence="ECO:0000269|PubMed:1310193"
FT   MUTAGEN         1262
FT                   /note="K->A: Complete loss of protein 2CATPase activity."
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   MUTAGEN         1268
FT                   /note="L->R: 95% loss of protein 2CATPase activity."
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   MUTAGEN         1272
FT                   /note="A->R: 80% loss of protein 2CATPase activity."
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   MUTAGEN         1304
FT                   /note="D->A: Complete loss of protein 2CATPase activity."
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   MUTAGEN         1350
FT                   /note="N->A: Complete loss of protein 2CATPase activity."
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   MUTAGEN         1368
FT                   /note="R->A: Complete loss of protein 2CATPase activity."
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   MUTAGEN         1396
FT                   /note="C->A: 78% loss of 2CATPase activity."
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   MUTAGEN         1399
FT                   /note="C->A: 30% loss of 2CATPase activity."
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   MUTAGEN         1405
FT                   /note="F->R: 80% loss of protein 2CATPase activity."
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   MUTAGEN         1408
FT                   /note="C->A: 87% loss of 2CATPase activity."
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   MUTAGEN         1411
FT                   /note="L->R: 80% loss of protein 2CATPase activity."
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   MUTAGEN         1413
FT                   /note="C->A: 90% loss of 2CATPase activity."
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   MUTAGEN         1450
FT                   /note="C->A: No effect on 2CATPase activity and on
FT                   oligomerization."
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   MUTAGEN         1451
FT                   /note="M->A: 90% loss of 2CATPase activity."
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   MUTAGEN         1454
FT                   /note="L->A: Complete loss of 2CATPase activity."
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   MUTAGEN         1455
FT                   /note="F->A: Almost complete loss of 2CATPase activity."
FT                   /evidence="ECO:0000269|PubMed:30231078"
FT   MUTAGEN         1636
FT                   /note="E->Q: Complete loss of catalytic activity; when
FT                   associated with S-1712."
FT                   /evidence="ECO:0000269|PubMed:8097606"
FT   MUTAGEN         1712
FT                   /note="C->S: Complete loss of catalytic activity; when
FT                   associated with Q-1636."
FT                   /evidence="ECO:0000269|PubMed:8097606"
FT   CONFLICT        242..264
FT                   /note="RFCPVDYLLGNGTLLGNAFVFPH -> SSARWITSLEMARCWGMPLCSA
FT                   (in Ref. 2; CAA24446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="I -> L (in Ref. 2; CAA24446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        309
FT                   /note="A -> V (in Ref. 2; CAA24446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        420..422
FT                   /note="DDP -> AAS (in Ref. 2; CAA24446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        464
FT                   /note="F -> S (in Ref. 2; CAA24446 and 3; AMS03992)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        515
FT                   /note="T -> S (in Ref. 2; CAA24446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        674
FT                   /note="P -> S (in Ref. 3; AMS03992)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        855..856
FT                   /note="AV -> QL (in Ref. 2; CAA24446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        906
FT                   /note="D -> E (in Ref. 3; AMS03992)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        972
FT                   /note="A -> V (in Ref. 2; CAA24446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        985
FT                   /note="A -> E (in Ref. 2; CAA24446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1052
FT                   /note="S -> G (in Ref. 3; AMS03992)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1140..1141
FT                   /note="NA -> QR (in Ref. 2; CAA24446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1619
FT                   /note="V -> A (in Ref. 2; CAA24446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1626..1627
