POLG_HRV16
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 03-AUG-2022, entry version 188.
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; 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 (PROTEIN 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 PRIDE; Q82122; -.
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:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
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:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
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-directed 5'-3' 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: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:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0044694; P:pore-mediated entry of viral genome into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039690; P:positive stranded viral RNA replication; IDA:UniProtKB.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; 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; ISS:UniProtKB.
DR GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; ISS:UniProtKB.
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:0006351; P:transcription, DNA-templated; IEA:InterPro.
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 CDD; cd00205; rhv_like; 3.
DR Gene3D; 2.40.10.10; -; 4.
DR Gene3D; 2.60.120.20; -; 3.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 6.10.20.20; -; 1.
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; SSF50494; SSF50494; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF89043; SSF89043; 1.
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
