ID   POLG_HRV14              Reviewed;        2179 AA.
AC   P03303; Q82083; Q82123; Q84736; Q84737; Q84738; Q84739; Q84740; Q84741;
AC   Q84774; Q84775; Q84776; Q84777; Q84778; Q84779; Q89441; Q89649; Q89763;
AC   Q89883;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 236.
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:0000250|UniProtKB:P03300};
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:0000250|UniProtKB:P03300};
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};
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   Human rhinovirus 14 (HRV-14).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Ensavirinae; Enterovirus;
OC   Enterovirus betarhino; Rhinovirus B.
OX   NCBI_TaxID=12131;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6093056; DOI=10.1093/nar/12.20.7859;
RA   Stanway G., Hughes P.J., Mountford R.C., Minor P.D., Almond J.W.;
RT   "The complete nucleotide sequence of a common cold virus: human rhinovirus
RT   14.";
RL   Nucleic Acids Res. 12:7859-7875(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND PROTEOLYTIC CLEAVAGE (CAPSID PROTEIN
RP   VP0).
RX   PubMed=8383233; DOI=10.1128/jvi.67.4.2110-2122.1993;
RA   Lee W.M., Monroe S., Rueckert R.R.;
RT   "Role of maturation cleavage in infectivity of picornaviruses: activation
RT   of an infectosome.";
RL   J. Virol. 67:2110-2122(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2983312; DOI=10.1073/pnas.82.3.732;
RA   Callahan P.L., Mizutani S., Colonno R.J.;
RT   "Molecular cloning and complete sequence determination of RNA genome of
RT   human rhinovirus type 14.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:732-736(1985).
RN   [4]
RP   FUNCTION (PROTEIN 3A), AND 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   [5]
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   [6]
RP   REVIEW.
RX   PubMed=20629045; DOI=10.1002/rmv.654;
RA   Fuchs R., Blaas D.;
RT   "Uncoating of human rhinoviruses.";
RL   Rev. Med. Virol. 20:281-297(2010).
RN   [7]
RP   REVIEW.
RX   PubMed=23227049; DOI=10.1155/2012/826301;
RA   Fuchs R., Blaas D.;
RT   "Productive entry pathways of human rhinoviruses.";
RL   Adv. Virol. 2012:826301-826301(2012).
RN   [8]
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   [9]
RP   FUNCTION (PROTEASE 3C), AND MUTAGENESIS OF CYS-1683.
RX   PubMed=33093214; DOI=10.1126/science.aay2002;
RA   Robinson K.S., Teo D.E.T., Tan K.S., Toh G.A., Ong H.H., Lim C.K., Lay K.,
RA   Au B.V., Lew T.S., Chu J.J.H., Chow V.T.K., Wang Y., Zhong F.L.,
RA   Reversade B.;
RT   "Enteroviral 3C protease activates the human NLRP1 inflammasome in airway
RT   epithelia.";
RL   Science 0:0-0(2020).
RN   [10]
RP   FUNCTION (PROTEASE 3C).
RX   PubMed=33410748; DOI=10.7554/elife.60609;
RA   Tsu B.V., Beierschmitt C., Ryan A.P., Agarwal R., Mitchell P.S.,
RA   Daugherty M.D.;
RT   "Diverse viral proteases activate the NLRP1 inflammasome.";
RL   Elife 10:0-0(2021).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=2993920; DOI=10.1038/317145a0;
RA   Rossman M.G., Arnold E., Erickson J.W., Frankenberger E.A., Griffith J.P.,
RA   Hecht H.-J., Johnson J.E., Kamer G., Luo M., Mosser A.G., Rueckert R.R.,
RA   Sherry B., Vriend G.;
RT   "Structure of a human common cold virus and functional relationship to
RT   other picornaviruses.";
RL   Nature 317:145-153(1985).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=2856083; DOI=10.1107/s0108767387011875;
RA   Arnold E., Rossman M.G.;
RT   "The use of molecular-replacement phases for the refinement of the human
RT   rhinovirus 14 structure.";
RL   Acta Crystallogr. A 44:270-282(1988).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=2156077; DOI=10.1016/0022-2836(90)90076-x;
RA   Arnold E., Rossman M.G.;
RT   "Analysis of the structure of a common cold virus, human rhinovirus 14,
RT   refined at a resolution of 3.0 A.";
RL   J. Mol. Biol. 211:763-801(1990).
RN   [14]
RP   STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF 70-856 IN COMPLEX WITH
RP   ICAM1, FUNCTION (CAPSID PROTEIN VP1), AND INTERACTION WITH HOST ICAM1
RP   (CAPSID PROTEIN VP1).
RX   PubMed=10562537; DOI=10.1093/emboj/18.22.6249;
RA   Kolatkar P.R., Bella J., Olson N.H., Bator C.M., Baker T.S., Rossmann M.G.;
RT   "Structural studies of two rhinovirus serotypes complexed with fragments of
RT   their cellular receptor.";
RL   EMBO J. 18:6249-6259(1999).
RN   [15]
RP   FUNCTION (PROTEASE 2A).
RX   PubMed=12163599; DOI=10.1128/jvi.76.17.8787-8796.2002;
RA   Gustin K.E., Sarnow P.;
RT   "Inhibition of nuclear import and alteration of nuclear pore complex
RT   composition by rhinovirus.";
RL   J. Virol. 76:8787-8796(2002).
RN   [16] {ECO:0007744|PDB:5W3E, ECO:0007744|PDB:5W3L, ECO:0007744|PDB:5W3M, ECO:0007744|PDB:5W3O}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.26 ANGSTROMS) OF 2-856, AND FUNCTION
RP   (CAPSID PROTEIN VP1).
RX   PubMed=28696310; DOI=10.1073/pnas.1707369114;
RA   Dong Y., Liu Y., Jiang W., Smith T.J., Xu Z., Rossmann M.G.;
RT   "Antibody-induced uncoating of human rhinovirus B14.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:8017-8022(2017).
