ID   POLG_CXA9               Reviewed;        2201 AA.
AC   P21404;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   24-JAN-2024, entry version 195.
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 A9 (strain Griggs).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Ensavirinae; Enterovirus; Enterovirus B.
OX   NCBI_TaxID=12068;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2558158; DOI=10.1099/0022-1317-70-12-3269;
RA   Chang K.H., Auvinen P., Hyypiae T., Stanway G.;
RT   "The nucleotide sequence of coxsackievirus A9; implications for receptor
RT   binding and enterovirus classification.";
RL   J. Gen. Virol. 70:3269-3280(1989).
RN   [2]
RP   INTERACTION WITH HOST ITGAV/ITGB6 INTEGRIN (CAPSID PROTEIN VP1).
RX   PubMed=15194773; DOI=10.1128/jvi.78.13.6967-6973.2004;
RA   Williams C.H., Kajander T., Hyypia T., Jackson T., Sheppard D., Stanway G.;
RT   "Integrin alpha v beta 6 is an RGD-dependent receptor for coxsackievirus
RT   A9.";
RL   J. Virol. 78:6967-6973(2004).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-870.
RX   PubMed=10647183; DOI=10.1016/s0969-2126(00)88343-4;
RA   Hendry E., Hatanaka H., Fry E., Smyth M., Tate J., Stanway G., Santti J.,
RA   Maaronen M., Hyypia T., Stuart D.;
RT   "The crystal structure of coxsackievirus A9: new insights into the
RT   uncoating mechanisms of enteroviruses.";
RL   Structure 7:1527-1538(1999).
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 integrin
CC       ITGAV/ITGB6 to provide virion attachment to target host cells
CC       (Probable). This attachment induces virion internalization (By
CC       similarity). Tyrosine kinases are probably involved in the entry
CC       process (By similarity). After binding to its receptor, the capsid
CC       undergoes conformational changes (By similarity). Capsid protein VP1 N-
CC       terminus (that contains an amphipathic alpha-helix) and capsid protein
CC       VP4 are externalized (By similarity). Together, they shape a pore in
CC       the host membrane through which viral genome is translocated to host
CC       cell cytoplasm (By similarity). {ECO:0000250|UniProtKB:P03300,
CC       ECO:0000305|PubMed:15194773}.
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: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       ECO:0000250|UniProtKB:P03313}.
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: [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   -!- 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 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   -!- 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). Interacts with host
CC       integrin heterodimer ITGAV/ITGB6 (PubMed:15194773).
CC       {ECO:0000250|UniProtKB:P03300, ECO:0000269|PubMed:15194773}.
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       ECO:0000250|UniProtKB:P03313}.
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
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}.
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1d4m";
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DR   EMBL; D00627; BAA00518.1; -; Genomic_RNA.
DR   PIR; JQ0523; GNNYA9.
DR   PDB; 1D4M; X-ray; 2.90 A; 1=569-867, 2=70-330, 3=331-568, 4=2-69.
DR   PDB; 3J2J; EM; 9.54 A; A=631-852, B=331-568, C=79-330.
DR   PDBsum; 1D4M; -.
DR   PDBsum; 3J2J; -.
DR   SMR; P21404; -.
DR   ELM; P21404; -.
DR   DrugBank; DB08726; 5-(7-(4-(4,5-dihydro-2-oxazolyl)phenoxy)heptyl)-3-methyl isoxazole.
DR   DrugBank; DB08231; Myristic acid.
DR   MEROPS; C03.011; -.
DR   MEROPS; C03.020; -.
DR   MEROPS; N08.001; -.
DR   EvolutionaryTrace; P21404; -.
DR   Proteomes; UP000000288; Segment.
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: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: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; 4.10.80.10; Picornavirus coat protein VP4; 1.
DR   Gene3D; 6.10.20.20; Poliovirus 3A protein-like; 1.
DR   Gene3D; 4.10.880.10; Poliovirus 3D polymerase Domain 1 (Nucleotidyltransferase); 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 4.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR   InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014838; P3A.
