ID   POLG_CX16T              Reviewed;        2193 AA.
AC   Q9QF31;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   24-JAN-2024, entry version 168.
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   Coxsackievirus A16 (strain Tainan/5079/98).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Ensavirinae; Enterovirus; Enterovirus A.
OX   NCBI_TaxID=231417;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11536241; DOI=10.1002/jmv.2038;
RA   Yan J.-J., Su I.-J., Chen P.-F., Liu C.-C., Yu C.-K., Wang J.-R.;
RT   "Complete genome analysis of enterovirus 71 isolated from an outbreak in
RT   Taiwan and rapid identification of enterovirus 71 and coxsackievirus A16 by
RT   RT-PCR.";
RL   J. Med. Virol. 65:331-339(2001).
RN   [2]
RP   INTERACTION WITH HOST RTN3 (PROTEIN 2C).
RX   PubMed=17182608; DOI=10.1074/jbc.m611145200;
RA   Tang W.-F., Yang S.-Y., Wu B.-W., Jheng J.-R., Chen Y.-L., Shih C.-H.,
RA   Lin K.-H., Lai H.-C., Tang P., Horng J.-T.;
RT   "Reticulon 3 binds the 2C protein of enterovirus 71 and is required for
RT   viral replication.";
RL   J. Biol. Chem. 282:5888-5898(2007).
RN   [3]
RP   INTERACTION WITH HOST IFIH1 (PROTEASE 3C), FUNCTION (PROTEASE 3C), AND
RP   INTERACTION WITH HOST MAP3K7 (PROTEASE 3C).
RC   STRAIN=CC024;
RX   PubMed=28424289; DOI=10.1128/jvi.00546-17;
RA   Rui Y., Su J., Wang H., Chang J., Wang S., Zheng W., Cai Y., Wei W.,
RA   Gordy J.T., Markham R., Kong W., Zhang W., Yu X.F.;
RT   "Disruption of MDA5-Mediated Innate Immune Responses by the 3C Proteins of
RT   Coxsackievirus A16, Coxsackievirus A6, and Enterovirus D68.";
RL   J. Virol. 91:0-0(2017).
RN   [4] {ECO:0007744|PDB:4MG3}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 863-1007 IN COMPLEX WITH ZINC,
RP   AND SUBUNIT (PROTEASE 2A).
RX   PubMed=24026848; DOI=10.1007/s13238-013-3914-z;
RA   Sun Y., Wang X., Yuan S., Dang M., Li X., Zhang X.C., Rao Z.;
RT   "An open conformation determined by a structural switch for 2A protease
RT   from coxsackievirus A16.";
RL   Protein Cell 4:782-792(2013).
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       to provide virion attachment to target host cells. This attachment
CC       induces virion internalization (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). 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 (By
CC       similarity). Counteracts stress granule formation probably by
CC       antagonizing its assembly or promoting its dissassembly (By
CC       similarity). Cleaves and inhibits host IFIH1/MDA5, thereby inhibiting
CC       the type-I IFN production and the establishment of the antiviral state
CC       (By similarity). Cleaves and inhibits host MAVS, thereby inhibiting the
CC       type-I IFN production and the establishment of the antiviral state (By
CC       similarity). {ECO:0000250|UniProtKB:P03300,
CC       ECO:0000250|UniProtKB:P03301, ECO:0000250|UniProtKB:P03313}.
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 (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 (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       Binds and inhibits host IFIH1/MDA5, thereby inhibiting the type-I IFN
CC       production and the establishment of the antiviral state
CC       (PubMed:28424289). Cleaves host MAP3K7/TAK1, resulting in inhibition of
CC       TRAF6-triggered NF-kappa-B induction (PubMed:28424289). Cleaves host
CC       NLRP1, triggers host N-glycine-mediated degradation of the
CC       autoinhibitory NLRP1 N-terminal fragment (By similarity).
CC       {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03303,
CC       ECO:0000269|PubMed:28424289}.
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 (By similarity).
CC       {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       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).
CC       {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:0000269|PubMed:24026848}.
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 (PubMed:17182608).
CC       Interacts with capsid protein VP3; this interaction may be important
CC       for virion morphogenesis (By similarity).
CC       {ECO:0000250|UniProtKB:P03300, ECO:0000269|PubMed:17182608}.
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: [Protease 3C]: Interacts with host IFIH1/MDA5; this
CC       interaction inhibits host IFIH1. {ECO:0000269|PubMed:28424289}.
CC   -!- SUBUNIT: [Protein 3CD]: Protein 3CD: Interacts with protein 3AB and
CC       with RNA-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
CC       degenerate C4-type zinc-finger with only 3 cysteines (By similarity).