RN   [17] {ECO:0007744|PDB:6HLT}
RP   X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 1430-1485, INTERACTION WITH HOST
RP   ACBD3 (PROTEIN 3A), AND FUNCTION (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. The capsid is 300
CC       Angstroms in diameter, composed of 60 copies of each capsid protein and
CC       enclosing the viral positive strand RNA genome (By similarity). Capsid
CC       protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1
CC       interacts with host ICAM1 to provide virion attachment to target host
CC       cells (PubMed:10562537). This attachment induces virion internalization
CC       (By similarity). Tyrosine kinases are probably involved in the entry
CC       process. After binding to its receptor, the capsid undergoes
CC       conformational changes (By similarity). Capsid protein VP1 N-terminus
CC       (that contains an amphipathic alpha-helix) and capsid protein VP4 are
CC       externalized (Probable). Together, they shape a pore in the host
CC       membrane through which viral genome is translocated to host cell
CC       cytoplasm (PubMed:28696310). After genome has been released, the
CC       channel shrinks. {ECO:0000250|UniProtKB:P03300,
CC       ECO:0000269|PubMed:10562537, ECO:0000269|PubMed:28696310,
CC       ECO:0000305|PubMed:28696310}.
CC   -!- FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo
CC       T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). 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 (By
CC       similarity). {ECO:0000250|UniProtKB:P03300}.
CC   -!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
CC       T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). 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 (By
CC       similarity). {ECO:0000250|UniProtKB:P03300}.
CC   -!- FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid
CC       shell (By similarity). After binding to the host receptor, the capsid
CC       undergoes conformational changes (By similarity). Capsid protein VP4 is
CC       released, Capsid protein VP1 N-terminus is externalized, and together,
CC       they shape a pore in the host membrane through which the viral genome
CC       is translocated into the host cell cytoplasm (By similarity).
CC       {ECO:0000250|UniProtKB:P03300}.
CC   -!- FUNCTION: [Capsid protein VP0]: Component of immature procapsids, which
CC       is cleaved into capsid proteins VP4 and VP2 after maturation (By
CC       similarity). Allows the capsid to remain inactive before the maturation
CC       step (By similarity). {ECO:0000250|UniProtKB:P03300}.
CC   -!- FUNCTION: [Protease 2A]: Cysteine protease that cleaves viral
CC       polyprotein and specific host proteins (By similarity). It is
CC       responsible for the autocatalytic cleavage between the P1 and P2
CC       regions, which is the first cleavage occurring in the polyprotein (By
CC       similarity). Also cleaves the host translation initiation factor
CC       EIF4G1, in order to shut down the capped cellular mRNA translation (By
CC       similarity). Inhibits the host nucleus-cytoplasm protein and RNA
CC       trafficking by cleaving host members of the nuclear pores including
CC       NUP62 and NUP153 (Probable). Counteracts stress granule formation
CC       probably by antagonizing its assembly or promoting its disassembly (By
CC       similarity). {ECO:0000250|UniProtKB:P03300,
CC       ECO:0000250|UniProtKB:P03301, ECO:0000305|PubMed:12163599}.
CC   -!- FUNCTION: [Protein 2B]: Plays an essential role in the virus
CC       replication cycle by acting as a viroporin. Creates a pore in the host
CC       endoplasmic reticulum and as a consequence releases Ca2+ in the
CC       cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium
CC       may trigger membrane trafficking and transport of viral ER-associated
CC       proteins to viroplasms, sites of viral genome replication.
CC       {ECO:0000250|UniProtKB:P03300}.
CC   -!- FUNCTION: [Protein 2C]: Induces and associates with structural
CC       rearrangements of intracellular membranes. Displays RNA-binding,
CC       nucleotide binding and NTPase activities. May play a role in virion
CC       morphogenesis and viral RNA encapsidation by interacting with the
CC       capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.
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:0000250|UniProtKB:P03300}.
CC   -!- FUNCTION: [Protein 3A]: Localizes the viral replication complex to the
CC       surface of membranous vesicles (By similarity). It inhibits host cell
CC       endoplasmic reticulum-to-Golgi apparatus transport and causes the
CC       disassembly of the Golgi complex, possibly through GBF1 interaction
CC       (PubMed:17005635). This would result in depletion of MHC, trail
CC       receptors and IFN receptors at the host cell surface (PubMed:17005635).
CC       Plays an essential role in viral RNA replication by recruiting ACBD3
CC       and PI4KB at the viral replication sites, thereby allowing the
CC       formation of the rearranged membranous structures where viral
CC       replication takes place (Probable). {ECO:0000250|UniProtKB:P03300,
CC       ECO:0000269|PubMed:17005635, ECO:0000305|PubMed:30755512,
CC       ECO:0000305|PubMed:31381608}.
CC   -!- FUNCTION: [Viral protein genome-linked]: Acts as a primer for viral RNA
CC       replication and remains covalently bound to viral genomic RNA. VPg is
CC       uridylylated prior to priming replication into VPg-pUpU. The oriI viral
CC       genomic sequence may act as a template for this. The VPg-pUpU is then
CC       used as primer on the genomic RNA poly(A) by the RNA-dependent RNA
CC       polymerase to replicate the viral genome. During genome replication,
CC       the VPg-RNA linkage is removed by the host TDP2, thereby accelerating
CC       replication. During the late stage of the replication cycle, host TDP2
CC       is excluded from sites of viral RNA synthesis and encapsidation,
CC       allowing for the generation of progeny virions.
CC       {ECO:0000250|UniProtKB:P03300}.
CC   -!- FUNCTION: [Protein 3CD]: Involved in the viral replication complex and
CC       viral polypeptide maturation. It exhibits protease activity with a
CC       specificity and catalytic efficiency that is different from protease
CC       3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the
CC       5'UTR of the viral genome. {ECO:0000250|UniProtKB:P03300}.