DR   InterPro; IPR036203; P3A_soluble_dom.
DR   InterPro; IPR044067; PCV_3C_PRO.
DR   InterPro; IPR000081; Peptidase_C3.
DR   InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR003138; Pico_P1A.
DR   InterPro; IPR036988; Pico_P1A_sf.
DR   InterPro; IPR002527; Pico_P2B.
DR   InterPro; IPR001676; Picornavirus_capsid.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR033703; Rhv-like.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF08727; P3A; 1.
DR   Pfam; PF00548; Peptidase_C3; 1.
DR   Pfam; PF02226; Pico_P1A; 1.
DR   Pfam; PF00947; Pico_P2A; 1.
DR   Pfam; PF01552; Pico_P2B; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   Pfam; PF00073; Rhv; 3.
DR   Pfam; PF00910; RNA_helicase; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF88633; Positive stranded ssRNA viruses; 2.
DR   SUPFAM; SSF89043; Soluble domain of poliovirus core protein 3a; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR   PROSITE; PS51874; PCV_3C_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51218; SF3_HELICASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activation of host autophagy by virus; ATP-binding;
KW   Autocatalytic cleavage; Capsid protein; Covalent protein-RNA linkage;
KW   DNA replication; Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host translation shutoff by virus; Helicase; Host cytoplasm;
KW   Host cytoplasmic vesicle; Host gene expression shutoff by virus;
KW   Host membrane; Host mRNA suppression by virus; Host nucleus;
KW   Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host mRNA nuclear export by virus;
KW   Inhibition of host RIG-I by virus; Inhibition of host RLR pathway by virus;
KW   Ion channel; Ion transport; Lipoprotein; Magnesium; Membrane;
KW   Metal-binding; Myristate; Nucleotide-binding; Nucleotidyltransferase;
KW   Phosphoprotein; Pore-mediated penetration of viral genome into host cell;
KW   Protease; 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..2201
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000426164"
FT   CHAIN           2..867
FT                   /note="P1"
FT                   /id="PRO_0000426165"
FT   CHAIN           2..330
FT                   /note="Capsid protein VP0"
FT                   /id="PRO_0000426166"
FT   CHAIN           2..69
FT                   /note="Capsid protein VP4"
FT                   /id="PRO_0000426167"
FT   CHAIN           70..330
FT                   /note="Capsid protein VP2"
FT                   /id="PRO_0000426168"
FT   CHAIN           331..568
FT                   /note="Capsid protein VP3"
FT                   /id="PRO_0000426169"
FT   CHAIN           569..867
FT                   /note="Capsid protein VP1"
FT                   /id="PRO_0000426170"
FT   CHAIN           868..1445
FT                   /note="P2"
FT                   /id="PRO_0000426171"
FT   CHAIN           868..1017
FT                   /note="Protease 2A"
FT                   /id="PRO_0000426172"
FT   CHAIN           1018..1116
FT                   /note="Protein 2B"
FT                   /id="PRO_0000039508"
FT   CHAIN           1117..1445
FT                   /note="Protein 2C"
FT                   /id="PRO_0000039509"
FT   CHAIN           1446..2201
FT                   /note="P3"
FT                   /id="PRO_0000426173"
FT   CHAIN           1446..1556
FT                   /note="Protein 3AB"
FT                   /id="PRO_0000426174"
FT   CHAIN           1446..1534
FT                   /note="Protein 3A"
FT                   /id="PRO_0000039510"
FT   CHAIN           1535..1556
FT                   /note="Viral protein genome-linked"
FT                   /id="PRO_0000426175"
FT   CHAIN           1557..2201
FT                   /note="Protein 3CD"
FT                   /id="PRO_0000426176"
FT   CHAIN           1557..1739
FT                   /note="Protease 3C"
FT                   /id="PRO_0000426177"
FT   CHAIN           1740..2201
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000426178"
FT   TOPO_DOM        2..1511
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        1512..1527
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1528..2201
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1221..1377
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1557..1735
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          1966..2082
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   ZN_FING         1385..1402
FT                   /note="C4-type; degenerate"
FT                   /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT   REGION          566..582
FT                   /note="Amphipathic alpha-helix"
FT                   /evidence="ECO:0000255"
FT   REGION          1117..1255
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1117..1189
FT                   /note="Membrane-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1138..1142
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1429..1436