FT                   /note="AL -> VF (in Ref. 2; CAA24446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1635
FT                   /note="L -> F (in Ref. 2; CAA24446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1682
FT                   /note="G -> R (in Ref. 2; CAA24446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1722..1730
FT                   /note="VIGMHVGGN -> SSGCMLVD (in Ref. 2; CAA24446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1743
FT                   /note="Y -> L (in Ref. 2; CAA24446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1752
FT                   /note="Q -> P (in Ref. 2; CAA24446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1759..1760
FT                   /note="EV -> DA (in Ref. 2; CAA24446)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1840
FT                   /note="T -> I (in Ref. 2; CAA24446)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..7
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          17..23
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          26..29
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:1AL2"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           51..54
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           66..69
FT                   /evidence="ECO:0007829|PDB:1POV"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:1POV"
FT   STRAND          83..87
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          90..96
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:1POV"
FT   HELIX           103..105
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:6P9O"
FT   HELIX           126..128
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          138..141
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          147..151
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           153..155
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          156..158
FT                   /evidence="ECO:0007829|PDB:6P9W"
FT   HELIX           159..167
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          168..180
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          187..197
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          206..210
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           214..217
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           220..222
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          227..229
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          236..238
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           247..249
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   TURN            250..253
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           256..261
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          262..268
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   TURN            269..271
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          273..279
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          284..288
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   TURN            290..292
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          296..308
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          311..313
FT                   /evidence="ECO:0007829|PDB:1AR7"
FT   STRAND          315..332
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   TURN            349..352
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          364..366
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          380..383
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           384..388
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   TURN            400..404
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           406..409
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          411..414
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          423..428
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   TURN            430..432
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   TURN            434..438
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           440..445
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          448..453
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          455..461
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          463..466
FT                   /evidence="ECO:0007829|PDB:6P9W"
FT   STRAND          470..476
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          478..480
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           486..489