CC   -!- FUNCTION: [Protease 3C]: Major viral protease that mediates proteolytic
CC       processing of the polyprotein (By similarity). Cleaves host EIF5B,
CC       contributing to host translation shutoff (PubMed:18572216). Cleaves
CC       also host PABPC1, contributing to host translation shutoff (By
CC       similarity). Cleaves host NLRP1, triggers host N-glycine-mediated
CC       degradation of the autoinhibitory NLRP1 N-terminal fragment
CC       (PubMed:33093214, PubMed:33410748). {ECO:0000250|UniProtKB:P03300,
CC       ECO:0000269|PubMed:18572216, ECO:0000269|PubMed:33093214,
CC       ECO:0000269|PubMed:33410748}.
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:0000250|UniProtKB:P03300}.
CC   -!- CATALYTIC ACTIVITY: [Protein 2C]:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + phosphate + H(+); 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:0000250|UniProtKB:P03300};
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:0000250|UniProtKB:P03300};
CC   -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
CC       Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC         diphosphate; 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 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   -!- COFACTOR: [RNA-directed RNA polymerase]:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P03300};
CC       Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal
CC       center (By similarity). The magnesium ions are not prebound but only
CC       present for catalysis (By similarity). Requires the presence of 3CDpro
CC       or 3CPro (By similarity). {ECO:0000250|UniProtKB:P03300,
CC       ECO:0000250|UniProtKB:P03313};
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:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [Capsid protein VP0]: Interacts with capsid protein VP1 and
CC       capsid protein VP3 to form heterotrimeric protomers.
CC       {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [Capsid protein VP1]: Interacts with capsid protein VP0, and
CC       capsid protein VP3 to form heterotrimeric protomers (By similarity).
CC       Five protomers subsequently associate to form pentamers which serve as
CC       building blocks for the capsid (By similarity). Interacts with capsid
CC       protein VP2, capsid protein VP3 and capsid protein VP4 following
CC       cleavage of capsid protein VP0 (By similarity). Interacts with host
CC       ICAM1 (PubMed:10562537). {ECO:0000250|UniProtKB:P03300,
CC       ECO:0000269|PubMed:10562537}.
CC   -!- SUBUNIT: [Capsid protein VP2]: Interacts with capsid protein VP1 and
CC       capsid protein VP3 in the mature capsid.
CC       {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [Capsid protein VP3]: Interacts with capsid protein VP0 and
CC       capsid protein VP1 to form heterotrimeric protomers (By similarity).
CC       Five protomers subsequently associate to form pentamers which serve as
CC       building blocks for the capsid (By similarity). Interacts with capsid
CC       protein VP4 in the mature capsid (By similarity). Interacts with
CC       protein 2C; this interaction may be important for virion morphogenesis
CC       (By similarity). {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [Capsid protein VP4]: Interacts with capsid protein VP1 and
CC       capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.
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 (By similarity).
CC       Interacts (via N-terminus) with host RTN3 (via reticulon domain); this
CC       interaction is important for viral replication (By similarity).
CC       Interacts with capsid protein VP3; this interaction may be important
CC       for virion morphogenesis (By similarity).
CC       {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [Protein 3AB]: Interacts with protein 3CD.
CC       {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [Protein 3A]: Homodimer (By similarity). Interacts with host
CC       GBF1 (PubMed:17005635). Interacts with host ACBD3 (via GOLD domain);
CC       this interaction allows the formation of a viral protein 3A/ACBD3
CC       heterotetramer with a 2:2 stoichiometry, which will stimulate the
CC       recruitment of host PI4KB in order to synthesize PI4P at the viral RNA
CC       replication sites (PubMed:31381608). {ECO:0000250|UniProtKB:P03300,
CC       ECO:0000269|PubMed:17005635, ECO:0000269|PubMed:31381608}.
CC   -!- SUBUNIT: [Viral protein genome-linked]: Interacts with RNA-directed RNA
CC       polymerase. {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [Protein 3CD]: Interacts with protein 3AB and with RNA-
CC       directed RNA polymerase. {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [RNA-directed RNA polymerase]: Interacts with Viral protein
CC       genome-linked and with protein 3CD. {ECO:0000250|UniProtKB:P03300}.
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:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
CC       {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC       {ECO:0000250|UniProtKB:P03300}. 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:0000250|UniProtKB:P03300}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:Q66478}.
CC   -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm.
CC   -!- SUBCELLULAR LOCATION: [Protein 3CD]: Host nucleus
CC       {ECO:0000250|UniProtKB:P03300}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:P03300}. 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 (By
CC       similarity). The N-terminus also displays RNA-binding properties (By
CC       similarity). The N-terminus is involved in oligomerization (By
CC       similarity). The central part contains an ATPase domain and a C4-type
CC       zinc-finger (By similarity). The C-terminus is involved in RNA-binding
CC       (By similarity). The extreme C-terminus contains a region involved in
CC       oligomerization (By similarity). {ECO:0000250|UniProtKB:P03300}.
CC   -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the
CC       viral proteases yield processing intermediates and the mature proteins.
CC       {ECO:0000250|UniProtKB:P03300}.
CC   -!- PTM: [Capsid protein VP0]: Myristoylation is required for the formation
CC       of pentamers during virus assembly. Further assembly of 12 pentamers
CC       and a molecule of genomic RNA generates the provirion.
CC       {ECO:0000250|UniProtKB:P03300}.
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:8383233}.
CC   -!- PTM: [Capsid protein VP4]: Myristoylation is required during RNA
CC       encapsidation and formation of the mature virus particle.
CC       {ECO:0000250|UniProtKB:P03300}.
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:0000250|UniProtKB:P03300}.
CC   -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC       {ECO:0000305}.
