ID   POLG_HRV3               Reviewed;        2178 AA.
AC   Q82081; A5GZD4; A7KC14;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2013, sequence version 4.
DT   24-JAN-2024, entry version 151.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=P1;
DE   Contains:
DE     RecName: Full=Capsid protein VP0;
DE     AltName: Full=VP4-VP2;
DE   Contains:
DE     RecName: Full=Capsid protein VP4;
DE     AltName: Full=P1A;
DE     AltName: Full=Virion protein 4;
DE   Contains:
DE     RecName: Full=Capsid protein VP2;
DE     AltName: Full=P1B;
DE     AltName: Full=Virion protein 2;
DE   Contains:
DE     RecName: Full=Capsid protein VP3;
DE     AltName: Full=P1C;
DE     AltName: Full=Virion protein 3;
DE   Contains:
DE     RecName: Full=Capsid protein VP1;
DE     AltName: Full=P1D;
DE     AltName: Full=Virion protein 1;
DE   Contains:
DE     RecName: Full=P2;
DE   Contains:
DE     RecName: Full=Protease 2A;
DE              Short=P2A;
DE              EC=3.4.22.29 {ECO:0000250|UniProtKB:P03300};
DE     AltName: Full=Picornain 2A;
DE     AltName: Full=Protein 2A;
DE   Contains:
DE     RecName: Full=Protein 2B;
DE              Short=P2B;
DE   Contains:
DE     RecName: Full=Protein 2C;
DE              Short=P2C;
DE              EC=3.6.1.15 {ECO:0000250|UniProtKB:P03300};
DE   Contains:
DE     RecName: Full=P3;
DE   Contains:
DE     RecName: Full=Protein 3AB;
DE   Contains:
DE     RecName: Full=Protein 3A;
DE              Short=P3A;
DE   Contains:
DE     RecName: Full=Viral protein genome-linked;
DE              Short=VPg;
DE     AltName: Full=Protein 3B;
DE              Short=P3B;
DE   Contains:
DE     RecName: Full=Protein 3CD;
DE              EC=3.4.22.28;
DE   Contains:
DE     RecName: Full=Protease 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE              EC=3.4.22.28 {ECO:0000255|PROSITE-ProRule:PRU01222};
DE     AltName: Full=Picornain 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE              Short=P3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase {ECO:0000255|PROSITE-ProRule:PRU00539};
DE              Short=RdRp;
DE              EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE     AltName: Full=3D polymerase;
DE              Short=3Dpol;
DE     AltName: Full=Protein 3D;
DE              Short=3D;
OS   Human rhinovirus 3 (HRV-3).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Ensavirinae; Enterovirus; Rhinovirus B.
OX   NCBI_TaxID=44130;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=17477878; DOI=10.1186/1743-422x-4-40;
RA   Kistler A.L., Webster D.R., Rouskin S., Magrini V., Credle J.J.,
RA   Schnurr D.P., Boushey H.A., Mardis E.R., Li H., DeRisi J.L.;
RT   "Genome-wide diversity and selective pressure in the human rhinovirus.";
RL   Virol. J. 4:40-40(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Tapparel C., Junier T., Gerlach D., Cordey S., Van Belle S., Perrin L.,
RA   Zdobnov E.M., Kaiser L.;
RT   "New complete genome sequences of human rhinoviruses shed light on their
RT   phylogeny and genomic features.";
RL   BMC Genomics 8:224-224(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-855, AND X-RAY CRYSTALLOGRAPHY (3.0
RP   ANGSTROMS).
RX   PubMed=8939746; DOI=10.1016/s0969-2126(96)00128-1;
RA   Zhao R., Pevear D.C., Kremer M.J., Giranda V.L., Kofron J.A., Kuhn R.J.,
RA   Rossmann M.G.;
RT   "Human rhinovirus 3 at 3.0-A resolution.";
RL   Structure 4:1205-1220(1996).
RN   [4]
RP   REVIEW.
RX   PubMed=23227049; DOI=10.1155/2012/826301;
RA   Fuchs R., Blaas D.;
RT   "Productive entry pathways of human rhinoviruses.";
RL   Adv. Virol. 2012:826301-826301(2012).
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 (By similarity). This
CC       attachment induces virion internalization (By similarity). Tyrosine
CC       kinases are probably involved in the entry process (By similarity).
