ID   POLG_HRV16              Reviewed;        2153 AA.
AC   Q82122;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   24-JAN-2024, entry version 194.
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 16 (HRV-16).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Ensavirinae; Enterovirus; Rhinovirus A.
OX   NCBI_TaxID=31708;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=7732663; DOI=10.1007/bf01702661;
RA   Lee W.M., Wang W., Rueckert R.R.;
RT   "Complete sequence of the RNA genome of human rhinovirus 16, a clinically
RT   useful common cold virus belonging to the ICAM-1 receptor group.";
RL   Virus Genes 9:177-181(1995).
RN   [2]
RP   FUNCTION (PROTEASE 3C).
RX   PubMed=19403669; DOI=10.1128/jvi.01748-08;
RA   Ghildyal R., Jordan B., Li D., Dagher H., Bardin P.G., Gern J.E.,
RA   Jans D.A.;
RT   "Rhinovirus 3C protease can localize in the nucleus and alter active and
RT   passive nucleocytoplasmic transport.";
RL   J. Virol. 83:7349-7352(2009).
RN   [3]
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).
RN   [4]
RP   FUNCTION (PROTEASE 3C).
RX   PubMed=33093214; DOI=10.1126/science.aay2002;
RA   Robinson K.S., Teo D.E.T., Tan K.S., Toh G.A., Ong H.H., Lim C.K., Lay K.,
RA   Au B.V., Lew T.S., Chu J.J.H., Chow V.T.K., Wang Y., Zhong F.L.,
RA   Reversade B.;
RT   "Enteroviral 3C protease activates the human NLRP1 inflammasome in airway
RT   epithelia.";
RL   Science 0:0-0(2020).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-853.
RX   PubMed=7915182; DOI=10.1016/0969-2126(93)90008-5;
RA   Oliveira M.A., Zhao R., Lee W.M., Kremer M.J., Minor I., Rueckert R.R.,
RA   Diana G.D., Pevear D.C., Dutko F.J., McKinlay M.A., Rossmann M.G.;
RT   "The structure of human rhinovirus 16.";
RL   Structure 1:51-68(1993).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-853, AND SEQUENCE REVISION TO
RP   547-548.
RX   PubMed=9083115; DOI=10.1016/s0969-2126(97)00199-8;
RA   Hadfield A.T., Lee W.M., Zhao R., Oliveira M.A., Minor I., Rueckert R.R.,
RA   Rossmann M.G.;
RT   "The refined structure of human rhinovirus 16 at 2.15-A resolution:
RT   implications for the viral life cycle.";
RL   Structure 5:427-441(1997).
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, ECO:0000250|UniProtKB:P04936}.
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 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:P04936}.
CC   -!- FUNCTION: [Viral protein genome-linked]: Acts as a primer for viral RNA
CC       replication and remains covalently bound to viral genomic RNA. VPg is
CC       uridylylated prior to priming replication into VPg-pUpU (By
CC       similarity). The oriI viral genomic sequence may act as a template for
CC       this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by
CC       the RNA-dependent RNA polymerase to replicate the viral genome (By
CC       similarity). Following genome release from the infecting virion in the
CC       cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By
CC       similarity). During the late stage of the replication cycle, host TDP2
CC       is excluded from sites of viral RNA synthesis and encapsidation,
CC       allowing for the generation of progeny virions (By similarity).
CC       {ECO:0000250|UniProtKB:P03300}.
CC   -!- FUNCTION: [Protein 3CD]: Involved in the viral replication complex and
CC       viral polypeptide maturation. It exhibits protease activity with a
CC       specificity and catalytic efficiency that is different from protease
CC       3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the
CC       5'UTR of the viral genome. {ECO:0000250|UniProtKB:P03300}.
CC   -!- FUNCTION: [Protease 3C]: Major viral protease that mediates proteolytic
CC       processing of the polyprotein (By similarity). Cleaves host EIF5B,
CC       contributing to host translation shutoff (By similarity). Cleaves also
CC       host PABPC1, contributing to host translation shutoff (By similarity).
