ID   POLG_POL32              Reviewed;        2206 AA.
AC   P06209;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 194.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=P3;
DE   Contains:
DE     RecName: Full=Protein 3AB;
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=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   Poliovirus type 3 (strain 23127).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Ensavirinae; Enterovirus;
OC   Enterovirus coxsackiepol; Enterovirus C.
OX   NCBI_TaxID=12087;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3020156; DOI=10.1099/0022-1317-67-10-2093;
RA   Hughes P.J., Evans D.M.A., Minor P.D., Schild G.C., Almond J.W.,
RA   Stanway G.;
RT   "The nucleotide sequence of a type 3 poliovirus isolated during a recent
RT   outbreak of poliomyelitis in Finland.";
RL   J. Gen. Virol. 67:2093-2102(1986).
CC   -!- FUNCTION: [Capsid protein VP1]: 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). Capsid protein VP1 mainly forms the vertices of the capsid
CC       (By similarity). Capsid protein VP1 interacts with host cell receptor
CC       PVR to provide virion attachment to target host cells (By similarity).
CC       This attachment induces virion internalization predominantly through
CC       clathrin- and caveolin-independent endocytosis in Hela cells and
CC       through caveolin-mediated endocytosis in brain microvascular
CC       endothelial cells (By similarity). Tyrosine kinases are probably
CC       involved in the entry process (By similarity). Virus binding to PVR
CC       induces increased junctional permeability and rearrangement of
CC       junctional proteins (By similarity). Modulation of endothelial tight
CC       junctions, as well as cytolytic infection of endothelial cells
CC       themselves, may result in loss of endothelial integrity which may help
CC       the virus to reach the CNS (By similarity). After binding to its
CC       receptor, the capsid undergoes conformational changes (By similarity).
CC       Capsid protein VP1 N-terminus (that contains an amphipathic alpha-
CC       helix) and capsid protein VP4 are externalized (By similarity).
CC       Together, they shape a pore in the host membrane through which viral
CC       genome is translocated to host cell cytoplasm (By similarity).
CC       {ECO:0000250|UniProtKB:P03300}.
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       NUP98, NUP62 and NUP153 (By similarity). Counteracts stress granule
CC       formation probably by antagonizing its assembly or promoting its
CC       disassembly (By similarity). Cleaves and inhibits host IFIH1/MDA5,
CC       thereby inhibiting the type-I IFN production and the establishment of
CC       the antiviral state (By similarity). Cleaves and inhibits host MAVS,
CC       thereby inhibiting the type-I IFN production and the establishment of
CC       the antiviral state (By similarity). {ECO:0000250|UniProtKB:P03300,
CC       ECO:0000250|UniProtKB:P03301}.
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 (By
CC       similarity). This would result in depletion of MHC, trail receptors and
CC       IFN receptors at the host cell surface (By similarity). Plays an
CC       essential role in viral RNA replication by recruiting ACBD3 and PI4KB
CC       at the viral replication sites, thereby allowing the formation of the
CC       rearranged membranous structures where viral replication takes place
CC       (By similarity). {ECO:0000250|UniProtKB:P03300}.
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 (By similarity). Also cleaves
CC       host PABPC1, contributing to host translation shutoff (By similarity).
CC       Cleaves host RIGI and thus contributes to the inhibition of type I
CC       interferon production (By similarity). Cleaves host NLRP1, triggers
CC       host N-glycine-mediated degradation of the autoinhibitory NLRP1 N-
CC       terminal fragment (By similarity). Inhibits the integrated stress
CC       response (ISR) in the infected cell by cleaving host G3BP1 (By
CC       similarity). Stress granule formation is thus inhibited, which allows
CC       protein synthesis and viral replication (By similarity).
CC       {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03303}.
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       Interacts with human PVR (By similarity). Five protomers subsequently
CC       associate to form pentamers which serve as building blocks for the
CC       capsid (By similarity). Interacts with capsid protein VP2, capsid
CC       protein VP3 and capsid protein VP4 following cleavage of capsid protein
CC       VP0 (By similarity). {ECO:0000250|UniProtKB:P03300}.