CC       After binding to its receptor, the capsid undergoes conformational
CC       changes (By similarity). Capsid protein VP1 N-terminus (that contains
CC       an amphipathic alpha-helix) and capsid protein VP4 are externalized (By
CC       similarity). Together, they shape a pore in the host membrane through
CC       which viral genome is translocated to host cell cytoplasm (By
CC       similarity). {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). {ECO:0000250|UniProtKB:P03300,
CC       ECO:0000250|UniProtKB:P03301}.
CC   -!- FUNCTION: [Protein 2B]: Plays an essential role in the virus
CC       replication cycle by acting as a viroporin. Creates a pore in the host
CC       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: [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).
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:0000250|UniProtKB:P04936}.
CC   -!- SUBUNIT: [Protein 2C]: Homohexamer; forms a hexameric ring structure
CC       with 6-fold symmetry characteristic of AAA+ ATPases (By similarity).
CC       Interacts (via N-terminus) with host RTN3 (via reticulon domain); this
CC       interaction is important for viral replication (By similarity).
CC       Interacts with capsid protein VP3; this interaction may be important
CC       for virion morphogenesis (By similarity).
CC       {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [Protein 3AB]: Interacts with protein 3CD.
CC       {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [Protein 3A]: Homodimer (By similarity). Interacts with host
CC       GBF1 (By similarity). Interacts (via GOLD domain) with host ACBD3 (via
CC       GOLD domain); this interaction allows the formation of a viral protein
CC       3A/ACBD3 heterotetramer with a 2:2 stoichiometry, which will stimulate
CC       the recruitment of host PI4KB in order to synthesize PI4P at the viral
CC       RNA replication sites (By similarity). {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [Viral protein genome-linked]: Interacts with RNA-directed RNA
CC       polymerase. {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [Protein 3CD]: Interacts with protein 3AB and with RNA-
CC       directed RNA polymerase. {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [RNA-directed RNA polymerase]: Interacts with Viral protein
CC       genome-linked and with protein 3CD. {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion
CC       {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
CC       {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC       {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC       side {ECO:0000305}. Note=Probably localizes to the surface of
CC       intracellular membrane vesicles that are induced after virus infection
CC       as the site for viral RNA replication. These vesicles are derived from
CC       the endoplasmic reticulum.
CC   -!- SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC       side {ECO:0000305}. Note=Probably localizes to the surface of
CC       intracellular membrane vesicles that are induced after virus infection
CC       as the site for viral RNA replication. These vesicles are derived from
CC       the endoplasmic reticulum.
CC   -!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC       side {ECO:0000305}. Note=Probably localizes to the surface of
CC       intracellular membrane vesicles that are induced after virus infection
CC       as the site for viral RNA replication. These vesicles are derived from
CC       the endoplasmic reticulum.
CC   -!- SUBCELLULAR LOCATION: [Protein 3AB]: Host cytoplasmic vesicle membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC       side {ECO:0000305}. Note=Probably localizes to the surface of
CC       intracellular membrane vesicles that are induced after virus infection
CC       as the site for viral RNA replication. These vesicles are derived from
CC       the endoplasmic reticulum.
CC   -!- SUBCELLULAR LOCATION: [Viral protein genome-linked]: Virion
CC       {ECO:0000250|UniProtKB:P03300}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:Q66478}.
CC   -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm.
CC   -!- SUBCELLULAR LOCATION: [Protein 3CD]: Host nucleus
CC       {ECO:0000250|UniProtKB:P03300}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:P03300}. Host cytoplasmic vesicle membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC       side {ECO:0000305}. Note=Probably localizes to the surface of
CC       intracellular membrane vesicles that are induced after virus infection
CC       as the site for viral RNA replication. These vesicles are derived from
CC       the endoplasmic reticulum.
CC   -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic
CC       vesicle membrane {ECO:0000305}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes
CC       to the surface of intracellular membrane vesicles that are induced
CC       after virus infection as the site for viral RNA replication. These
CC       vesicles are derived from the endoplasmic reticulum.
