ID   POLG_POL1S              Reviewed;        2209 AA.
AC   P03301; Q84881; Q84882; Q84883; Q84884; Q84885; Q84886; Q84887; Q84888;
AC   Q84889; Q84890;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 193.
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   Poliovirus type 1 (strain Sabin).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Ensavirinae; Enterovirus; Enterovirus C.
OX   NCBI_TaxID=12082;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6310545; DOI=10.1073/pnas.79.19.5793;
RA   Nomoto A., Omata T., Toyoda H., Kuge S., Horie H., Kataoka Y., Genba Y.,
RA   Nakano Y., Imura N.;
RT   "Complete nucleotide sequence of the attenuated poliovirus Sabin 1 strain
RT   genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 79:5793-5797(1982).
RN   [2]
RP   PROTEIN SEQUENCE OF 882-905, PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN), AND
RP   FUNCTION (PROTEASE 2A).
RX   PubMed=3011278; DOI=10.1016/0092-8674(86)90790-7;
RA   Toyoda H., Nicklin M.J., Murray M.G., Anderson C.W., Dunn J.J.,
RA   Studier F.W., Wimmer E.;
RT   "A second virus-encoded proteinase involved in proteolytic processing of
RT   poliovirus polyprotein.";
RL   Cell 45:761-770(1986).
RN   [3]
RP   ACTIVE SITE (PROTEASE 3C), AND MUTAGENESIS OF HIS-1605; GLU-1636; ASP-1650
RP   AND CYS-1712.
RX   PubMed=1848550; DOI=10.1016/s0021-9258(19)67610-6;
RA   Haemmerle T., Hellen C.U.T., Wimmer E.;
RT   "Site-directed mutagenesis of the putative catalytic triad of poliovirus 3C
RT   proteinase.";
RL   J. Biol. Chem. 266:5412-5416(1991).
RN   [4]
RP   FUNCTION (PROTEASE 2A).
RX   PubMed=30867299; DOI=10.1128/jvi.00222-19;
RA   Visser L.J., Langereis M.A., Rabouw H.H., Wahedi M., Muntjewerff E.M.,
RA   de Groot R.J., van Kuppeveld F.J.M.;
RT   "Essential Role of Enterovirus 2A Protease in Counteracting Stress Granule
RT   Formation and the Induction of Type I Interferon.";
RL   J. Virol. 93:0-0(2019).
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 (PubMed:3011278). 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). Cleaves also 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       dissassembly (PubMed:30867299). 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:0000269|PubMed:3011278, ECO:0000269|PubMed:30867299}.
CC   -!- FUNCTION: [Protein 2B]: Plays an essential role in the virus
CC       replication cycle by acting as a viroporin. Creates a pore in the host
CC       reticulum endoplasmic and as a consequence releases Ca2+ in the
CC       cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium
CC       may trigger membrane trafficking and transport of viral ER-associated
CC       proteins to viroplasms, sites of viral genome replication.
CC       {ECO: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. It inhibits host cell endoplasmic
CC       reticulum-to-Golgi apparatus transport and causes the disassembly of
CC       the Golgi complex, possibly through GBF1 interaction (By similarity).
CC       This would result in depletion of MHC, trail receptors and IFN
CC       receptors at the host cell surface (By similarity). Plays an essential
CC       role in viral RNA replication by recruiting ACBD3 and PI4KB at the
CC       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 (By
CC       similarity). The oriI viral genomic sequence may act as a template for
CC       this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by
CC       the RNA-dependent RNA polymerase to replicate the viral genome (By
CC       similarity). Following genome release from the infecting virion in the
CC       cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By
CC       similarity). 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 (By similarity).
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). Cleaves also
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 + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC         Evidence={ECO: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=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY: [Protease 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:0000269|PubMed:3011278}.
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   -!- MISCELLANEOUS: This virus is a live vaccine strain derived from the
CC       mahoney strain by spontaneous mutations during the attenuation process.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; V01150; CAA24465.1; -; Genomic_RNA.
DR   PIR; A03899; GNNY3P.
DR   PDB; 8E8Z; EM; 3.15 A; 1=601-881, 4=2-69.
DR   PDBsum; 8E8Z; -.
DR   BMRB; P03301; -.
DR   EMDB; EMD-27951; -.
DR   SMR; P03301; -.
DR   IntAct; P03301; 3.
DR   MINT; P03301; -.
DR   MEROPS; C03.020; -.