CC       The C-terminus is involved in RNA-binding (By similarity). The extreme
CC       C-terminus contains a region involved in oligomerization (By
CC       similarity). {ECO:0000250|UniProtKB:B9VUU3,
CC       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; AF177911; AAD55085.1; -; Genomic_RNA.
DR   PDB; 4MG3; X-ray; 1.80 A; A/B=863-1007.
DR   PDB; 5C8C; X-ray; 2.50 A; A=566-862, B=1-323, C=324-565.
DR   PDB; 6LHT; EM; 3.67 A; A/B/C/D/E=566-862.
DR   PDB; 7Y7M; EM; 3.05 A; D=1-69.
DR   PDB; 7YMS; EM; 2.90 A; D=1-69.
DR   PDBsum; 4MG3; -.
DR   PDBsum; 5C8C; -.
DR   PDBsum; 6LHT; -.
DR   PDBsum; 7Y7M; -.
DR   PDBsum; 7YMS; -.
DR   EMDB; EMD-0897; -.
DR   SMR; Q9QF31; -.
DR   MEROPS; C03.020; -.
DR   ABCD; Q9QF31; 3 sequenced antibodies.
DR   BRENDA; 3.4.22.29; 12962.
DR   Proteomes; UP000001439; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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: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:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
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: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:0039644; P:suppression by virus of host NF-kappaB cascade; 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: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; 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; 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   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.
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 MDA5 by virus;
KW   Inhibition of host mRNA nuclear export by virus;
KW   Inhibition of host NF-kappa-B by virus;
KW   Inhibition of host RLR pathway by virus; Ion channel; Ion transport;
KW   Lipoprotein; Magnesium; Membrane; Metal-binding; Myristate;
KW   Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW   Pore-mediated penetration of viral genome into host cell; Protease; Repeat;
KW   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..2193
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000426193"
FT   CHAIN           2..862
FT                   /note="P1"
FT                   /id="PRO_0000426194"
FT   CHAIN           2..323
FT                   /note="Capsid protein VP0"
FT                   /id="PRO_0000426195"
FT   CHAIN           2..69
FT                   /note="Capsid protein VP4"
FT                   /id="PRO_0000426196"
FT   CHAIN           70..323
FT                   /note="Capsid protein VP2"
FT                   /id="PRO_0000426197"
FT   CHAIN           324..565
FT                   /note="Capsid protein VP3"
FT                   /id="PRO_0000426198"
FT   CHAIN           566..862
FT                   /note="Capsid protein VP1"
FT                   /id="PRO_0000426199"
FT   CHAIN           863..1440
FT                   /note="P2"
FT                   /id="PRO_0000426200"
FT   CHAIN           863..1012
FT                   /note="Protease 2A"
FT                   /id="PRO_0000039529"
FT   CHAIN           1013..1111
FT                   /note="Protein 2B"
FT                   /id="PRO_0000039530"
FT   CHAIN           1112..1440
FT                   /note="Protein 2C"
FT                   /id="PRO_0000039531"
FT   CHAIN           1441..2193
FT                   /note="P3"
FT                   /id="PRO_0000426201"
FT   CHAIN           1441..1548
FT                   /note="Protein 3AB"
FT                   /id="PRO_0000426202"
FT   CHAIN           1441..1526
FT                   /note="Protein 3A"
FT                   /id="PRO_0000039532"
FT   CHAIN           1527..1548
FT                   /note="Viral protein genome-linked"
FT                   /id="PRO_0000426203"
FT   CHAIN           1549..2193
FT                   /note="Protein 3CD"
FT                   /id="PRO_0000426204"
FT   CHAIN           1549..1731
FT                   /note="Protease 3C"
FT                   /id="PRO_0000426205"
FT   CHAIN           1732..2193
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000426206"
FT   TOPO_DOM        2..1503
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        1504..1519
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1520..2193
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1216..1374
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1549..1727
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          1958..2074
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   ZN_FING         1381..1397
FT                   /note="C4-type; degenerate"
FT                   /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          566..588
FT                   /note="Amphipathic alpha-helix"
FT                   /evidence="ECO:0000255"
FT   REGION          1112..1250
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1112..1184
FT                   /note="Membrane-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1133..1137
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1424..1431
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1435..1440
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        883
FT                   /note="For protease 2A activity"
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        972
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        1588
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1619
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1695
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   BINDING         918
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000269|PubMed:24026848"
FT   BINDING         920
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000269|PubMed:24026848"