CC   -!- DOMAIN: [Protein 2C]: The N-terminus has membrane-binding (By
CC       similarity). The N-terminus also displays RNA-binding properties (By
CC       similarity). The N-terminus is involved in oligomerization (By
CC       similarity). The central part contains an ATPase domain and a C4-type
CC       zinc-finger (By similarity). The C-terminus is involved in RNA-binding
CC       (By similarity). The extreme C-terminus contains a region involved in
CC       oligomerization (By similarity). {ECO:0000250|UniProtKB:P03300}.
CC   -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the
CC       viral proteases yield processing intermediates and the mature proteins.
CC       {ECO:0000250|UniProtKB:P03300}.
CC   -!- PTM: [Capsid protein VP0]: Myristoylation is required for the formation
CC       of pentamers during virus assembly. Further assembly of 12 pentamers
CC       and a molecule of genomic RNA generates the provirion.
CC       {ECO:0000250|UniProtKB:P03300}.
CC   -!- PTM: [Capsid protein VP0]: During virion maturation, immature virions
CC       are rendered infectious following cleavage of VP0 into VP4 and VP2.
CC       This maturation seems to be an autocatalytic event triggered by the
CC       presence of RNA in the capsid and it is followed by a conformational
CC       change infectious virion. {ECO:0000250|UniProtKB:P03300}.
CC   -!- PTM: [Capsid protein VP4]: Myristoylation is required during RNA
CC       encapsidation and formation of the mature virus particle.
CC       {ECO:0000250|UniProtKB:P03300}.
CC   -!- PTM: [Viral protein genome-linked]: VPg is uridylylated by the
CC       polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for
CC       the genomic RNA replication. {ECO:0000250|UniProtKB:P03300}.
CC   -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1rhi";
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DR   EMBL; DQ473485; ABF51179.1; -; Genomic_RNA.
DR   EMBL; EF173422; ABO69378.1; -; Genomic_RNA.
DR   EMBL; U60874; AAB05616.1; -; Genomic_RNA.
DR   PDB; 1RHI; X-ray; 3.00 A; 1=568-855, 2=70-331, 3=332-567, 4=2-69.
DR   PDBsum; 1RHI; -.
DR   SMR; Q82081; -.
DR   MEROPS; C03.013; -.
DR   MEROPS; C03.020; -.
DR   MEROPS; N08.001; -.
DR   EvolutionaryTrace; Q82081; -.
DR   Proteomes; UP000013737; Genome.
DR   Proteomes; UP000165566; Genome.
DR   GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO: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; 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; 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   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..2178
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000426521"
FT   CHAIN           2..855
FT                   /note="P1"
FT                   /id="PRO_0000426522"
FT   CHAIN           2..331
FT                   /note="Capsid protein VP0"
FT                   /id="PRO_0000426523"
FT   CHAIN           2..69
FT                   /note="Capsid protein VP4"
FT                   /id="PRO_0000426524"
FT   CHAIN           70..331
FT                   /note="Capsid protein VP2"
FT                   /id="PRO_0000426525"
FT   CHAIN           332..561
FT                   /note="Capsid protein VP3"
FT                   /id="PRO_0000426526"
FT   CHAIN           562..855
FT                   /note="Capsid protein VP1"
FT                   /id="PRO_0000426527"
FT   CHAIN           856..1428
FT                   /note="P2"
FT                   /id="PRO_0000426528"
FT   CHAIN           856..1001
FT                   /note="Protease 2A"
FT                   /id="PRO_0000423099"
FT   CHAIN           1002..1098
FT                   /note="Protein 2B"
FT                   /id="PRO_0000423100"
FT   CHAIN           1099..1428
FT                   /note="Protein 2C"
FT                   /id="PRO_0000426529"
FT   CHAIN           1429..2178
FT                   /note="P3"
FT                   /id="PRO_0000426530"
FT   CHAIN           1429..1536
FT                   /note="Protein 3AB"
FT                   /id="PRO_0000426531"
FT   CHAIN           1429..1513
FT                   /note="Protein 3A"
FT                   /id="PRO_0000423102"
FT   CHAIN           1514..1536
FT                   /note="Viral protein genome-linked"
FT                   /id="PRO_0000426532"
FT   CHAIN           1537..2178
FT                   /note="Protein 3CD"
FT                   /id="PRO_0000426533"
FT   CHAIN           1537..1718
FT                   /note="Protease 3C"
FT                   /id="PRO_0000426534"
FT   CHAIN           1719..2178
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000426535"
FT   TOPO_DOM        2..1490
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        1491..1506
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1507..2178
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1204..1360
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1537..1714
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          1946..2059
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   ZN_FING         1368..1385
FT                   /note="C4-type"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..584
FT                   /note="Amphipathic alpha-helix"
FT                   /evidence="ECO:0000255"
FT   REGION          1100..1238