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 (By similarity). Interacts (via GOLD domain) with host ACBD3 (via
CC       GOLD domain); this interaction allows the formation of a viral protein
CC       3A/ACBD3 heterotetramer with a 2:2 stoichiometry, which will stimulate
CC       the recruitment of host PI4KB in order to synthesize PI4P at the viral
CC       RNA replication sites (By similarity). {ECO:0000250|UniProtKB:P03300}.
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:0000250|UniProtKB:P03300}.
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}.
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DR   EMBL; X04468; CAA28155.1; -; Genomic_RNA.
DR   PIR; A27245; GNNY27.
DR   BMRB; P06209; -.
DR   SMR; P06209; -.
DR   IntAct; P06209; 1.
DR   MEROPS; C03.001; -.
DR   MEROPS; C03.020; -.
DR   MEROPS; N08.001; -.
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:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; 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:0039545; P:symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; IEA:UniProtKB-KW.
DR   GO; GO:0039554; P:symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity; IEA:UniProtKB-KW.
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; cd23213; Enterovirus_RdRp; 1.
DR   CDD; cd00205; rhv_like; 3.
DR   FunFam; 1.20.960.20:FF:000001; Genome polyprotein; 1.
DR   FunFam; 2.40.10.10:FF:000018; Genome polyprotein; 1.
DR   FunFam; 2.40.10.10:FF:000020; Genome polyprotein; 1.
DR   FunFam; 2.40.10.10:FF:000022; 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:000003; Genome polyprotein; 1.
DR   FunFam; 3.30.70.270:FF:000008; Genome polyprotein; 1.
DR   FunFam; 4.10.880.10:FF:000001; Genome polyprotein; 1.
DR   FunFam; 4.10.880.10:FF:000002; 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; 6.10.20.20; Poliovirus 3A protein-like; 1.
DR   Gene3D; 4.10.880.10; Poliovirus 3D polymerase Domain 1 (Nucleotidyltransferase); 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 4.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR   InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014838; P3A.
DR   InterPro; IPR036203; P3A_soluble_dom.
DR   InterPro; IPR044067; PCV_3C_PRO.
DR   InterPro; IPR000081; Peptidase_C3.
DR   InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR003138; Pico_P1A.
DR   InterPro; IPR002527; Pico_P2B.
DR   InterPro; IPR001676; Picornavirus_capsid.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR033703; Rhv-like.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF08727; P3A; 1.
DR   Pfam; PF00548; Peptidase_C3; 1.
DR   Pfam; PF02226; Pico_P1A; 1.
DR   Pfam; PF00947; Pico_P2A; 1.
DR   Pfam; PF01552; Pico_P2B; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   Pfam; PF00073; Rhv; 3.
DR   Pfam; PF00910; RNA_helicase; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF88633; Positive stranded ssRNA viruses; 2.
DR   SUPFAM; SSF89043; Soluble domain of poliovirus core protein 3a; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR   PROSITE; PS51874; PCV_3C_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51218; SF3_HELICASE_2; 1.