CC       Cleaves host NLRP1, triggers host N-glycine-mediated degradation of the
CC       autoinhibitory NLRP1 N-terminal fragment (PubMed:33093214).
CC       {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03313,
CC       ECO:0000269|PubMed:33093214}.
CC   -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genomic
CC       RNA on the surface of intracellular membranes. May form linear arrays
CC       of subunits that propagate along a strong head-to-tail interaction
CC       called interface-I. Covalently attaches UMP to a tyrosine of VPg, which
CC       is used to prime RNA synthesis. The positive stranded RNA genome is
CC       first replicated at virus induced membranous vesicles, creating a dsRNA
CC       genomic replication form. This dsRNA is then used as template to
CC       synthesize positive stranded RNA genomes. ss(+)RNA genomes are either
CC       translated, replicated or encapsidated. {ECO:0000250|UniProtKB:P03300}.
CC   -!- CATALYTIC ACTIVITY: [Protein 2C]:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC         Evidence={ECO:0000250|UniProtKB:P03300};
CC   -!- CATALYTIC ACTIVITY: [Protease 2A]:
CC       Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus
CC         polyprotein.; EC=3.4.22.29; Evidence={ECO:0000250|UniProtKB:P03300};
CC   -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY: [Protease 3C]:
CC       Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus
CC         polyprotein. In other picornavirus reactions Glu may be substituted
CC         for Gln, and Ser or Thr for Gly.; EC=3.4.22.28;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU01222};
CC   -!- COFACTOR: [RNA-directed RNA polymerase]:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P03300};
CC       Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal
CC       center (By similarity). The magnesium ions are not prebound but only
CC       present for catalysis (By similarity). Requires the presence of 3CDpro
CC       or 3CPro (By similarity). {ECO:0000250|UniProtKB:P03300,
CC       ECO:0000250|UniProtKB:P03313};
CC   -!- ACTIVITY REGULATION: [RNA-directed RNA polymerase]: Replication or
CC       transcription is subject to high level of random mutations by the
CC       nucleotide analog ribavirin. {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [Capsid protein VP0]: Interacts with capsid protein VP1 and
CC       capsid protein VP3 to form heterotrimeric protomers.
CC       {ECO:0000250|UniProtKB:P03300}.
CC   -!- SUBUNIT: [Capsid protein VP1]: Interacts with capsid protein VP0, and
CC       capsid protein VP3 to form heterotrimeric protomers (By similarity).
CC       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
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 at high resolution;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1aym";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1ayn";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure in complex with antiviral drug VP63843 (pleconaril);
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1c8m";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure in complex with a two-domain fragment of its cellular
CC       receptor ICAM1;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1d3e";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure in complex with antiviral compound pleconaril;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1ncr";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1nd2";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure in complex with antiviral compound pleconaril;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1nd3";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure in complex with antiviral compound VP61209;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1qju";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure in complex with antiviral compound WIN68934;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1qjx";
CC   -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC       structure in complex with antiviral compound VP65099;
CC       URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1qjy";
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DR   EMBL; L24917; AAA69862.1; -; Genomic_RNA.
DR   PDB; 1AYM; X-ray; 2.15 A; 1=569-853, 2=70-330, 3=331-568.
DR   PDB; 1AYN; X-ray; 2.90 A; 1=569-853, 2=70-330, 3=331-568.
DR   PDB; 1C8M; X-ray; 2.80 A; 1=569-853, 2=79-330, 3=331-568, 4=2-78.
DR   PDB; 1D3E; EM; 28.00 A; 1=570-853, 2=79-330, 3=331-568, 4=2-69.
DR   PDB; 1NCR; X-ray; 2.70 A; A=569-853, B=70-330, C=331-568, D=2-69.