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1100..1172
FT                   /note="Membrane-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1121..1125
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1412..1419
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1423..1428
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        875
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        893
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        964
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        1576
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1607
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1682
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   BINDING         910
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         912
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         970
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         972
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         1368
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1371
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1380
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1385
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   BINDING         1951
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         1951
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         2045
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         2045
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            331..332
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            855..856
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1001..1002
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1098..1099
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1124
FT                   /note="Involved in the interaction with host RTN3"
FT                   /evidence="ECO:0000250|UniProtKB:Q66478"
FT   SITE            1428..1429
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1513..1514
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1536..1537
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1718..1719
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   MOD_RES         1516
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   VARIANT         87
FT                   /note="L -> M"
FT   VARIANT         98
FT                   /note="A -> R"
FT   VARIANT         260
FT                   /note="L -> M"
FT   VARIANT         475
FT                   /note="E -> K"
FT   VARIANT         523
FT                   /note="Q -> L"
FT   VARIANT         846
FT                   /note="I -> V"
FT   VARIANT         1349
FT                   /note="M -> L"
FT   VARIANT         1389
FT                   /note="I -> V"
FT   VARIANT         1703
FT                   /note="R -> Q"
FT   VARIANT         1925
FT                   /note="E -> G"
FT   VARIANT         1978
FT                   /note="Q -> H"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           51..54
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          83..87
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          90..96
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           103..105
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   TURN            113..115
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           126..128
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          138..140
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          147..151
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           153..155
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           159..165
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          168..180
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          188..197
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          203..205
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           213..216
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           219..221
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   TURN            238..244
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           247..252
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          253..259
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   TURN            260..262
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          264..270
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          275..279
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          281..284
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          286..298
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          307..323
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   TURN            339..342
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          354..356
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   TURN            374..379
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          390..392
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           395..398
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          399..402
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          410..415
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           421..423