CC   -!- CAUTION: The PDB data bank contains the 3D-structure coordinates of
CC       proteins VP1, VP2, VP3 and VP4. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=4rhv";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=2r04";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=2r06";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=2r07";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=2rm2";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=2rmu";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=2rr1";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=2rs1";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=2rs3";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=2rs5";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=2hwb";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=2hwc";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1vrh";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1rmu";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1ruc";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1rud";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1rue";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1ruf";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1rug";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1ruh";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1rui";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1ruj";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1rvf";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1r08";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1r09";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1ncq";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1na1";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1k5m";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1d3i";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure complexed with antiviral compound SCH 38057;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1hri";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure complexed with antiviral compound SDZ 35-682;
CC       URL="https://viperdb.org/Info_Page.php?VDB=1hrv";
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DR   EMBL; X01087; CAA25565.1; -; Genomic_RNA.
DR   EMBL; L05355; AAA45758.1; -; Genomic_RNA.
DR   EMBL; K02121; AAA45756.1; -; Genomic_RNA.
DR   PIR; A03901; GNNYH4.
DR   RefSeq; NP_041009.1; NC_001490.1.
DR   PDB; 1D3I; EM; 26.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 1HRI; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 1HRV; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 1K5M; X-ray; 2.70 A; A=568-856, B=70-331, C=332-567, D=2-69.
DR   PDB; 1NA1; X-ray; 3.30 A; A=568-856, B=70-331, C=332-567, D=2-69.
DR   PDB; 1NCQ; X-ray; 2.50 A; A=568-856, B=70-331, C=332-567, D=2-69.
DR   PDB; 1R08; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 1R09; X-ray; 2.90 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 1RMU; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 1RUC; X-ray; 3.10 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 1RUD; X-ray; 2.90 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 1RUE; X-ray; 2.90 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 1RUF; X-ray; 2.90 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 1RUG; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 1RUH; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 1RUI; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 1RUJ; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 1RVF; X-ray; 4.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 1VRH; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 1XR5; X-ray; 2.80 A; A=1720-2179.
DR   PDB; 2B0F; NMR; -; A=1538-1719.
DR   PDB; 2HWB; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 2HWC; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 2IN2; NMR; -; A=1538-1719.
DR   PDB; 2R04; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 2R06; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 2R07; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 2RM2; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 2RMU; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 2RR1; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 2RS1; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 2RS3; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 2RS5; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 4PDW; X-ray; 3.00 A; A=568-856, B=70-331, C=332-567.
DR   PDB; 4RHV; X-ray; 3.00 A; 1=568-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 5W3E; EM; 2.53 A; A=568-856, B=332-567, C=70-331, D=2-69.
DR   PDB; 5W3L; EM; 2.71 A; A=568-856, B=332-567, C=70-331, D=2-69.
DR   PDB; 5W3M; EM; 2.26 A; A=568-856, B=332-567, C=70-331, D=2-69.
DR   PDB; 5W3O; EM; 3.01 A; A=568-856, B=332-567, C=70-331.
DR   PDB; 6HLT; X-ray; 2.81 A; B/D=1430-1485.
DR   PDB; 6KYZ; X-ray; 1.84 A; A/D=1538-1719.
DR   PDB; 6KZ0; X-ray; 2.40 A; A/D/G/J=1538-1719.
DR   PDB; 7BG6; EM; 2.60 A; 1=584-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 7BG7; EM; 2.40 A; 1=564-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 7NUL; EM; 4.00 A; 1=564-856, 2=70-331, 3=332-563.
DR   PDB; 7NUM; EM; 3.90 A; 1=564-856, 2=70-331, 3=332-563.
DR   PDB; 7NUN; EM; 3.60 A; 1=564-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 7NUO; EM; 3.90 A; 1=564-856, 2=70-331, 3=332-563.
DR   PDB; 7NUQ; EM; 2.80 A; 1=564-856, 2=70-331, 3=332-567, 4=2-69.
DR   PDB; 8PNB; EM; 3.80 A; 1=627-856, 2=76-331, 3=332-567.
DR   PDB; 8PNF; EM; 2.90 A; 1=574-856, 2=76-331, 3=332-567, 4=23-69.
DR   PDB; 9LGP; X-ray; 2.11 A; A/B/C/D=1538-1719.
DR   PDB; 9U5P; EM; 2.96 A; A/O=1539-1718.
DR   PDB; 9U5Q; EM; 3.35 A; A=1539-1718.
DR   PDB; 9U5R; EM; 3.59 A; O=1539-1718.
DR   PDB; 9URM; EM; 4.24 A; A=1539-1718.
DR   PDB; 9WB3; EM; 3.17 A; A=1539-1718.
DR   PDB; 9WB4; EM; 3.32 A; A=1539-1718.
DR   AlphaFoldDB; P03303; -.
DR   BMRB; P03303; -.
DR   EMDB; EMD-12171; -.
DR   EMDB; EMD-12172; -.
DR   EMDB; EMD-12594; -.
DR   EMDB; EMD-12595; -.
DR   EMDB; EMD-12596; -.
DR   EMDB; EMD-12597; -.
DR   EMDB; EMD-12599; -.
DR   EMDB; EMD-17780; -.
DR   EMDB; EMD-17781; -.
DR   EMDB; EMD-63878; -.
DR   EMDB; EMD-63879; -.
DR   EMDB; EMD-63881; -.
DR   EMDB; EMD-65832; -.
DR   EMDB; EMD-65833; -.
DR   EMDB; EMD-8754; -.
DR   EMDB; EMD-8761; -.
DR   EMDB; EMD-8762; -.
DR   EMDB; EMD-8763; -.
DR   SMR; P03303; -.
DR   IntAct; P03303; 2.
DR   BindingDB; P03303; -.
DR   ChEMBL; CHEMBL4295564; -.
DR   DrugBank; DB08725; (S)-5-(7-(4-(4-Ethyl-4,5-dihydro-2-oxazolyl)phenoxy)heptyl)-3-methylisoxazole.
DR   DrugBank; DB08543; 1-[2-HYDROXY-3-(4-CYCLOHEXYL-PHENOXY)-PROPYL]-4-(2-PYRIDYL)-PIPERAZINE.