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          492..498
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          500..502
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          504..509
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          514..521
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           524..526
FT                   /evidence="ECO:0007829|PDB:1POV"
FT   STRAND          530..537
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          542..544
FT                   /evidence="ECO:0007829|PDB:6P9O"
FT   STRAND          547..557
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          562..566
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          570..572
FT                   /evidence="ECO:0007829|PDB:1POV"
FT   STRAND          586..589
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          594..596
FT                   /evidence="ECO:0007829|PDB:2PLV"
FT   HELIX           626..628
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           636..638
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           652..654
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           656..660
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          664..673
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          676..678
FT                   /evidence="ECO:0007829|PDB:6P9O"
FT   HELIX           681..683
FT                   /evidence="ECO:0007829|PDB:6P9O"
FT   STRAND          685..688
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          693..695
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           696..701
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          704..721
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          723..725
FT                   /evidence="ECO:0007829|PDB:1AR7"
FT   STRAND          733..739
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           752..755
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          757..759
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          761..765
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          771..775
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          780..786
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          790..793
FT                   /evidence="ECO:0007829|PDB:1POV"
FT   STRAND          796..799
FT                   /evidence="ECO:0007829|PDB:1POV"
FT   TURN            801..804
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   HELIX           812..814
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          818..823
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          827..830
FT                   /evidence="ECO:0007829|PDB:6P9W"
FT   STRAND          832..850
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   TURN            856..859
FT                   /evidence="ECO:0007829|PDB:6PSZ"
FT   STRAND          860..863
FT                   /evidence="ECO:0007829|PDB:1HXS"
FT   STRAND          1250..1255
FT                   /evidence="ECO:0007829|PDB:5Z3Q"
FT   HELIX           1262..1276
FT                   /evidence="ECO:0007829|PDB:5Z3Q"
FT   STRAND          1281..1284
FT                   /evidence="ECO:0007829|PDB:5Z3Q"
FT   STRAND          1298..1305
FT                   /evidence="ECO:0007829|PDB:5Z3Q"
FT   HELIX           1312..1320
FT                   /evidence="ECO:0007829|PDB:5Z3Q"
FT   STRAND          1321..1324
FT                   /evidence="ECO:0007829|PDB:5Z3Q"
FT   HELIX           1333..1335
FT                   /evidence="ECO:0007829|PDB:5Z3Q"
FT   STRAND          1343..1351
FT                   /evidence="ECO:0007829|PDB:5Z3Q"
FT   HELIX           1366..1368
FT                   /evidence="ECO:0007829|PDB:5Z3Q"
FT   STRAND          1370..1377
FT                   /evidence="ECO:0007829|PDB:5Z3Q"
FT   HELIX           1379..1381
FT                   /evidence="ECO:0007829|PDB:5Z3Q"
FT   HELIX           1389..1392
FT                   /evidence="ECO:0007829|PDB:5Z3Q"
FT   STRAND          1403..1407
FT                   /evidence="ECO:0007829|PDB:5Z3Q"
FT   TURN            1410..1412
FT                   /evidence="ECO:0007829|PDB:5Z3Q"
FT   STRAND          1413..1421
FT                   /evidence="ECO:0007829|PDB:5Z3Q"
FT   TURN            1422..1424
FT                   /evidence="ECO:0007829|PDB:5Z3Q"
FT   HELIX           1430..1454
FT                   /evidence="ECO:0007829|PDB:5Z3Q"
FT   HELIX           1474..1484
FT                   /evidence="ECO:0007829|PDB:6HLV"
FT   HELIX           1487..1495
FT                   /evidence="ECO:0007829|PDB:6HLV"