DR   PDB; 1ND2; X-ray; 2.50 A; A=569-853, B=70-330, C=331-568, D=2-69.
DR   PDB; 1ND3; X-ray; 2.80 A; A=569-853, B=70-330, C=331-568, D=2-69.
DR   PDB; 1QJU; X-ray; 2.80 A; 1=569-853, 2=70-330, 3=331-568, 4=2-69.
DR   PDB; 1QJX; X-ray; 2.80 A; 1=569-853, 2=70-330, 3=331-568, 4=2-69.
DR   PDB; 1QJY; X-ray; 2.80 A; 1=569-853, 2=70-330, 3=331-568, 4=2-69.
DR   PDB; 1TP7; X-ray; 2.40 A; A/B/C/D=1694-2153.
DR   PDB; 1XR7; X-ray; 2.30 A; A/B=1694-2153.
DR   PDB; 4K50; X-ray; 2.93 A; A/E/I/M=1694-2153.
DR   PDBsum; 1AYM; -.
DR   PDBsum; 1AYN; -.
DR   PDBsum; 1C8M; -.
DR   PDBsum; 1D3E; -.
DR   PDBsum; 1NCR; -.
DR   PDBsum; 1ND2; -.
DR   PDBsum; 1ND3; -.
DR   PDBsum; 1QJU; -.
DR   PDBsum; 1QJX; -.
DR   PDBsum; 1QJY; -.
DR   PDBsum; 1TP7; -.
DR   PDBsum; 1XR7; -.
DR   PDBsum; 4K50; -.
DR   SMR; Q82122; -.
DR   BindingDB; Q82122; -.
DR   ChEMBL; CHEMBL5296; -.
DR   DrugBank; DB08715; 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[2-METHYL-4-ISOXAZOLYL]-PHENOL.
DR   DrugBank; DB08713; 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[2N-METHYL-2H-TETRAZOL-5-YL]-PHENOL.
DR   DrugBank; DB08714; 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL.
DR   DrugBank; DB03017; Lauric acid.
DR   DrugBank; DB08231; Myristic acid.
DR   MEROPS; C03.007; -.
DR   MEROPS; N08.001; -.
DR   BRENDA; 2.7.7.48; 2703.
DR   BRENDA; 3.4.22.28; 2703.
DR   EvolutionaryTrace; Q82122; -.
DR   Proteomes; UP000007680; 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; IDA:UniProtKB.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 6.10.20.20; Poliovirus 3A protein-like; 1.
DR   Gene3D; 4.10.880.10; Poliovirus 3D polymerase Domain 1 (Nucleotidyltransferase); 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 4.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR   InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014838; P3A.
DR   InterPro; IPR036203; P3A_soluble_dom.
DR   InterPro; IPR044067; PCV_3C_PRO.
DR   InterPro; IPR000081; Peptidase_C3.
DR   InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR003138; Pico_P1A.
DR   InterPro; IPR002527; Pico_P2B.
DR   InterPro; IPR001676; Picornavirus_capsid.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR033703; Rhv-like.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF08727; P3A; 1.
DR   Pfam; PF00548; Peptidase_C3; 1.
DR   Pfam; PF02226; Pico_P1A; 1.
DR   Pfam; PF00947; Pico_P2A; 1.
DR   Pfam; PF01552; Pico_P2B; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   Pfam; PF00073; Rhv; 3.
DR   Pfam; PF00910; RNA_helicase; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF88633; Positive stranded ssRNA viruses; 2.