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1440..1445
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   MOTIF           858..860
FT                   /note="Cell attachment site"
FT   ACT_SITE        888
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        906
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        977
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        1596
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1627
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1703
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   BINDING         923
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         925
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         983
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         985
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         1385
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         1402
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT   BINDING         1972
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         1972
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         2068
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         2068
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            330..331
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            867..868
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1017..1018
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1116..1117
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1141
FT                   /note="Involved in the interaction with host RTN3"
FT                   /evidence="ECO:0000250|UniProtKB:Q66478"
FT   SITE            1445..1446
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1534..1535
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1556..1557
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1739..1740
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   MOD_RES         1537
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   STRAND          3..7
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          26..29
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           51..54
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          83..87
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          90..96
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   TURN            113..115
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           126..128
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          138..140
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          147..151
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           153..155
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           159..167
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          168..180
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          188..197
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          203..205
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           212..214
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          225..227
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           239..241
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   TURN            242..245
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           248..253
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          254..260
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   TURN            261..263
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          265..271
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          276..280
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   TURN            282..284
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          288..299
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          308..324
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   TURN            338..341
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          353..355
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           374..377
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           394..398
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          400..404
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          411..416
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   TURN            419..421
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   TURN            423..427
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           429..434
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          437..442
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          444..450
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          459..465
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           475..478