FT   BINDING         978
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000269|PubMed:24026848"
FT   BINDING         980
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000269|PubMed:24026848"
FT   BINDING         1240..1247
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   BINDING         1381
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT   BINDING         1392
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT   BINDING         1397
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT   BINDING         1964
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         1964
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         2060
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         2060
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            323..324
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            862..863
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1012..1013
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1111..1112
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1136
FT                   /note="Involved in the interaction with host RTN3"
FT                   /evidence="ECO:0000250|UniProtKB:Q66478"
FT   SITE            1440..1441
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1526..1527
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1548..1549
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1731..1732
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   MOD_RES         1529
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   TURN            19..22
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:7Y7M"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           51..54
FT                   /evidence="ECO:0007829|PDB:7YMS"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:7YMS"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:7YMS"
FT   TURN            73..75
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          83..87
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          90..95
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           97..99
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           103..105
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   TURN            113..115
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           126..128
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          138..140
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          147..151
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           153..155
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           159..167
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          168..180
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          188..198
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   TURN            205..208
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           217..220
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           223..225
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           232..234
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   TURN            235..238
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           241..246
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          247..253
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   TURN            254..256
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          258..264
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          269..273
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   TURN            275..277
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          281..292
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          301..317
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   TURN            331..334
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          345..348
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          362..365
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           367..370
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           382..384
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           388..392
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          394..397
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          405..410
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          415..417
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           418..421
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           423..428
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          431..436
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          438..444
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          453..459
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          461..465
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           469..472
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          475..481
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   TURN            482..484
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          486..492
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          497..502
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           508..512
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          516..523
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          533..543
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          548..552