DR   SUPFAM; SSF89043; Soluble domain of poliovirus core protein 3a; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR   PROSITE; PS51874; PCV_3C_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51218; SF3_HELICASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activation of host autophagy by virus; ATP-binding;
KW   Autocatalytic cleavage; Capsid protein; 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..2153
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000426551"
FT   CHAIN           2..853
FT                   /note="P1"
FT                   /id="PRO_0000426552"
FT   CHAIN           2..330
FT                   /note="Capsid protein VP0"
FT                   /id="PRO_0000426553"
FT   CHAIN           2..69
FT                   /note="Capsid protein VP4"
FT                   /id="PRO_0000426554"
FT   CHAIN           70..330
FT                   /note="Capsid protein VP2"
FT                   /id="PRO_0000426555"
FT   CHAIN           331..562
FT                   /note="Capsid protein VP3"
FT                   /id="PRO_0000426556"
FT   CHAIN           563..853
FT                   /note="Capsid protein VP1"
FT                   /id="PRO_0000426557"
FT   CHAIN           854..1412
FT                   /note="P2"
FT                   /id="PRO_0000426558"
FT   CHAIN           854..995
FT                   /note="Protease 2A"
FT                   /id="PRO_0000426559"
FT   CHAIN           996..1090
FT                   /note="Protein 2B"
FT                   /id="PRO_0000040041"
FT   CHAIN           1091..1412
FT                   /note="Protein 2C"
FT                   /id="PRO_0000040042"
FT   CHAIN           1413..2153
FT                   /note="P3"
FT                   /id="PRO_0000426560"
FT   CHAIN           1413..1510
FT                   /note="Protein 3AB"
FT                   /id="PRO_0000426561"
FT   CHAIN           1413..1489
FT                   /note="Protein 3A"
FT                   /id="PRO_0000040043"
FT   CHAIN           1490..1510
FT                   /note="Viral protein genome-linked"
FT                   /id="PRO_0000426562"
FT   CHAIN           1511..2153
FT                   /note="Protein 3CD"
FT                   /id="PRO_0000426563"
FT   CHAIN           1511..1693
FT                   /note="Protease 3C"
FT                   /id="PRO_0000426564"
FT   CHAIN           1694..2153
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000426565"
FT   TOPO_DOM        2..1466
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        1467..1482
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1483..2153
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1186..1346
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1511..1689
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          1921..2034
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   ZN_FING         1353..1369
FT                   /note="C4-type; degenerate"
FT                   /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT   REGION          565..582
FT                   /note="Amphipathic alpha-helix"
FT                   /evidence="ECO:0000255"
FT   REGION          1091..1224
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1091..1160
FT                   /note="Membrane-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1112..1116
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1396..1403
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   REGION          1407..1412
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        871
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        888
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        959
FT                   /note="For protease 2A activity"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   ACT_SITE        1550
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1581
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1657
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   BINDING         905
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P04936"
FT   BINDING         907
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P04936"
FT   BINDING         965
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P04936"
FT   BINDING         967
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P04936"
FT   BINDING         1353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT   BINDING         1364
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT   BINDING         1369
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT   BINDING         1927
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         1927
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         2020
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         2020
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            853..854
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            995..996
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1090..1091
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1115
FT                   /note="Involved in the interaction with host RTN3"
FT                   /evidence="ECO:0000250|UniProtKB:Q66478"
FT   SITE            1412..1413
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1489..1490
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1510..1511
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   SITE            1693..1694
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03301"
FT   MOD_RES         1492
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   CONFLICT        547..548
FT                   /note="KD -> NH (in Ref. 1; AAA69862)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..5