DR   Proteomes; UP000000478; Genome.
DR   GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0039520; P:induction by virus of host autophagy; ISS:UniProtKB.
DR   GO; GO:0044694; P:pore-mediated entry of viral genome into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR   GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0039554; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host MDA-5 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039540; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity; IEA:UniProtKB-KW.
DR   GO; GO:0039545; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039707; P:virus-mediated pore formation in host cell membrane; IEA:UniProtKB-KW.
DR   CDD; cd23213; Enterovirus_RdRp; 1.
DR   CDD; cd00205; rhv_like; 3.
DR   Gene3D; 1.20.960.20; -; 1.
DR   Gene3D; 2.60.120.20; -; 3.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 6.10.20.20; Poliovirus 3A protein-like; 1.
DR   Gene3D; 4.10.880.10; Poliovirus 3D polymerase Domain 1 (Nucleotidyltransferase); 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 4.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR   InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014838; P3A.
DR   InterPro; IPR036203; P3A_soluble_dom.
DR   InterPro; IPR044067; PCV_3C_PRO.
DR   InterPro; IPR000081; Peptidase_C3.
DR   InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR003138; Pico_P1A.
DR   InterPro; IPR002527; Pico_P2B.
DR   InterPro; IPR001676; Picornavirus_capsid.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR033703; Rhv-like.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF08727; P3A; 1.
DR   Pfam; PF00548; Peptidase_C3; 1.
DR   Pfam; PF02226; Pico_P1A; 1.
DR   Pfam; PF00947; Pico_P2A; 1.
DR   Pfam; PF01552; Pico_P2B; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   Pfam; PF00073; Rhv; 3.
DR   Pfam; PF00910; RNA_helicase; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF88633; Positive stranded ssRNA viruses; 2.
DR   SUPFAM; SSF89043; Soluble domain of poliovirus core protein 3a; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR   PROSITE; PS51874; PCV_3C_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51218; SF3_HELICASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activation of host autophagy by virus; ATP-binding;
KW   Autocatalytic cleavage; Capsid protein;
KW   Clathrin- and caveolin-independent endocytosis of virus by host;
KW   Covalent protein-RNA linkage; Direct protein sequencing; 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..2209
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000426596"
FT   CHAIN           2..881
FT                   /note="P1"
FT                   /id="PRO_0000426597"
FT   CHAIN           2..341
FT                   /note="Capsid protein VP0"
FT                   /id="PRO_0000426598"
FT   CHAIN           2..69
FT                   /note="Capsid protein VP4"
FT                   /id="PRO_0000426599"
FT   CHAIN           70..341
FT                   /note="Capsid protein VP2"
FT                   /id="PRO_0000426600"
FT   CHAIN           342..579
FT                   /note="Capsid protein VP3"
FT                   /id="PRO_0000426601"
FT   CHAIN           580..881
FT                   /note="Capsid protein VP1"
FT                   /id="PRO_0000426602"
FT   CHAIN           882..1456
FT                   /note="P2"
FT                   /id="PRO_0000426603"
FT   CHAIN           882..1030
FT                   /note="Protease 2A"
FT                   /id="PRO_0000426604"
FT   CHAIN           1031..1127
FT                   /note="Protein 2B"
FT                   /id="PRO_0000040096"
FT   CHAIN           1128..1456
FT                   /note="Protein 2C"
FT                   /id="PRO_0000040097"
FT   CHAIN           1457..2209
FT                   /note="P3"
FT                   /id="PRO_0000426605"
FT   CHAIN           1457..1565
FT                   /note="Protein 3AB"
FT                   /id="PRO_0000426606"
FT   CHAIN           1457..1543
FT                   /note="Protein 3A"
FT                   /id="PRO_0000040098"
FT   CHAIN           1544..1565
FT                   /note="Viral protein genome-linked"
FT                   /id="PRO_0000426607"
FT   CHAIN           1566..2209
FT                   /note="Protein 3CD"
FT                   /id="PRO_0000426608"
FT   CHAIN           1566..1748
FT                   /note="Protease 3C"
FT                   /id="PRO_0000426609"
FT   CHAIN           1749..2209
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000426610"
FT   TOPO_DOM        2..1520
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        1521..1536
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1537..2209
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1232..1388
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1566..1744
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          1975..2090
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   ZN_FING         1396..1413
FT                   /note="C4-type"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          580..600
FT                   /note="Amphipathic alpha-helix"
FT                   /evidence="ECO:0000255"
FT   REGION          1128..1266
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1128..1200
FT                   /note="Membrane-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1149..1153
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1440..1447
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1451..1456
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        901
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        919
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        990