FT   STRAND          1498..1501
FT                   /evidence="ECO:0007829|PDB:6HLV"
FT   HELIX           1503..1505
FT                   /evidence="ECO:0007829|PDB:6HLV"
FT   STRAND          1507..1511
FT                   /evidence="ECO:0007829|PDB:6HLV"
FT   STRAND          1546..1550
FT                   /evidence="ECO:0007829|PDB:2BBL"
FT   STRAND          1556..1558
FT                   /evidence="ECO:0007829|PDB:2BBL"
FT   HELIX           1560..1564
FT                   /evidence="ECO:0007829|PDB:2BBL"
FT   HELIX           1567..1579
FT                   /evidence="ECO:0007829|PDB:4DCD"
FT   STRAND          1580..1585
FT                   /evidence="ECO:0007829|PDB:4DCD"
FT   STRAND          1588..1597
FT                   /evidence="ECO:0007829|PDB:4DCD"
FT   STRAND          1599..1603
FT                   /evidence="ECO:0007829|PDB:4DCD"
FT   HELIX           1604..1606
FT                   /evidence="ECO:0007829|PDB:4DCD"
FT   STRAND          1610..1614
FT                   /evidence="ECO:0007829|PDB:4DCD"
FT   STRAND          1617..1628
FT                   /evidence="ECO:0007829|PDB:4DCD"
FT   STRAND          1634..1645
FT                   /evidence="ECO:0007829|PDB:4DCD"
FT   HELIX           1652..1654
FT                   /evidence="ECO:0007829|PDB:4DCD"
FT   STRAND          1662..1669
FT                   /evidence="ECO:0007829|PDB:4DCD"
FT   STRAND          1671..1674
FT                   /evidence="ECO:0007829|PDB:4DCD"
FT   STRAND          1677..1692
FT                   /evidence="ECO:0007829|PDB:4DCD"
FT   STRAND          1695..1705
FT                   /evidence="ECO:0007829|PDB:4DCD"
FT   STRAND          1715..1718
FT                   /evidence="ECO:0007829|PDB:4DCD"
FT   STRAND          1721..1729
FT                   /evidence="ECO:0007829|PDB:4DCD"
FT   STRAND          1734..1738
FT                   /evidence="ECO:0007829|PDB:4DCD"
FT   HELIX           1741..1744
FT                   /evidence="ECO:0007829|PDB:4DCD"
FT   STRAND          1750..1756
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   TURN            1757..1761
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   TURN            1763..1766
FT                   /evidence="ECO:0007829|PDB:1RDR"
FT   HELIX           1770..1772
FT                   /evidence="ECO:0007829|PDB:1RDR"
FT   TURN            1777..1781
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   STRAND          1786..1788
FT                   /evidence="ECO:0007829|PDB:4K4S"
FT   STRAND          1792..1794
FT                   /evidence="ECO:0007829|PDB:4K4S"
FT   HELIX           1802..1807
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   HELIX           1820..1834
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   TURN            1835..1837
FT                   /evidence="ECO:0007829|PDB:2IM0"
FT   HELIX           1845..1850
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   STRAND          1860..1862
FT                   /evidence="ECO:0007829|PDB:4NLR"
FT   TURN            1866..1872
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   HELIX           1875..1878
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   TURN            1881..1884
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   HELIX           1887..1895
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   STRAND          1902..1906
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   STRAND          1910..1912
FT                   /evidence="ECO:0007829|PDB:4K4S"
FT   HELIX           1913..1917
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   STRAND          1923..1926
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   HELIX           1929..1948
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   TURN            1952..1955
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   HELIX           1962..1965
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   TURN            1966..1968
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   HELIX           1969..1972
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   STRAND          1975..1978
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   STRAND          1981..1984
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   HELIX           1985..1988
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   HELIX           1991..2003
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   TURN            2004..2006
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   HELIX           2007..2010
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   HELIX           2011..2017
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   STRAND          2018..2023