FT                   /evidence="ECO:0007829|PDB:1ND2"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:1ND2"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:1ND2"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:1ND2"
FT   STRAND          83..87
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          90..96
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           103..105
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   TURN            113..115
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           126..128
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          138..140
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          147..151
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           153..155
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           159..167
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          168..180
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          188..197
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          204..206
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           213..216
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           219..221
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   TURN            225..227
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           239..241
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   TURN            242..245
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           248..253
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          254..260
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   TURN            261..263
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          265..271
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          276..280
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   TURN            282..284
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          288..299
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          307..323
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   TURN            338..341
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          353..355
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          369..372
FT                   /evidence="ECO:0007829|PDB:1ND2"
FT   HELIX           374..377
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   TURN            389..393
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           395..398
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          399..402
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          406..409
FT                   /evidence="ECO:0007829|PDB:1C8M"
FT   STRAND          411..416
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   TURN            422..426
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           428..433
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          436..441
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          443..449
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          458..464
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          466..468
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           474..478
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          480..486
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          488..490
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          492..497
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          502..504
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          506..509
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           512..514
FT                   /evidence="ECO:0007829|PDB:1ND2"
FT   STRAND          518..525
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          537..545
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          550..554
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           570..579
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          582..584
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           605..607
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           615..618
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           631..633
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           635..639
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          643..651
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           656..659
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          660..665
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           672..678
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          681..701
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          707..713
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           726..729
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          731..739
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          746..749
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          754..760
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          764..769
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   TURN            776..779
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          784..789
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          798..816
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   HELIX           838..840
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          847..849
FT                   /evidence="ECO:0007829|PDB:1AYM"
FT   STRAND          1695..1701
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           1702..1705
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   TURN            1722..1726
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           1747..1751