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           427..432
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          435..440
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          442..448
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          457..463
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           473..476
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          479..485
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          487..489
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          491..496
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          501..503
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          505..508
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           511..513
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          517..524
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          536..544
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          549..553
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          585..587
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           604..606
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           614..616
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           630..632
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           634..637
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          642..651
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           660..663
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          665..669
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          673..676
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           677..683
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          686..702
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          714..720
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           733..736
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          738..740
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          742..746
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          749..755
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          760..766
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          770..774
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          776..778
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   HELIX           784..786
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          790..795
FT                   /evidence="ECO:0007829|PDB:1RHI"
FT   STRAND          804..822
FT                   /evidence="ECO:0007829|PDB:1RHI"
SQ   SEQUENCE   2178 AA;  242794 MW;  0DFED5280AF25CCF CRC64;
     MGAQVSTQKS GSHENQNILT NGSNQTFTVI NYYKDAASSS SAGQSFSMDP SKFTEPVKDL
     MLKGAPALNS PNVEACGYSD RVQQITLGNS TITTQEAANA IVCYAEWPEY LSDNDASDVN
     KTSKPDISVC RFYTLDSKTW KATSKGWCWK LPDALKDMGV FGQNMFYHSL GRTGYTIHVQ
     CNATKFHSGC LLVVVIPEHQ LASHEGGTVS VKYKYTHPGD RGIDLDTVEV AGGPTSDAIY
     NMDGTLLGNL LIFPHQFINL RTNNTATIVV PYINSVPIDS MTRHNNVSLM VVPIAPLNAP
     TGSSPTLPVT VTIAPMCTEF TGIRSRSIVP QGLPTTTLPG SGQFLTTDDR QSPSALPSYE
     PTPRIHIPGK VRNLLEIIQV GTLIPMNNTG TNDNVTNYLI PLHADRQNEQ IFGTKLYIGD
     GVFKTTLLGE IAQYYTHWSG SLRISLMYTG PALSSAKIIL AYTPPGTRGP EDRKEAMLGT
     HVVWDIGLQS TIVMTIPWTS GVQFRYTDPD TYTSAGYLSC WYQTSLILPP QTSGQVYLLS
     FISACPDFKL RLMKDTQTIS QTDALTEGLS DELEEVIVEK TKQTLASVSS GPKHTQSVPA
     LTANETGATL PTRPSDNVET RTTYMHFNGS ETDVESFLGR AACVHVTEIK NKNAAGLDNH
     RKEGLFNDWK INLSSLVQLR KKLELFTYVR FDSEYTILAT ASQPEASSYS SNLTVQAMYV
     PPGAPNPKEW DDYTWQSASN PSVFFKVGET SRFSVPFVGI ASAYNCFYDG YSHDDPDTPY
     GITVLNHMGS MAFRVVNEHD VHTTIVKIRV YHRAKHVEAW IPRAPRALPY VSIGRTNYPR
     DSKTIIKKRT NIKTYGLGPR FGGVFTSNVK IINYHLMTPD DHLNLVAPYP NRDLAVVATG
     AHGAETIPHC NCTSGVYYSR YYRKFYPIIC ERPTNIWIEG SSYYPSRYQA GVMKGVGPAE
     PGDCGGILRC IHGPIGLLTA GGGGYVCFAD IRQLDFIADE QGLGDYITSL GRAFGTGFTD
     QISAKVCELQ DVAKDFLTTK VLSKVVKMIS ALVIICRNHD DLVTVTATLA LLGCDGSPWR
     FLKMYISKHF QVPYIERQAN DGWFRKFNDA CNAAKGLEWI ANKISKLIEW IKNKVLPQAR
     EKLEFCSKLK QLDILERQIA SIHDSNPTQE KREQLFNNVL WLEQMSQKFS PLYASEAKRI
     RDLKNKITNY MQFKSKQRTE PVCVLIHGTP GSGKSLTTSI VGRALAEHFN SSVYSLPPDP
     KHFDGYQQQE VVIMDDLNQN PDGQDISMFC QMVSSVDFLP PMASLDNKGM LFTSNFVLAS
     TNSNTLSPPT ILNPEALIRR FGFDLDICMH STYTKNGKLN AAMATSLCKD CHQPSNFKKC
     CPLVCGKAIS LVDRVSNVRF SIDQLVTAII NDYKNKVKIT DSLEVLFQGP VYKDLEIDIC
     NTPPPECISD LLKSVDSEEV REYCKKKKWI IPQISTNIER AVNQASMIIN TILMFVSTLG
     IVYVIYKLFA QTQGPYSGNP VHNKLKPPTL KPVVVQGPNT EFALSLLRKN ILTITTEKGE
     FTSLGIHDRI CVLPTHAQPG DNVLVNGQKI QIKDKYKLVD PDNTNLELTI IELDRNEKFR
     DIRGFISEDL EGLDATLVVH SNGFTNTILD VGPITMAGLI NLSNTPTTRM IRYDYPTKTG
     QCGGVLCTTG KIFGIHVGGN GRRGFSAQLK KQYFVEKQGL IVSKQKVRDI GLNPINTPTK
     TKLHPSVFYN VFPGSKQPAV LNDNDPRLEV KLAESLFSKY KGNVQMEPTE NMLIAVDHYA
     GQLMSLDIST KELTLKEALY GVDGLEPIDV TTSAGYPYVS LGIKKRDILN KETQDVEKMK
     FYLDKYGIDL PLVTYIKDEL RSVDKVRLGK SRLIEASSLN DSVNMRMKLG NLYKAFHQNP
     GIITESAVGC DPDVFWSVIP CLMDGHLMAF DYSNFDASLS PVWFECLEKV LNKLGFKQPS
     LIQSICNTHH IFRDEIYRVE GGMPSGCSGT SIFNSMINNI IIRTLILDAY KGIDLDSLRI
     LAYGDDLIVS YPFELDSNIL AAIGKNYGLT ITPPDKSDAF TKITWENITF LKRYFRPDPQ
     FPFLIHPVMP MQDIYESIRW TRDPRNTQDH VRSLCMLAWH SGEKDYNDFI TKIRTTDIGK
     CLNLPEYSVL RRRWLDLF
//