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   STRAND          2026..2032
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   STRAND          2036..2038
FT                   /evidence="ECO:0007829|PDB:4NLV"
FT   HELIX           2041..2060
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   STRAND          2061..2063
FT                   /evidence="ECO:0007829|PDB:4K4V"
FT   HELIX           2066..2068
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   STRAND          2070..2074
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   STRAND          2077..2084
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   HELIX           2088..2097
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   STRAND          2102..2104
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   TURN            2105..2107
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   TURN            2116..2118
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   STRAND          2124..2128
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   STRAND          2130..2132
FT                   /evidence="ECO:0007829|PDB:1TQL"
FT   STRAND          2135..2139
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   HELIX           2142..2149
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   STRAND          2151..2153
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   HELIX           2155..2157
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   HELIX           2158..2169
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   HELIX           2170..2172
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   HELIX           2174..2184
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   HELIX           2188..2191
FT                   /evidence="ECO:0007829|PDB:1RA6"
FT   HELIX           2198..2208
FT                   /evidence="ECO:0007829|PDB:1RA6"
SQ   SEQUENCE   2209 AA;  246540 MW;  DF1754F87F2E97D6 CRC64;
     MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYRDSASNA ASKQDFSQDP SKFTEPIKDV
     LIKTAPMLNS PNIEACGYSD RVLQLTLGNS TITTQEAANS VVAYGRWPEY LRDSEANPVD
     QPTEPDVAAC RFYTLDTVSW TKESRGWWWK LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ
     CNASKFHQGA LGVFAVPEMC LAGDSNTTTM HTSYQNANPG EKGGTFTGTF TPDNNQTSPA
     RRFCPVDYLL GNGTLLGNAF VFPHQIINLR TNNCATLVLP YVNSLSIDSM VKHNNWGIAI
     LPLAPLNFAS ESSPEIPITL TIAPMCCEFN GLRNITLPRL QGLPVMNTPG SNQYLTADNF
     QSPCALPEFD VTPPIDIPGE VKNMMELAEI DTMIPFDLSA TKKNTMEMYR VRLSDKPHTD
     DPILCLSLSP ASDPRLSHTM LGEILNYYTH WAGSLKFTFL FCGFMMATGK LLVSYAPPGA
     DPPKKRKEAM LGTHVIWDIG LQSSCTMVVP WISNTTYRQT IDDSFTEGGY ISVFYQTRIV
     VPLSTPREMD ILGFVSACND FSVRLLRDTT HIEQKALAQG LGQMLESMID NTVRETVGAA
     TSRDALPNTE ASGPTHSKEI PALTAVETGA TNPLVPSDTV QTRHVVQHRS RSESSIESFF
     ARGACVTIMT VDNPASTTNK DKLFAVWKIT YKDTVQLRRK LEFFTYSRFD MELTFVVTAN
     FTETNNGHAL NQVYQIMYVP PGAPVPEKWD DYTWQTSSNP SIFYTYGTAP ARISVPYVGI
     SNAYSHFYDG FSKVPLKDQS AALGDSLYGA ASLNDFGILA VRVVNDHNPT KVTSKIRVYL
     KPKHIRVWCP RPPRAVAYYG PGVDYKDGTL TPLSTKDLTT YGFGHQNKAV YTAGYKICNY
     HLATQDDLQN AVNVMWSRDL LVTESRAQGT DSIARCNCNA GVYYCESRRK YYPVSFVGPT
     FQYMEANNYY PARYQSHMLI GHGFASPGDC GGILRCHHGV IGIITAGGEG LVAFSDIRDL
     YAYEEEAMEQ GITNYIESLG AAFGSGFTQQ ISDKITELTN MVTSTITEKL LKNLIKIISS
     LVIITRNYED TTTVLATLAL LGCDASPWQW LRKKACDVLE IPYVIKQGDS WLKKFTEACN
     AAKGLEWVSN KISKFIDWLK EKIIPQARDK LEFVTKLRQL EMLENQISTI HQSCPSQEHQ
     EILFNNVRWL SIQSKRFAPL YAVEAKRIQK LEHTINNYIQ FKSKHRIEPV CLLVHGSPGT
     GKSVATNLIA RAIAERENTS TYSLPPDPSH FDGYKQQGVV IMDDLNQNPD GADMKLFCQM
     VSTVEFIPPM ASLEEKGILF TSNYVLASTN SSRISPPTVA HSDALARRFA FDMDIQVMNE
     YSRDGKLNMA MATEMCKNCH QPANFKRCCP LVCGKAIQLM DKSSRVRYSI DQITTMIINE
     RNRRSNIGNC MEALFQGPLQ YKDLKIDIKT SPPPECINDL LQAVDSQEVR DYCEKKGWIV
     NITSQVQTER NINRAMTILQ AVTTFAAVAG VVYVMYKLFA GHQGAYTGLP NKKPNVPTIR
     TAKVQGPGFD YAVAMAKRNI VTATTSKGEF TMLGVHDNVA ILPTHASPGE SIVIDGKEVE
     ILDAKALEDQ AGTNLEITII TLKRNEKFRD IRPHIPTQIT ETNDGVLIVN TSKYPNMYVP
     VGAVTEQGYL NLGGRQTART LMYNFPTRAG QCGGVITCTG KVIGMHVGGN GSHGFAAALK
     RSYFTQSQGE IQWMRPSKEV GYPIINAPSK TKLEPSAFHY VFEGVKEPAV LTKNDPRLKT
     DFEEAIFSKY VGNKITEVDE YMKEAVDHYA GQLMSLDINT EQMCLEDAMY GTDGLEALDL
     STSAGYPYVA MGKKKRDILN KQTRDTKEMQ KLLDTYGINL PLVTYVKDEL RSKTKVEQGK
     SRLIEASSLN DSVAMRMAFG NLYAAFHKNP GVITGSAVGC DPDLFWSKIP VLMEEKLFAF
     DYTGYDASLS PAWFEALKMV LEKIGFGDRV DYIDYLNHSH HLYKNKTYCV KGGMPSGCSG
     TSIFNSMINN LIIRTLLLKT YKGIDLDHLK MIAYGDDVIA SYPHEVDASL LAQSGKDYGL
     TMTPADKSAT FETVTWENVT FLKRFFRADE KYPFLIHPVM PMKEIHESIR WTKDPRNTQD
     HVRSLCLLAW HNGEEEYNKF LAKIRSVPIG RALLLPEYST LYRRWLDSF
//