PE   3: Inferred from homology;
KW   Activation of host autophagy by virus; ATP-binding; Autocatalytic cleavage;
KW   Capsid protein;
KW   Clathrin- and caveolin-independent endocytosis of virus by host;
KW   Covalent protein-RNA linkage; DNA replication;
KW   Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host transcription 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 eukaryotic host transcription initiation by virus;
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; Repeat; RNA-binding; RNA-directed RNA polymerase;
KW   T=pseudo3 icosahedral capsid protein; Thiol protease; Transferase;
KW   Transport; Viral attachment to host cell; Viral immunoevasion;
KW   Viral ion channel; Viral penetration into host cytoplasm;
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..2206
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000426641"
FT   CHAIN           2..878
FT                   /note="P1"
FT                   /id="PRO_0000426642"
FT   CHAIN           2..340
FT                   /note="Capsid protein VP0"
FT                   /id="PRO_0000426643"
FT   CHAIN           2..69
FT                   /note="Capsid protein VP4"
FT                   /id="PRO_0000426644"
FT   CHAIN           70..340
FT                   /note="Capsid protein VP2"
FT                   /id="PRO_0000426645"
FT   CHAIN           341..578
FT                   /note="Capsid protein VP3"
FT                   /id="PRO_0000426646"
FT   CHAIN           579..878
FT                   /note="Capsid protein VP1"
FT                   /id="PRO_0000426647"
FT   CHAIN           879..1453
FT                   /note="P2"
FT                   /id="PRO_0000426648"
FT   CHAIN           879..1027
FT                   /note="Protease 2A"
FT                   /id="PRO_0000426649"
FT   CHAIN           1028..1124
FT                   /note="Protein 2B"
FT                   /id="PRO_0000040129"
FT   CHAIN           1125..1453
FT                   /note="Protein 2C"
FT                   /id="PRO_0000040130"
FT   CHAIN           1454..2206
FT                   /note="P3"
FT                   /id="PRO_0000426650"
FT   CHAIN           1454..1562
FT                   /note="Protein 3AB"
FT                   /id="PRO_0000426651"
FT   CHAIN           1454..1540
FT                   /note="Protein 3A"
FT                   /id="PRO_0000040131"
FT   CHAIN           1541..1562
FT                   /note="Viral protein genome-linked"
FT                   /id="PRO_0000426652"
FT   CHAIN           1563..2206
FT                   /note="Protein 3CD"
FT                   /id="PRO_0000426653"
FT   CHAIN           1563..1745
FT                   /note="Protease 3C"
FT                   /id="PRO_0000426654"
FT   CHAIN           1746..2206
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000426655"
FT   TOPO_DOM        2..1517
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        1518..1533
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1534..2206
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1229..1385
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1563..1741
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          1972..2087
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   ZN_FING         1393..1410
FT                   /note="C4-type"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          579..603
FT                   /note="Amphipathic alpha-helix"
FT                   /evidence="ECO:0000255"
FT   REGION          579..599
FT                   /note="Amphipathic alpha-helix"
FT                   /evidence="ECO:0000255"
FT   REGION          1125..1263
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1125..1197
FT                   /note="Membrane-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1146..1150
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1437..1444
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1448..1453
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        898
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        916
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        987
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        1602
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1633
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1709
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   BINDING         933