DR   DrugBank; DB08509; 1-[6-(2-CHLORO-4-METHYXYPHENOXY)-HEXYL]-IMIDAZOLE.
DR   DrugBank; DB08540; 2-[4-(2H-1,4-BENZOTHIAZINE-3-YL)-PIPERAZINE-1-LY]-1,3-THIAZOLE-4-CARBOXYLIC ACID ETHYLESTER.
DR   DrugBank; DB08017; 3-METHOXY-6-[4-(3-METHYLPHENYL)-1-PIPERAZINYL]PYRIDAZINE.
DR   DrugBank; DB08727; 3-Methyl-5-(7-{4-[(4R)-4-methyl-4,5-dihydro-1,3-oxazol-2-yl]phenoxy}heptyl)-1,2-oxazole.
DR   DrugBank; DB08728; 5-(3-(2,6-dichloro-4-(4,5-dihydro-2-oxazolyl)phenoxy)propyl)-3-methyl isoxazole.
DR   DrugBank; DB08721; 5-(5-(2,6-dichloro-4-(4,5-dihydro-2-oxazolyl)phenoxy)pentyl)-3-(hydroxyethyl oxymethyleneoxymethyl) isoxazole.
DR   DrugBank; DB08720; 5-(5-(4-(4,5-dihydro-2-oxazoly)phenoxy)pentyl)-3-methyl osoxazole.
DR   DrugBank; DB08724; 5-(5-(4-(5-hydro-4-methyl-2-oxazolyl)phenoxy)pentyl)-3-methyl isoxazole.
DR   DrugBank; DB08719; 5-(5-(6-CHLORO-4-(4,5-DIHYDRO-2-OXAZOLYL)PHENOXY)PENTYL)-3-METHYL ISOXAZOLE.
DR   DrugBank; DB08722; 5-(7-(6-chloro-4-(5-hydro-4-methyl-2-oxazolyl)phenoxy)heptyl)-3-methyl isoxazole.
DR   DrugBank; DB08726; Disoxaril.
DR   DrugBank; DB05102; Rupintrivir.
DR   DrugBank; DB03203; Sphingosine.
DR   DrugBank; DB08723; WIN-54954.
DR   MEROPS; C03.013; -.
DR   MEROPS; C03.020; -.
DR   MEROPS; N08.001; -.
DR   ABCD; P03303; 5 sequenced antibodies.
DR   DNASU; 1461213; -.
DR   GeneID; 1461213; -.
DR   KEGG; vg:1461213; -.
DR   BRENDA; 3.4.22.28; 12958.
DR   EvolutionaryTrace; P03303; -.
DR   Proteomes; UP000118299; Segment.
DR   GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR   GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; ISS:UniProtKB.
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:0015267; F:channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; ISS:UniProtKB.
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 RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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:0039664; P:lysis of host organelle involved in viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0044694; P:symbiont genome entry into host cell via pore formation in plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039520; P:symbiont-mediated activation of host autophagy; ISS:UniProtKB.
DR   GO; GO:0039540; P:symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity; IEA:UniProtKB-KW.
DR   GO; GO:0039522; P:symbiont-mediated suppression of host mRNA export from nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   CDD; cd00205; rhv_like; 3.
DR   FunFam; 1.20.960.20:FF:000001; Genome polyprotein; 1.
DR   FunFam; 2.60.120.20:FF:000001; Genome polyprotein; 1.
DR   FunFam; 2.60.120.20:FF:000002; Genome polyprotein; 1.
DR   FunFam; 2.60.120.20:FF:000004; Genome polyprotein; 1.
DR   FunFam; 3.30.70.270:FF:000008; Genome polyprotein; 1.
DR   Gene3D; 1.20.960.20; -; 1.
DR   Gene3D; 2.60.120.20; -; 3.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 4.10.80.10; Picornavirus coat protein VP4; 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; IPR003593; AAA+_ATPase.
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; IPR003138; Pico_P1A.
DR   InterPro; IPR036988; Pico_P1A_sf.
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   SMART; SM00382; AAA; 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.
DR   PDBsum; 1D3I; -.
DR   PDBsum; 1HRI; -.
DR   PDBsum; 1HRV; -.
DR   PDBsum; 1K5M; -.
DR   PDBsum; 1NA1; -.
DR   PDBsum; 1NCQ; -.
DR   PDBsum; 1R08; -.
DR   PDBsum; 1R09; -.
DR   PDBsum; 1RMU; -.
DR   PDBsum; 1RUC; -.
DR   PDBsum; 1RUD; -.
DR   PDBsum; 1RUE; -.
DR   PDBsum; 1RUF; -.
DR   PDBsum; 1RUG; -.
DR   PDBsum; 1RUH; -.
DR   PDBsum; 1RUI; -.
DR   PDBsum; 1RUJ; -.
DR   PDBsum; 1RVF; -.
DR   PDBsum; 1VRH; -.
DR   PDBsum; 1XR5; -.
DR   PDBsum; 2B0F; -.
DR   PDBsum; 2HWB; -.
DR   PDBsum; 2HWC; -.
DR   PDBsum; 2IN2; -.
DR   PDBsum; 2R04; -.
DR   PDBsum; 2R06; -.
DR   PDBsum; 2R07; -.
DR   PDBsum; 2RM2; -.
DR   PDBsum; 2RMU; -.
DR   PDBsum; 2RR1; -.
DR   PDBsum; 2RS1; -.
DR   PDBsum; 2RS3; -.
DR   PDBsum; 2RS5; -.
DR   PDBsum; 4PDW; -.
DR   PDBsum; 4RHV; -.
DR   PDBsum; 5W3E; -.
DR   PDBsum; 5W3L; -.
DR   PDBsum; 5W3M; -.
DR   PDBsum; 5W3O; -.
DR   PDBsum; 6HLT; -.
DR   PDBsum; 6KYZ; -.
DR   PDBsum; 6KZ0; -.
DR   PDBsum; 7BG6; -.
