POLG_POL1M
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 03-AUG-2022, entry version 225.
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; 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 (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 [35]
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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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 [41]
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 [42]
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 [43]
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 [44]
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 [45]
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 [46]
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 [47]
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 [48]
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 [49]
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 [50]
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 [51]
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 [52]
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 [53]
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 [54]
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 [55]
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 [56]
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 [57]
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 [58]
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 [59]
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 [60]
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 [61]
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 [62]
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 [63]
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 [64]
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 [65]
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 [66]
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 [67]
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 [68] {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 [69] {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 [70] {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 [71] {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 [72] {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 DDX58/RIG-I 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).
CC {ECO:0000250|UniProtKB:P03303, ECO:0000269|PubMed:18572216,
CC ECO:0000269|PubMed:18632855, ECO:0000269|PubMed:24390337,
CC 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 SMR; P03300; -.
DR ELM; P03300; -.
DR IntAct; P03300; 4.
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 PRIDE; 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:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IDA:CACAO.
DR GO; GO:0005198; F:structural molecule activity; 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:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0044694; P:pore-mediated entry of viral genome into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039690; P:positive stranded viral RNA replication; IDA:UniProtKB.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; 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:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IDA:UniProtKB.
DR GO; GO:0019068; P:virion assembly; IDA:UniProtKB.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR CDD; cd00205; rhv_like; 3.
DR Gene3D; 2.40.10.10; -; 4.
DR Gene3D; 2.60.120.20; -; 3.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 6.10.20.20; -; 1.
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; SSF50494; SSF50494; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF89043; SSF89043; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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 2C ATPase activity."
FT /evidence="ECO:0000269|PubMed:30231078"
FT MUTAGEN 1268
FT /note="L->R: 95% loss of protein 2C ATPase activity."
FT /evidence="ECO:0000269|PubMed:30231078"
FT MUTAGEN 1272
FT /note="A->R: 80% loss of protein 2C ATPase activity."
FT /evidence="ECO:0000269|PubMed:30231078"
FT MUTAGEN 1304
FT /note="D->A: Complete loss of protein 2C ATPase activity."
FT /evidence="ECO:0000269|PubMed:30231078"
FT MUTAGEN 1350
FT /note="N->A: Complete loss of protein 2C ATPase activity."
FT /evidence="ECO:0000269|PubMed:30231078"
FT MUTAGEN 1368
FT /note="R->A: Complete loss of protein 2C ATPase activity."
FT /evidence="ECO:0000269|PubMed:30231078"
FT MUTAGEN 1396
FT /note="C->A: 78% loss of 2C ATPase activity."
FT /evidence="ECO:0000269|PubMed:30231078"
FT MUTAGEN 1399
FT /note="C->A: 30% loss of 2C ATPase activity."
FT /evidence="ECO:0000269|PubMed:30231078"
FT MUTAGEN 1405
FT /note="F->R: 80% loss of protein 2C ATPase activity."
FT /evidence="ECO:0000269|PubMed:30231078"
FT MUTAGEN 1408
FT /note="C->A: 87% loss of 2C ATPase activity."
FT /evidence="ECO:0000269|PubMed:30231078"
FT MUTAGEN 1411
FT /note="L->R: 80% loss of protein 2C ATPase activity."
FT /evidence="ECO:0000269|PubMed:30231078"
FT MUTAGEN 1413
FT /note="C->A: 90% loss of 2C ATPase activity."
FT /evidence="ECO:0000269|PubMed:30231078"
FT MUTAGEN 1450
FT /note="C->A: No effect on 2C ATPase activity and on
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:30231078"
FT MUTAGEN 1451
FT /note="M->A: 90% loss of 2C ATPase activity."
FT /evidence="ECO:0000269|PubMed:30231078"
FT MUTAGEN 1454
FT /note="L->A: Complete loss of 2C ATPase activity."
FT /evidence="ECO:0000269|PubMed:30231078"
FT MUTAGEN 1455
FT /note="F->A: Almost complete loss of 2C ATPase 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