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        1605
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222,
FT                   ECO:0000269|PubMed:1848550"
FT   ACT_SITE        1636
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222,
FT                   ECO:0000269|PubMed:1848550"
FT   ACT_SITE        1712
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222,
FT                   ECO:0000269|PubMed:1848550"
FT   BINDING         936
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         938
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         996
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         998
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         1256..1263
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   BINDING         1396
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1399
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1408
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1413
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1981
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic; for RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1981
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic; for RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         2076
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic; for RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         2076
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic; for RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   SITE            69..70
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   SITE            341..342
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000269|PubMed:3011278"
FT   SITE            579..580
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000269|PubMed:3011278"
FT   SITE            881..882
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000269|PubMed:3011278"
FT   SITE            1030..1031
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000269|PubMed:3011278"
FT   SITE            1127..1128
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000269|PubMed:3011278"
FT   SITE            1152
FT                   /note="Involved in the interaction with host RTN3"
FT                   /evidence="ECO:0000250|UniProtKB:Q66478"
FT   SITE            1456..1457
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000269|PubMed:3011278"
FT   SITE            1543..1544
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000269|PubMed:3011278"
FT   SITE            1565..1566
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000269|PubMed:3011278"
FT   SITE            1748..1749
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000269|PubMed:3011278"
FT   MOD_RES         1546
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         1605
FT                   /note="H->Y: Complete loss of protease activity."
FT                   /evidence="ECO:0000269|PubMed:1848550"
FT   MUTAGEN         1636
FT                   /note="E->Q: Complete loss of protease activity."
FT                   /evidence="ECO:0000269|PubMed:1848550"
FT   MUTAGEN         1650
FT                   /note="D->N: No effect on protease activity; complete loss
FT                   of autoprocessing ability."
FT                   /evidence="ECO:0000269|PubMed:1848550"
FT   MUTAGEN         1712
FT                   /note="C->S: Complete loss of protease activity."
FT                   /evidence="ECO:0000269|PubMed:1848550"
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          26..29
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           51..54
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          83..87
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          90..97
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           103..105
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   TURN            113..115
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           126..128
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          138..140
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          147..151
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           153..155
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           159..167
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          168..180
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          188..197
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          206..208
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           214..217
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           220..222
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          227..229
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   TURN            247..253
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           256..261
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          262..268
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   TURN            269..271
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          273..279
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          284..288
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   TURN            290..292
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          296..307
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          316..332
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   TURN            349..352
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          364..366
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          381..383
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           385..388