DR   PDBsum; 7BG7; -.
DR   PDBsum; 7NUL; -.
DR   PDBsum; 7NUM; -.
DR   PDBsum; 7NUN; -.
DR   PDBsum; 7NUO; -.
DR   PDBsum; 7NUQ; -.
DR   PDBsum; 8PNB; -.
DR   PDBsum; 8PNF; -.
DR   PDBsum; 9LGP; -.
DR   PDBsum; 9U5P; -.
DR   PDBsum; 9U5Q; -.
DR   PDBsum; 9U5R; -.
DR   PDBsum; 9URM; -.
DR   PDBsum; 9WB3; -.
DR   PDBsum; 9WB4; -.
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   DNA replication; Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host translation shutoff by virus; Helicase; Host cytoplasm;
KW   Host cytoplasmic vesicle; Host gene expression shutoff by virus;
KW   Host membrane; Host mRNA suppression by virus; Host nucleus;
KW   Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host mRNA nuclear export by virus;
KW   Inhibition of host RIG-I by virus; Inhibition of host RLR pathway by virus;
KW   Ion channel; Ion transport; Lipoprotein; 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;
KW   Viral penetration via lysis of host organellar membrane;
KW   Viral RNA replication; Virion; Virus endocytosis by host;
KW   Virus entry into host cell; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   CHAIN           2..2179
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000426536"
FT   CHAIN           2..856
FT                   /note="P1"
FT                   /id="PRO_0000426537"
FT   CHAIN           2..331
FT                   /note="Capsid protein VP0"
FT                   /id="PRO_0000426538"
FT   CHAIN           2..69
FT                   /note="Capsid protein VP4"
FT                   /id="PRO_0000426539"
FT   CHAIN           70..331
FT                   /note="Capsid protein VP2"
FT                   /id="PRO_0000426540"
FT   CHAIN           332..561
FT                   /note="Capsid protein VP3"
FT                   /id="PRO_0000426541"
FT   CHAIN           562..856
FT                   /note="Capsid protein VP1"
FT                   /id="PRO_0000426542"
FT   CHAIN           857..1429
FT                   /note="P2"
FT                   /id="PRO_0000426543"
FT   CHAIN           857..1002
FT                   /note="Protease 2A"
FT                   /id="PRO_0000040029"
FT   CHAIN           1003..1099
FT                   /note="Protein 2B"
FT                   /id="PRO_0000040030"
FT   CHAIN           1100..1429
FT                   /note="Protein 2C"
FT                   /id="PRO_0000426544"
FT   CHAIN           1430..2179
FT                   /note="P3"
FT                   /id="PRO_0000426545"
FT   CHAIN           1430..1537
FT                   /note="Protein 3AB"
FT                   /id="PRO_0000426546"
FT   CHAIN           1430..1514
FT                   /note="Protein 3A"
FT                   /id="PRO_0000040032"
FT   CHAIN           1515..1537
FT                   /note="Viral protein genome-linked"
FT                   /id="PRO_0000426547"
FT   CHAIN           1538..2179
FT                   /note="Protein 3CD"
FT                   /id="PRO_0000426548"
FT   CHAIN           1538..1719
FT                   /note="Protease 3C"
FT                   /id="PRO_0000426549"
FT   CHAIN           1720..2179
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000426550"
FT   TOPO_DOM        2..1491
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        1492..1507
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1508..2179
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1205..1361
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1538..1715
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          1946..2060
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   ZN_FING         1369..1386
FT                   /note="C4-type"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..584
FT                   /note="Amphipathic alpha-helix"
FT                   /evidence="ECO:0000255"
FT   REGION          1101..1239
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1101..1173
FT                   /note="Membrane-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1122..1126
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1413..1420
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1424..1429
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        876
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        894
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        965
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        1577
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1608
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1683
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   BINDING         911
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QF31"
FT   BINDING         913
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QF31"
FT   BINDING         971
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QF31"
FT   BINDING         973
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QF31"
FT   BINDING         1369
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1372
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1381
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1386
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1952
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic; for RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1952
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic; for RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         2046
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic; for RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         2046
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic; for RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   SITE            69..70
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000305|PubMed:8383233"
FT   SITE            331..332
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            561..562
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            856..857
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1002..1003
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1099..1100
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1125
FT                   /note="Involved in the interaction with host RTN3"
FT                   /evidence="ECO:0000250|UniProtKB:Q66478"
FT   SITE            1429..1430
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1514..1515
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1537..1538
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1719..1720
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   MOD_RES         1517
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   MUTAGEN         1683
FT                   /note="C->A: Inhibits protease 3C activity on host NLRP1."