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           625..628
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           641..643
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           645..649
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          653..660
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          662..667
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          669..675
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           682..688
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          691..705
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          715..721
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           734..737
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          739..741
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          743..747
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          753..757
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          762..768
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           781..786
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           791..793
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          797..806
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          812..828
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          838..841
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   HELIX           846..848
FT                   /evidence="ECO:0007829|PDB:5C8C"
FT   STRAND          869..881
FT                   /evidence="ECO:0007829|PDB:4MG3"
FT   HELIX           882..884
FT                   /evidence="ECO:0007829|PDB:4MG3"
FT   HELIX           887..891
FT                   /evidence="ECO:0007829|PDB:4MG3"
FT   STRAND          893..897
FT                   /evidence="ECO:0007829|PDB:4MG3"
FT   HELIX           898..900
FT                   /evidence="ECO:0007829|PDB:4MG3"
FT   STRAND          902..912
FT                   /evidence="ECO:0007829|PDB:4MG3"
FT   STRAND          922..927
FT                   /evidence="ECO:0007829|PDB:4MG3"
FT   TURN            928..931
FT                   /evidence="ECO:0007829|PDB:4MG3"
FT   STRAND          932..937
FT                   /evidence="ECO:0007829|PDB:4MG3"
FT   STRAND          942..946
FT                   /evidence="ECO:0007829|PDB:4MG3"
FT   STRAND          950..952
FT                   /evidence="ECO:0007829|PDB:4MG3"
FT   STRAND          954..965
FT                   /evidence="ECO:0007829|PDB:4MG3"
FT   HELIX           969..971
FT                   /evidence="ECO:0007829|PDB:4MG3"
FT   STRAND          975..978
FT                   /evidence="ECO:0007829|PDB:4MG3"
FT   STRAND          981..990
FT                   /evidence="ECO:0007829|PDB:4MG3"
FT   STRAND          993..998
FT                   /evidence="ECO:0007829|PDB:4MG3"
FT   HELIX           1003..1005
FT                   /evidence="ECO:0007829|PDB:4MG3"
SQ   SEQUENCE   2193 AA;  243184 MW;  927839DB58F61E7F CRC64;
     MGSQVSTQRS GSHENSNSAS EGSTINYTTI NYYKDAYAAS AGRQDMSQDP KKFTDPVMDV
     IHEMAPPLKS PSAEACGYSD RVAQLTIGNS TITTQEAANI VIAYGEWPEY CPDTDATAVD
     KPTRPDVSVN RFFTLDTKSW AKDSKGWYWK FPDVLTEVGV FGQNAQFHYL YRSGFCVHVQ
     CNASKFHQGA LLVAVLPEYV LGTIAGGTGN ENSHPPYATT QPGQVGAVLT HPYVLDAGIP
     LSQLTVCPHQ WINLRTNNCA TIIVPYMNTV PFDSALNHCN FGLLVVPVVP LDFNAGATSE
     IPITVTIAPM CAEFAGLRQA VKQGIPTELK PGTNQFLTTD DGVSAPILPG FHPTPPIHIP
     GEVHNLLEIC RVETILEVNN LKTNETTPMQ RLCFPVSVQS KTGELCAAFR ADPGRDGPWQ
     STILGQLCRY YTQWSGSLEV TFMFAGSFMA TGKMLIAYTP PGGNVPADRI TAMLGTHVIW
     DFGLQSSVTL VVPWISNTHY RAHARAGYFD YYTTGIITIW YQTNYVVPIG APTTAYIVAL
     AAAQDNFTMK LCKDTEDIEQ TANIQGDPIA DMIDQTVNNQ VNRSLTALQV LPTAADTEAS
     SHRLGTGVVP ALQAAETGAS SNASDKNLIE TRCVLNHHST QETAIGNFFS RAGLVSIITM
     PTTGTQNTDG YVNWDIDLMG YAQLRRKCEL FTYMRFDAEF TFVVAKPNGE LVPQLLQYMY
     VPPGAPKPTS RDSFAWQTAT NPSVFVKMTD PPAQVSVPFM SPASAYQWFY DGYPTFGEHL
     QANDLDYGQC PNNMMGTFSI RTVGTEKSPH SITLRVYMRI KHVRAWIPRP LRNQPYLFKT
     NPNYKGNDIK CTSTSRDKIT TLGKFGQQSG AIYVGNYRVV NRHLATHNDW ANLVWEDSSR
     DLLVSSTTAQ GCDTIARCNC QTGVYYCSSK RKHYPVSFTK PSLIFVEASE YYPARYQSHL
     MLAVGHSEPG DCGGILRCQH GVVGIVSTGG NGLVGFADVR DLLWLDEEAM EQGVSDYIKG
     LGDAFGVGFT DAVSREVEAL KNHLIGSEGA VEKILKNLVK LISALVIVVR SDYDMVTLTA
     TLALIGCHGS PWAWIKAKTA SILGIPIVQK QSASWLKKFN DMANAAKGLE WISSKISKFI
     DWLKEKIIPA AKEKVEFLNN LKQLPLLENQ ISNLEQSAAS QEDLEAMFGN VSYLAHFCRK
     FQPLYATEAK RVYALEKRMN NYMQFKSKHR IEPVCLIIRG SPGTGKSLAT GIIARAIADK
     YHSSVYSLPP DPDHFDGYKQ QVVTVMDDLC QNPDGKDMSL FCQMVSTVDF IPPMASLEEK
     GVSFTSKFVI ASTNASNIVV PTVSDSDAIR RRFYMDCDIE VTDSYKTDLG RLDAGRAAKL
     CTENNTANFK RCSPLVCGKA IQLRDRKSKV RYSIDTVVSE LIREYNNRSA IGNTIEALFQ
     GPLKFKPIRI SLEEKPAPDA ISDLLASVDS EEVRQYCREQ GWIIPETPTN VERHLNRAVL
     VMQSIATVVA VVSLVYVIYK LFAGFQGAYS GAPKQALKKP VLRTATVQGP SLDFALSLLR
     RNIRQVQTDQ GHFTMLGVRD RLAILPRHSQ PGKTIWVEHK LINVLDAVEL VDEQGVNLEL
     TLVTLDTNEK FRDVTKFIPE TITGASDATL VINTEHMPSM FVPVGDVVQY GFLNLSGKPT
     HRTMMYNFPT KAGQCGGVVT SVGKIIGIHI GGNGRQGFCA GLKRGYFASE QGEIQWMKPN
     KETGRLNING PTRTKLEPSV FHDVFEGNKE PAVLTSKDPR LEVDFEQALF SKYVGNTLHE
     PDEYVTQAAL HYANQLKQLD ININKMSMEE ACYGTEYLEA IDLHTSAGYP YSALGVKKRD
     ILDPITRDTT KMKFYMDKYG LDLPYSTYVK DELRSLDKIK KGKSRLIEAS SLNDSVYLRM
     TFGHLYETFH ANPGTVTGSA VGCNPDVFWS KLPILLPGSL FAFDYSGYDA SLSPVWFRAL
     EVVLREIGYS EEAVSLIEGI NHTHHVYRNK TYCVLGGMPS GCSGTSIFNS MINNIIIRTL
     LIKTFKGIDL DELNMVAYGD DVLASYPFPI DCSELAKTGK EYGLTMTPAD KSPCFNEVTW
     ENATFLKRGF LPDHQFPFLI HPTMPMREIH ESIRWTKDAR NTQDHVRSLC LLAWHNGKEE
     YEKFVSTIRS VPIGKALAIP NFENLRRNWL ELF
//