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   TURN            400..404
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           406..409
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          411..414
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          423..426
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   TURN            430..432
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           436..438
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           440..446
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          447..453
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          455..461
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          470..476
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          478..480
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           486..489
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          492..498
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          500..502
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          504..509
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          514..521
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           524..526
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          530..537
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          547..557
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           626..628
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           636..638
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           652..654
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           656..659
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          664..673
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          685..688
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           695..701
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          704..721
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          733..739
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           752..755
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          757..759
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          761..765
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          771..775
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          780..786
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          790..793
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          796..799
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   HELIX           801..804
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          813..816
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          818..823
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          832..847
FT                   /evidence="ECO:0007829|PDB:8E8Z"
FT   STRAND          860..863
FT                   /evidence="ECO:0007829|PDB:8E8Z"
SQ   SEQUENCE   2209 AA;  246578 MW;  9EC1EF4D174A28A4 CRC64;
     MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYRDSASNA ASKQDFSQDP SKFTEPIKDV
     LIKTSPMLNS PNIEACGYSD RVLQLTLGNS TITTQEAANS VVAYGRWPEY LRDSEANPVD
     QPTEPDVAAC RFYTLDTVSW TKESRGWWWK LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ
     CNASKFHQGA LGVFAVPEMC LAGDSNTTTM HTSYQNANPG EKGGTFTGTF TPDDNQTSPA
     RRFCPVDYLF GNGTLLGNAF VFPHQIINLR TNNCATLVLP YVNSLSIDSM VKHNNWGIAI
     LPLAPLNFAS ESSPEIPITL TIAPMCCEFN GLRNITLPRL QGLPVMNTPG SNQYLTADNF
     QSPCALPEFD VTPPIDIPGE VKNMMELAEI DTMIPFDLSA KKKNTMEMYR VRLSDKPHTD
     DPILCLSLSP ASDPRLSHTM LGEILNYYTH WAGSLKFTFL FCGSMMATGK LLVSYAPPGA
     DPPKKRKEAM LGTHVIWDIG LQSSCTMVVP WISNTTYRQT IDDSFTEGGY ISVFYQTRIV
     VPLSTPREMD ILGFVSACND FSVRLMRDTT HIEQKALAQG LGQMLESMID NTVRETVGAA
     TSRDALPNTE ASGPAHSKEI PALTAVETGA TNPLVPSDTV QTRHVVQHRS RSESSIESFF
     ARGACVAIIT VDNSASTKNK DKLFTVWKIT YKDTVQLRRK LEFFTYSRFD MEFTFVVTAN
     FTETNNGHAL NQVYQIMYVP PGAPVPEKWD DYTWQTSSNP SIFYTYGTAP ARISVPYVGI
     SNAYSHFYDG FSKVPLKDQS AALGDSLYGA ASLNDFGILA VRVVNDHNPT KVTSKIRVYL
     KPKHIRVWCP RPPRAVAYYG PGVDYKDGTL TPLSTKDLTT YGFGHQNKAV YTAGYKICNY
     HLATQEDLQN AVNVMWNRDL LVTESRAQGT DSIARCNCNA GVYYCESRRK YYPVSFVGPT
     FQYMEANNYY PARYQSHMLI GHGFASPGDC GGILRCHHGV IGIITAGGEG LVAFTDIRDL
     YAYEEEAMEQ GITNYIESLG AAFGSGFTQQ IGDKITELTN MVTSTITEKL LKNLIKIISS
     LVIITRNYED TTTVLATLAL LGCDASPWQW LRKKACDVLE IPYVTKQGDS WLKKFTEACN
     AAKGLEWVSN KISKFIDWLK EKIIPQARDK LEFVTKLRQL EMLENQISTI HQSCPSQEHQ
     EILFNNVRWL SIQSKRFAPL YAVEAKRIQK LEHTINNYIQ FKSKHRIEPV CLLVHGSPGT
     GKSVATNLIA RAIAERENTS TYSLPPDPSH FDGYKQQGVV IMDDLNQNPD GADMKLFCQM
     VSTVEFIPPM ASLEEKGILF TSNYVLASTN SSRISPPTVA HSDALARRFA FDMDIQVMNE
     YSRDGKLNMA MATEMCKNCH QPANFKRCCP LVCGKAIQLM DKSSRVRYSI DQITTMIINE
     RNRRSNIGNC MEALFQGPLQ YKDLKIDIKT SPPPECINDL LQAVDSQEVR DYCEKKGWIV
     NITSQVQTER NINRAMTILQ AVTTFAAVAG VVYVMYKLFA GHQGAYTGLP NKKPNVPTIR
     TAKVQGPGFD YAVAMAKRNI VTATTSKGEF TMLGVHDNVA ILPTHASPGE SIVIDGKEVE
     ILDAKALEDQ AGTNLEITII TLKRNEKFRD IRPHIPTQIT ETNDGVLIVN TSKYPNMYVP
     VGAVTEQGYL NLGGRQTART LMYNFPTRAG QCGGVITCTG KVIGMHVGGN GSHGFAAALK
     RSYFTQSQGE IQWMRPSKEV GYPIINAPSK TKLEPSAFHY VFEGVKEPAV LTKNDPRLKT
     NFEEAIFSKY VGNKITEVDE HMKEAVDHYA GQLMSLDINT EQMCLEDAMY GTDGLEALDL
     STSAGYPYVA MGKKKRDILN KQTRDTKEMQ KLLDTYGINL PLVTYVKDEL RSKTKVEQGK
     SRLIEASSLN DSVAMRMAFG NLYAAFHKNP GVITGSAVGC DPDLFWSKIP VLMEEKLFAF
     DYTGYDASLS PAWFEALEMV LEKIGFGDRV DYIDYLNHSH HLYKNKTYCV KGGMPSGCSG
     TSIFNSMINN LIIRTLLLKT YKGIDLDHLK MIAYGDDVIA SYPHEVDASL LAQSGKDYGL
     TMTPADKSAI FETVTWENVT FLKRFFRADE KYPFLIHPVM PMKEIHESIR WTKDPRNTQD
     HVRSLCLLAW HNGEEEYNKF LAKIRSVPIG RALLLPEYST LYRRWLDSF
//