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          481..487
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          493..498
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          503..505
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          507..510
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          519..526
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          536..546
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          551..555
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           602..604
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           612..615
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           628..630
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           632..636
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          640..650
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           654..657
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          658..662
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          665..668
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           669..675
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          678..695
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          709..715
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           728..731
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          733..735
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          737..741
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          748..751
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          756..762
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          766..769
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   TURN            770..772
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          773..777
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   HELIX           778..781
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          786..793
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          800..818
FT                   /evidence="ECO:0007829|PDB:1D4M"
FT   STRAND          843..845
FT                   /evidence="ECO:0007829|PDB:1D4M"
SQ   SEQUENCE   2201 AA;  246535 MW;  CCEA86F9E80F385F CRC64;
     MGAQVSTQKT GAHETSLSAA GNSIIHYTNI NYYKDAASNS ANRQDFTQDP SKFTEPVKDV
     MIKSLPALNS PTVEECGYSD RVRSITLGNS TITTQECANV VVGYGRWPTY LRDDEATAED
     QPTQPDVATC RFYTLDSIKW EKGSVGWWWK FPEALSDMGL FGQNMQYHYL GRAGYTIHLQ
     CNASKFHQGC LLVVCVPEAE MGGAVVGQAF SATAMANGDK AYEFTSATQS DQTKVQTAIH
     NAGMGVGVGN LTIYPHQWIN LRTNNSATIV MPYINSVPMD NMFRHYNFTL MVIPFVKLDY
     ADTASTYVPI TVTVAPMCAE YNGLRLAQAQ GLPTMNTPGS TQFLTSDDFQ SPCALPQFDV
     TPSMNIPGEV KNLMEIAEVD SVVPVNNVQD TTDQMEMFRI PVTINAPLQQ QVFGLRLQPG
     LDSVFKHTLL GEILNYYAHW SGSMKLTFVF CGSAMATGKF LIAYSPPGAN PPKTRKDAML
     GTHIIWDIGL QSSCVLCVPW ISQTHYRLVQ QDEYTSAGYV TCWYQTGMIV PPGTPNSSSI
     MCFASACNDF SVRMLRDTPF ISQDNKLQGD VEEAIERARC TVADTMRTGP SNSASVPALT
     AVETGHTSQV TPSDTMQTRH VKNYHSRSES TVENFLGRSA CVYMEEYKTT DKHVNKKFVA
     WPINTKQMVQ MRRKLEMFTY LRFDMEVTFV ITSRQDPGTT LAQDMPVLTR QIMYVPPGGP
     IPAKVDDYAW QTSTNPSIFW TEGNAPARMS IPFISIGNAY SNFYDGWSNF DQRGSYGYNT
     LNNLGHIYVR HVSGSSPHPI TSTIRVYFKP KHTRAWVPRP PRLCQYKKAF SVDFTPTPIT
     DTRKDINTVT TVAQSRRRGD MSTLNTHGAF GQQSGAVYVG NYRVINRHLA THTDWQNCVW
     EDYNRDLLVS TTTAHGCDVI ARCQCTTGVY FCASKNKHYP VSFEGPGLVE VQESEYYPKR
     YQSHVLLAAG FSEPGDCGGI LRCEHGVIGI VTMGGEGVVG FADVRDLLWL EDDAMEQGVK
     DYVEQLGNAF GSGFTNQICE QVNLLKESLV GQDSILEKSL KALVKIISAL VIVVRNHDDL
     ITVTAILALI GCTSSPWRWL KQKVSQYYGI PMAERQNDSW LKKFTEMTNA CKRMEWIAIK
     IQKFIEWLKV KILPEVREKH EFLNRLKQLP LLESQIATIE QSAPSQSDQE QLFSNVQYFA
     HYCRKYAPLY AAEAKRVFSL EKKMSNYIQF KSKCRIEPVC LLLHGSPGAG KSVATNLIGR
     SLAEKLNSSV YSLPPDPDHF DGYKQQAVVI MDDLCQNPDG KDVSLFCQMV SSVDFVPPMA
     ALEEKGILFT SPFVLASTNA GSINAPTVSD SRALARRFHF DMNIEVISMY SQNGKINMPM
     SVKTCDEECC PVNFKKCCPL VCGKAIQFID RRTQVRYSLD MLVTEMFREY NHRHSVGATL
     EALFQGPPIY REIKISVAPE TPPPPVIADL LKSVDSEDVR EYCKEKGWLI PEVNSTLQIE
     KYVSRAFICL QAITTFVSVA GIIYIIYKLF AGFQGAYTGI PNQKPKVPTL RQAKVQGPAF
     EFAVAMMKRN SSTVKTEYGE FTMLGIYDRW AVLPRHAKPG PTILMNDQEV GVMDAKELVD
     KDGTNLELTL LKLNRNEKFR DIRGFLAKEE MEVNEAVLAI NTSKFPNMYI PVGQVTDYGF
     LNLGGTPTKR MLMYNFPTRA GQCGGVLMST GKVLGIHVGG NGHQGFSAAL LKHYFNDEQG
     EIEFIESSKD AGFPIINTPS KTKLEPSVFH QVFEGVKEPA VLRNGDPRLK ANFEEAIFSK
     YIGNVNTHVD EYMLEAVDHY AGQLATLDIS TEPMKLEDAV YGTEGLEALD LTTSAGYPYV
     ALGIKKRDIL SKKTRDLTKL KECMDKYGLN LPMITYVKDQ LRSAEKVAKG KSRLIEASSL
     NDSVAMRQTF GNLYKTFHLN PGIVTGSAVG CDPDLFWSKI PVMLNGHLIA FDYSGYDASL
     SPVWFACLKL LLEKLGYSHK ETNYIDYLCN SHHLYRDKHY FVRGGMPSGC SGTSIFNSMI
     NNIIIRTLML KVYKGIDLDQ FRMIAYGDDV IASYPWPIDA SLLAEAGKDY GLIMTPADKG
     ECFNEVTWTN VTFLKRYFRA DEQYPFLVHP VMPMKDIHES IRWTKDPKNT QDHVRSLCLL
     AWHNGEHEYE EFIRKIRSVP VGRCLTLPAF STLRRKWLDS F
//