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         935
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         993
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         995
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         1253..1260
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   BINDING         1393
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1396
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1405
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1410
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1978
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         1978
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         2073
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         2073
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:0000250|UniProtKB:P03300"
FT   SITE            340..341
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            578..579
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            878..879
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1027..1028
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1124..1125
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1149
FT                   /note="Involved in the interaction with host RTN3"
FT                   /evidence="ECO:0000250|UniProtKB:Q66478"
FT   SITE            1453..1454
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1540..1541
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1562..1563
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1745..1746
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   MOD_RES         1543
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"
SQ   SEQUENCE   2206 AA;  245733 MW;  F226AD85403C37BA CRC64;
     MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYKDSASNA ASKQDYSQDP SKFTEPLKDV
     LIKTAPALNS PNVEACGYSD RVLQLTLGNS TITTQEAANS VVAYGRWPEF IRDDEANPVD
     QPTEPDVATS RFYTLDTVMW GKESRGWWWK LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ
     CNASKFHQGS LGVFAIPEFC LAGDSDTQRY TSYANANPGE KGGKFYAQFN KDTAVTSPKR
     EFCPVDYLLG CGVLIGNAFV FPHQIINLRT NNSATLVLPY VNALSIDSMV KHNNWGIAIL
     PLSPLDFAQD SSVEIPITVT IAPMCSEFNG LRNVTAPKLQ GLPVLNTPGS NQYLTSDNHQ
     SPCAIPEFDV TPPIDIPGEV KNVMELAEID TMIPLNLENT KRNTMDMYRV RLSDSANLSG
     PILCLSLSPA ADPRLSHTML GEVLNYYTHW AGSLKFTFLF CGSMMATGKL LVAYAPPGAQ
     PPTSRKEAML GTHVIWDLGL QSSCTMVVPW ISNVTYRQTT QDSFTEGGYI SMFYQTRIVV
     PLSTPKAMDM LGFVSACNDF SVRLLRDTTH ISQAAMPQGV DDLITEVAQN ALALSLPKPQ
     SNLPDTKASG PAHSKEVPTL TAVETGATNP LVPSDTVQTR HVIQQRSRSE STIESFFARG
     ACVAIIEVDN EQPATNVQKL FATWRITYKD TVQLRRKLEF FTYSRFDMEF TFVVTANFTN
     SNNGHALNQV YQIMYIPPGA PTPKSWDDYT WQTSSNPSIF YTYGAAPARI SVPYVGLANA
     YSHFYDGFAK VPLKSDANDQ VGDSLYSAMA VDDFGVLAIR VVNDHNPTKV TSKVRVYMKP
     KHVRVWCPRP PRAVPYYGPG VDYKDGLAPL SEKGLTTYGF GHQNKAVYTA GYKICNYHLA
     TQEDLQNAVS VMWNRDLLVT ESKAQGIDSI ARCNCSTGVY YCESRSRYYP VSFVGPTFQY
     MEANDYYPAR YQSHMLIGHG FASPGDCGGI LRCQHGVIGI ITAGGEGLVA FSDIRDLYAY
     EEEAMEQGIS SYVESLGAAF GSGFTQQIGD KIIELTGMVT STITEKLLKN LIKIVSSLVI
     ITRNYDDTTT VLATLALLGC DVSPWQWLKK KACDILEIPY VMRQGDSWLK KFTEACNAAK
     GLEWVSNKIS KFIDWLREKI IPQARDKLEF VTKLKQLEML ENQIATIHQS CPSQEHQEIL
     FNNVRWLSIQ SKRFAPLYAL EAKRIQKLEH TINNYIQFKS KHRIEPVCLL VHGSPGTGKS
     VATNLIARAI AEKENTSTYS LPPDPSHFDG YKQQGVVIMD DLNQNPDGAD MKLFCQMVST
     VEFIPPMASL EEKGILFTSN YVLASTNSSR ITPPTVAHSD ALARRFAFDM DIQVMSEYSR
     DGKLNMTMAT EMCKNCHQPA NFKRCCPLVC GKAIQLMDKS SRVRYSIDQI TTMIVNEKNR
     RSNIGNCMEA LFQGPLQYKD LKIDIKTTPP PECINDLLQA VDSQEVRDYC EKKGWIVNIT
     SQVQTERNIN RAMTILQAVT TFAAVAGVVY VMYKLFAGHQ GAYTGLPNKR PNVPTIRTAK
     VQGPGFDYAV AMAKRNILTA TTSKGEFTML GVHDNVAILP THASPGETIV IDGKEIEVLD
     AKALEDQAGT NLEITIVTLK RNEKFRDIRP HIPAQITETN DGVLIVNTSK YPNMYVPVGA
     VTEQGYLNLG GRQTARTLMY NFPTRAGQCG GVITCTGKVI GMHVGGNGSH GFAAALKRSY
     FTQSQGEIQW MRPSKEVGYP IINAPSKTKL EPSAFHYVFE GVKEPAVLTK NDPRFKTGFE
     EAIFSKYVGN KITEVDEYMK EAVDHYAGQL MSLDINTEQM CLEDAMYGTD GLEALDLSTS
     AGYPYVTMGK KKRDILNKQT RDTKEMQRLL DTYGINLPLV TYVKDELRSK TKVEQGKSRL
     IEASSLNDSV AMRMAFGNLY AAFHKNPGVV TGSAVGCDPD LFWSKIPVLM EEKLFAFDYT
     GYDASLSPAW FEALKMVLEK IGFGDRVDYI DYLNHSHHLY KNKTYCVKGG MPSGCSGTSI
     FNSMINNLII RTLLLKTYKG IDLDHLKMIA YGDDVIASYP HEVDASLLAQ SGKDYGLTMT
     PADKSATFET VTWENVTFLK RFFRADERYP FLIHPVMPMK EIHESIRWTK DPRNTQDHVR
     SLCLLAWHNG EDEYNKFLAM IRSVPIGRAL LLPEYSTLYR RWLDSF
//