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           1752..1754
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           1765..1779
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           1790..1795
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   STRAND          1805..1807
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   TURN            1811..1817
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           1820..1823
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   TURN            1826..1829
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           1832..1841
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   STRAND          1847..1851
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   STRAND          1854..1856
FT                   /evidence="ECO:0007829|PDB:1TP7"
FT   HELIX           1859..1862
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   STRAND          1868..1871
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           1874..1893
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   TURN            1897..1900
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           1907..1917
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   STRAND          1920..1930
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           1931..1934
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           1937..1949
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           1958..1961
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   STRAND          1962..1967
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   STRAND          1970..1977
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           1985..2004
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           2010..2012
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   STRAND          2014..2018
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   STRAND          2021..2028
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           2032..2037
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           2038..2042
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   STRAND          2046..2049
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   TURN            2060..2062
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   STRAND          2068..2072
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   STRAND          2079..2083
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           2086..2093
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   STRAND          2095..2097
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           2099..2101
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           2102..2113
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           2114..2116
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           2118..2128
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           2132..2135
FT                   /evidence="ECO:0007829|PDB:1XR7"
FT   HELIX           2142..2150
FT                   /evidence="ECO:0007829|PDB:1XR7"
SQ   SEQUENCE   2153 AA;  242244 MW;  6B11D0D93DF11C04 CRC64;
     MGAQVSRQNV GTHSTQNMVS NGSSLNYFNI NYFKDAASSG ASRLDFSQDP SKFTDPVKDV
     LEKGIPTLQS PSVEACGYSD RIIQITRGDS TITSQDVANA VVGYGVWPHY LTPQDATAID
     KPTQPDTSSN RFYTLDSKMW NSTSKGWWWK LPDALKDMGI FGENMFYHFL GRSGYTVHVQ
     CNASKFHQGT LLVVMIPEHQ LATVNKGNVN AGYKYTHPGE AGREVGTQVE NEKQPSDDNW
     LNFDGTLLGN LLIFPHQFIN LRSNNSATLI VPYVNAVPMD SMVRHNNWSL VIIPVCQLQS
     NNISNIVPIT VSISPMCAEF SGARAKTVVQ GLPVYVTPGS GQFMTTDDMQ SPCALPWYHP
     TKEIFIPGEV KNLIEMCQVD TLIPINSTQS NIGNVSMYTV TLSPQTKLAE EIFAIKVDIA
     SHPLATTLIG EIASYFTHWT GSLRFSFMFC GTANTTLKVL LAYTPPGIGK PRSRKEAMLG
     THVVWDVGLQ STVSLVVPWI SASQYRFTTP DTYSSAGYIT CWYQTNFVVP PNTPNTAEML
     CFVSGCKDFC LRMARDTDLH KQTGPITQNP VERYVDEVLN EVLVVPNINQ SHPTTSNAAP
     VLDAAETGHT NKIQPEDTIE TRYVQSSQTL DEMSVESFLG RSGCIHESVL DIVDNYNDQS
     FTKWNINLQE MAQIRRKFEM FTYARFDSEI TMVPSVAAKD GHIGHIVMQY MYVPPGAPIP
     TTRDDYAWQS GTNASVFWQH GQPFPRFSLP FLSIASAYYM FYDGYDGDTY KSRYGTVVTN
     DMGTLCSRIV TSEQLHKVKV VTRIYHKAKH TKAWCPRPPR AVQYSHTHTT NYKLSSEVHN
     DVAIRPRTNL TTVGPSDMYV HVGNLIYRNL HLFNSDIHDS ILVSYSSDLI IYRTSTQGDG
     YIPTCNCTEA TYYCKHKNRY YPINVTPHDW YEIQESEYYP KHIQYNLLIG EGPCEPGDCG
     GKLLCKHGVI GIITAGGEGH VAFIDLRHFH CAEEQGITDY IHMLGEAFGS GFVDSVKDQI
     NSINPINNIS SKMVKWMLRI ISAMVIIIRN SSDPQTIIAT LTLIGCNGSP WRFLKEKFCK
     WTQLTYIHKE SDSWLKKFTE MCNAARGLEW IGNKISKFID WMKSMLPQAQ LKVKYLSELK
     KLNFLEKQVE NLRAADTNTQ EKIKCEIDTL HDLSCKFLPL YASEAKRIKV LYHKCTNIIK
     QKKRSEPVAV MIHGPPGTGK SITTSFLARM ITNESDIYSL PPDPKYFDGY DNQSVVIMDD
     IMQNPGGEDM TLFCQMVSSV TFIPPMADLP DKGKPFDSRF VLCSTNHSLL APPTISSLPA
     MNRRFYLDLD ILVHDNYKDN QGKLDVSRAF RLCDVDSKIG NAKCCPFVCG KAVTFKDRNT
     CRTYSLSQIY NQILEEDKRR RQVVDVMSAI FQGPISMDKP PPPAITDLLR SVRTPEVIKY
     CQDNKWIVPA DCQIERDLNI ANSIITIIAN IISIAGIIYI IYKLFCSLQG PYSGEPKPKT
     KVPERRVVAQ GPEEEFGMSI IKNNTCVVTT TNGKFTGLGI YDRILILPTH ADPGSEIQVN
     GIHTKVLDSY DLFNKEGVKL EITVLKLDRN EKFRDIRKYI PESEDDYPEC NLALVANQTE
     PTIIKVGDVV SYGNILLSGT QTARMLKYNY PTKSGYCGGV LYKIGQILGI HVGGNGRDGF
     SSMLLRSYFT EQQGQIQISK HVKDVGLPSI HTPTKTKLQP SVFYDIFPGS KEPAVLTEKD
     PRLKVDFDSA LFSKYKGNTE CSLNEHIQVA VAHYSAQLAT LDIDPQPIAM EDSVFGMDGL
     EALDLNTSAG YPYVTLGIKK KDLINNKTKD ISKLKLALDK YDVDLPMITF LKDELRKKDK
     IAAGKTRVIE ASSINDTILF RTVYGNLFSK FHLNPGVVTG CAVGCDPETF WSKIPLMLDG
     DCIMAFDYTN YDGSIHPIWF KALGMVLDNL SFNPTLINRL CNSKHIFKST YYEVEGGVPS
     GCSGTSIFNS MINNIIIRTL VLDAYKHIDL DKLKIIAYGD DVIFSYKYKL DMEAIAKEGQ
     KYGLTITPAD KSSEFKELDY GNVTFLKRGF RQDDKYKFLI HPTFPVEEIY ESIRWTKKPS
     QMQEHVLSLC HLMWHNGPEI YKDFETKIRS VSAGRALYIP PYELLRHEWY EKF
//