FT                   /evidence="ECO:0000269|PubMed:33093214"
FT   CONFLICT        368
FT                   /note="P -> L (in Ref. 3; AAA45756)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        459
FT                   /note="I -> T (in Ref. 3; AAA45756)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        722
FT                   /note="P -> H (in Ref. 3; AAA45756)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        726..727
FT                   /note="NP -> KS (in Ref. 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        729..731
FT                   /note="EWD -> RVG (in Ref. 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        913
FT                   /note="C -> R (in Ref. 3; AAA45756)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        942
FT                   /note="N -> S (in Ref. 3; AAA45756)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        962
FT                   /note="P -> L (in Ref. 3; AAA45756)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        982
FT                   /note="G -> E (in Ref. 3; AAA45756)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1193
FT                   /note="L -> F (in Ref. 3; AAA45756)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1193
FT                   /note="L -> H (in Ref. 2; AAA45758)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1220
FT                   /note="I -> T (in Ref. 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1399
FT                   /note="I -> V (in Ref. 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1446
FT                   /note="P -> S (in Ref. 3; AAA45756)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1739
FT                   /note="P -> A (in Ref. 3; AAA45756)"
FT                   /evidence="ECO:0000305"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:1NCQ"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           51..54
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:5W3E"
FT   STRAND          83..87
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          90..96
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:5W3O"
FT   HELIX           103..105
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           106..108
FT                   /evidence="ECO:0007829|PDB:5W3L"
FT   HELIX           110..112
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   TURN            113..115
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           126..129
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           135..137
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          138..140
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          147..151
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           153..155
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           159..167
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          168..180
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          188..197
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           200..202
FT                   /evidence="ECO:0007829|PDB:5W3E"
FT   STRAND          203..205
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           209..212
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           213..216
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           219..221
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           225..227
FT                   /evidence="ECO:0007829|PDB:1K5M"
FT   HELIX           228..230
FT                   /evidence="ECO:0007829|PDB:5W3O"
FT   HELIX           238..240
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   TURN            241..244
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           247..252
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          253..259
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   TURN            260..262
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          264..270
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          275..279
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          281..284
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          287..298
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          307..323
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           326..330
FT                   /evidence="ECO:0007829|PDB:5W3E"
FT   HELIX           336..338
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   TURN            339..342
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          354..356
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           361..366
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          368..373
FT                   /evidence="ECO:0007829|PDB:5W3E"
FT   HELIX           374..377
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   TURN            386..389
FT                   /evidence="ECO:0007829|PDB:1R09"
FT   STRAND          390..392
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           395..398
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          399..402
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          410..415
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           421..423
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           427..432
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          435..440
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          442..448
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          455..463
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           468..470
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          471..473
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           474..477
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          479..485
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          487..489
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          491..496
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          501..503
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          505..508
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          509..512
FT                   /evidence="ECO:0007829|PDB:1K5M"
FT   STRAND          517..527
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          536..544
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          549..553
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          557..559
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           580..582
FT                   /evidence="ECO:0007829|PDB:1K5M"
FT   STRAND          585..587
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           604..606
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           608..610
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           614..616
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           630..632
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           634..637
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          642..651
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   TURN            660..664
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          665..670
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          673..676
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           677..683
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          686..702
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           709..713
FT                   /evidence="ECO:0007829|PDB:1RUG"
FT   STRAND          714..719
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          722..724
FT                   /evidence="ECO:0007829|PDB:2RM2"
FT   HELIX           725..727
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          729..731
FT                   /evidence="ECO:0007829|PDB:2HWB"
FT   HELIX           733..736
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          738..740
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          742..747
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          749..755
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          760..766
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          772..774
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          776..778
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          780..782
FT                   /evidence="ECO:0007829|PDB:1RUE"
FT   HELIX           784..786
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          790..795
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   STRAND          804..822
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           824..826
FT                   /evidence="ECO:0007829|PDB:5W3E"
FT   STRAND          832..834
FT                   /evidence="ECO:0007829|PDB:1NCQ"
FT   HELIX           842..844
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           847..849
FT                   /evidence="ECO:0007829|PDB:5W3M"
FT   HELIX           1446..1455
FT                   /evidence="ECO:0007829|PDB:6HLT"
FT   HELIX           1459..1467
FT                   /evidence="ECO:0007829|PDB:6HLT"
FT   STRAND          1470..1473
FT                   /evidence="ECO:0007829|PDB:6HLT"
FT   STRAND          1479..1482
FT                   /evidence="ECO:0007829|PDB:6HLT"
FT   HELIX           1542..1550
FT                   /evidence="ECO:0007829|PDB:6KYZ"
FT   STRAND          1552..1557
FT                   /evidence="ECO:0007829|PDB:6KYZ"
FT   STRAND          1560..1569
FT                   /evidence="ECO:0007829|PDB:6KYZ"
FT   STRAND          1571..1575
FT                   /evidence="ECO:0007829|PDB:6KYZ"
FT   HELIX           1576..1578
FT                   /evidence="ECO:0007829|PDB:6KYZ"
FT   STRAND          1582..1586
FT                   /evidence="ECO:0007829|PDB:6KYZ"
FT   STRAND          1589..1600
FT                   /evidence="ECO:0007829|PDB:6KYZ"
FT   TURN            1602..1604
FT                   /evidence="ECO:0007829|PDB:2B0F"
FT   STRAND          1606..1614
FT                   /evidence="ECO:0007829|PDB:6KYZ"
FT   HELIX           1624..1626
FT                   /evidence="ECO:0007829|PDB:6KYZ"
FT   STRAND          1635..1642
FT                   /evidence="ECO:0007829|PDB:6KYZ"
FT   STRAND          1645..1663
FT                   /evidence="ECO:0007829|PDB:6KYZ"
FT   STRAND          1666..1676
FT                   /evidence="ECO:0007829|PDB:6KYZ"
FT   HELIX           1680..1682
FT                   /evidence="ECO:0007829|PDB:6KYZ"
FT   STRAND          1686..1689
FT                   /evidence="ECO:0007829|PDB:6KYZ"
FT   STRAND          1692..1700
FT                   /evidence="ECO:0007829|PDB:6KYZ"
FT   STRAND          1702..1709
FT                   /evidence="ECO:0007829|PDB:6KYZ"
FT   HELIX           1712..1714
FT                   /evidence="ECO:0007829|PDB:6KYZ"
FT   STRAND          1721..1726
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           1728..1731
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           1748..1750
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           1773..1778
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           1791..1805
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           1812..1815
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           1816..1821
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   STRAND          1824..1826
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           1839..1842
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           1846..1849
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   TURN            1852..1855
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           1858..1867
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   STRAND          1873..1877
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           1884..1888
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   STRAND          1894..1897
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           1900..1906
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   TURN            1907..1909
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           1911..1919
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   TURN            1923..1926
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           1933..1936
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           1937..1939
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           1940..1943
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   STRAND          1949..1955
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           1957..1959
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           1962..1975
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   TURN            1978..1981
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           1982..1987
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   STRAND          1988..1992
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   STRAND          1994..2002
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   STRAND          2008..2010
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           2011..2030
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           2036..2038
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   STRAND          2040..2044
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   STRAND          2047..2051
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           2058..2065
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   TURN            2066..2069
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   TURN            2086..2088
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   STRAND          2094..2098
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   STRAND          2100..2102
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   STRAND          2105..2109
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           2112..2119
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   STRAND          2121..2124
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   TURN            2125..2127
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           2128..2139
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           2140..2142
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           2144..2154
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           2158..2162
FT                   /evidence="ECO:0007829|PDB:1XR5"
FT   HELIX           2168..2177
FT                   /evidence="ECO:0007829|PDB:1XR5"
SQ   SEQUENCE   2179 AA;  242991 MW;  827201A3032F0285 CRC64;
     MGAQVSTQKS GSHENQNILT NGSNQTFTVI NYYKDAASTS SAGQSLSMDP SKFTEPVKDL
     MLKGAPALNS PNVEACGYSD RVQQITLGNS TITTQEAANA VVCYAEWPEY LPDVDASDVN
     KTSKPDTSVC RFYTLDSKTW TTGSKGWCWK LPDALKDMGV FGQNMFFHSL GRSGYTVHVQ
     CNATKFHSGC LLVVVIPEHQ LASHEGGNVS VKYTFTHPGE RGIDLSSANE VGGPVKDVIY
     NMNGTLLGNL LIFPHQFINL RTNNTATIVI PYINSVPIDS MTRHNNVSLM VIPIAPLTVP
     TGATPSLPIT VTIAPMCTEF SGIRSKSIVP QGLPTTTLPG SGQFLTTDDR QSPSALPNYE
     PTPRIHIPGK VHNLLEIIQV DTLIPMNNTH TKDEVNSYLI PLNANRQNEQ VFGTNLFIGD
     GVFKTTLLGE IVQYYTHWSG SLRFSLMYTG PALSSAKLIL AYTPPGARGP QDRREAMLGT
     HVVWDIGLQS TIVMTIPWTS GVQFRYTDPD TYTSAGFLSC WYQTSLILPP ETTGQVYLLS
     FISACPDFKL RLMKDTQTIS QTVALTEGLG DELEEVIVEK TKQTVASISS GPKHTQKVPI
     LTANETGATM PVLPSDSIET RTTYMHFNGS ETDVECFLGR AACVHVTEIQ NKDATGIDNH
     REAKLFNDWK INLSSLVQLR KKLELFTYVR FDSEYTILAT ASQPDSANYS SNLVVQAMYV
     PPGAPNPKEW DDYTWQSASN PSVFFKVGDT SRFSVPYVGL ASAYNCFYDG YSHDDAETQY
     GITVLNHMGS MAFRIVNEHD EHKTLVKIRV YHRAKHVEAW IPRAPRALPY TSIGRTNYPK
     NTEPVIKKRK GDIKSYGLGP RYGGIYTSNV KIMNYHLMTP EDHHNLIAPY PNRDLAIVST
     GGHGAETIPH CNCTSGVYYS TYYRKYYPII CEKPTNIWIE GNPYYPSRFQ AGVMKGVGPA
     EPGDCGGILR CIHGPIGLLT AGGSGYVCFA DIRQLECIAE EQGLSDYITG LGRAFGVGFT
     DQISTKVTEL QEVAKDFLTT KVLSKVVKMV SALVIICRNH DDLVTVTATL ALLGCDGSPW
     RFLKMYISKH FQVPYIERQA NDGWFRKFND ACNAAKGLEW IANKISKLIE WIKNKVLPQA
     KEKLEFCSKL KQLDILERQI TTMHISNPTQ EKREQLFNNV LWLEQMSQKF APLYAVESKR
     IRELKNKMVN YMQFKSKQRI EPVCVLIHGT PGSGKSLTTS IVGRAIAEHF NSAVYSLPPD
     PKHFDGYQQQ EVVIMDDLNQ NPDGQDISMF CQMVSSVDFL PPMASLDNKG MLFTSNFVLA
     STNSNTLSPP TILNPEALVR RFGFDLDICL HTTYTKNGKL NAGMSTKTCK DCHQPSNFKK
     CCPLVCGKAI SLVDRTTNIR YSVDQLVTAI ISDFKSKMQI TDSLETLFQG PVYKDLEIDV
     CNTPPPECIN DLLKSVDSEE IREYCKKKKW IIPEIPTNIE RAMNQASMII NTILMFVSTL
     GIVYVIYKLF AQTQGPYSGN PPHNKLKAPT LRPVVVQGPN TEFALSLLRK NIMTITTSKG
     EFTGLGIHDR VCVIPTHAQP GDDVLVNGQK IRVKDKYKLV DPENINLELT VLTLDRNEKF
     RDIRGFISED LEGVDATLVV HSNNFTNTIL EVGPVTMAGL INLSSTPTNR MIRYDYATKT
     GQCGGVLCAT GKIFGIHVGG NGRQGFSAQL KKQYFVEKQG QVIARHKVRE FNINPVNTPT
     KSKLHPSVFY DVFPGDKEPA VLSDNDPRLE VKLTESLFSK YKGNVNTEPT ENMLVAVDHY
     AGQLLSLDIP TSELTLKEAL YGVDGLEPID ITTSAGFPYV SLGIKKRDIL NKETQDTEKM
     KFYLDKYGID LPLVTYIKDE LRSVDKVRLG KSRLIEASSL NDSVNMRMKL GNLYKAFHQN
     PGVLTGSAVG CDPDVFWSVI PCLMDGHLMA FDYSNFDASL SPVWFVCLEK VLTKLGFAGS
     SLIQSICNTH HIFRDEIYVV EGGMPSGCSG TSIFNSMINN IIIRTLILDA YKGIDLDKLK
     ILAYGDDLIV SYPYELDPQV LATLGKNYGL TITPPDKSET FTKMTWENLT FLKRYFKPDQ
     QFPFLVHPVM PMKDIHESIR WTKDPKNTQD HVRSLCMLAW HSGEKEYNEF IQKIRTTDIG
     KCLILPEYSV LRRRWLDLF
//