POLG_ENMGO
ID POLG_ENMGO Reviewed; 2293 AA.
AC P12296; Q2V6G9;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Leader protein;
DE Short=L;
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=Rho;
DE AltName: Full=Virion protein 4;
DE Contains:
DE RecName: Full=Capsid protein VP2;
DE AltName: Full=Beta;
DE AltName: Full=P1B;
DE AltName: Full=Virion protein 2;
DE Contains:
DE RecName: Full=Capsid protein VP3;
DE AltName: Full=Gamma;
DE AltName: Full=P1C;
DE AltName: Full=Virion protein 3;
DE Contains:
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=Alpha;
DE AltName: Full=P1D;
DE AltName: Full=Virion protein 1;
DE Contains:
DE RecName: Full=Protein 2A;
DE Short=P2A;
DE AltName: Full=G;
DE Contains:
DE RecName: Full=Protein 2B;
DE Short=I;
DE Short=P2B;
DE Contains:
DE RecName: Full=Protein 2C;
DE Short=C;
DE Short=P2C;
DE EC=3.6.4.13;
DE Contains:
DE RecName: Full=Protein 3A;
DE Short=P3A;
DE Contains:
DE RecName: Full=VPg;
DE Short=P3B;
DE AltName: Full=H;
DE AltName: Full=Protein 3B;
DE Contains:
DE RecName: Full=Protease 3C;
DE Short=P3C;
DE EC=3.4.22.28 {ECO:0000269|PubMed:8972564};
DE AltName: Full=Picornain 3C;
DE AltName: Full=p22;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE Short=RdRp;
DE EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539, ECO:0000269|PubMed:24600002};
DE AltName: Full=3D polymerase;
DE Short=3Dpol;
DE AltName: Full=E;
DE AltName: Full=Protein 3D;
DE Short=3D;
DE Flags: Precursor;
OS Mengo encephalomyocarditis virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Cardiovirus.
OX NCBI_TaxID=12107;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Medium plague;
RX PubMed=16103157; DOI=10.1128/jvi.79.17.11062-11070.2005;
RA Fata-Hartley C.L., Palmenberg A.C.;
RT "Dipyridamole reversibly inhibits mengovirus RNA replication.";
RL J. Virol. 79:11062-11070(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 69-901, FUNCTION (CAPSID PROTEIN
RP VP1), FUNCTION (CAPSID PROTEIN VP2), FUNCTION (CAPSID PROTEIN VP3),
RP FUNCTION (CAPSID PROTEIN VP4), SUBCELLULAR LOCATION (CAPSID PROTEIN VP1),
RP SUBCELLULAR LOCATION (CAPSID PROTEIN VP2), AND SUBCELLULAR LOCATION (CAPSID
RP PROTEIN VP3).
RX PubMed=3026048; DOI=10.1126/science.3026048;
RA Luo M., Vriend G., Kamer G., Minor I., Arnold E., Rossmann M.G., Boege U.,
RA Scraba D.G., Duke G.M., Palmenberg A.C.;
RT "The atomic structure of Mengo virus at 3.0-A resolution.";
RL Science 235:182-191(1987).
RN [3]
RP CATALYTIC ACTIVITY (PROTEASE 3C), FUNCTION (PROTEASE 3C), PROTEOLYTIC
RP CLEAVAGE (GENOME POLYPROTEIN), AND BIOPHYSICOCHEMICAL PROPERTIES (PROTEASE
RP 3C).
RX PubMed=8972564; DOI=10.1007/bf00568903;
RA Hall D.J., Palmenberg A.C.;
RT "Mengo virus 3C proteinase: recombinant expression, intergenus substrate
RT cleavage and localization in vivo.";
RL Virus Genes 13:99-110(1996).
RN [4]
RP FUNCTION (PROTEIN 2A), AND SUBCELLULAR LOCATION (PROTEIN 2A).
RX PubMed=12921995; DOI=10.1016/s0168-1702(03)00162-x;
RA Aminev A.G., Amineva S.P., Palmenberg A.C.;
RT "Encephalomyocarditis viral protein 2A localizes to nucleoli and inhibits
RT cap-dependent mRNA translation.";
RL Virus Res. 95:45-57(2003).
RN [5]
RP RIBOSOMAL FRAMESHIFT.
RX PubMed=22025686; DOI=10.1073/pnas.1102932108;
RA Loughran G., Firth A.E., Atkins J.F.;
RT "Ribosomal frameshifting into an overlapping gene in the 2B-encoding region
RT of the cardiovirus genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:E1111-E1119(2011).
RN [6]
RP FUNCTION (PROTEIN 2A).
RX PubMed=28593994; DOI=10.1038/ncomms15582;
RA Napthine S., Ling R., Finch L.K., Jones J.D., Bell S., Brierley I.,
RA Firth A.E.;
RT "Protein-directed ribosomal frameshifting temporally regulates gene
RT expression.";
RL Nat. Commun. 8:15582-15582(2017).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SEQUENCE REVISION TO 451 AND 669,
RP FUNCTION (CAPSID PROTEIN VP1), FUNCTION (CAPSID PROTEIN VP2), FUNCTION
RP (CAPSID PROTEIN VP3), FUNCTION (CAPSID PROTEIN VP4), SUBCELLULAR LOCATION
RP (CAPSID PROTEIN VP1), SUBCELLULAR LOCATION (CAPSID PROTEIN VP2),
RP SUBCELLULAR LOCATION (CAPSID PROTEIN VP3), AND DISULFIDE BOND.
RX PubMed=2156078; DOI=10.1016/0022-2836(90)90077-y;
RA Krishnaswamy S., Rossmann M.G.;
RT "Structural refinement and analysis of Mengo virus.";
RL J. Mol. Biol. 211:803-844(1990).
RN [8] {ECO:0007744|PDB:1MEC}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 625-898; 138-393; 394-624 AND
RP 68-137.
RX PubMed=2155508; DOI=10.1016/0042-6822(90)90198-z;
RA Kim S., Boege U., Krishnaswamy S., Minor I., Smith T.J., Luo M.,
RA Scraba D.G., Rossmann M.G.;
RT "Conformational variability of a picornavirus capsid: pH-dependent
RT structural changes of Mengo virus related to its host receptor attachment
RT site and disassembly.";
RL Virology 175:176-190(1990).
RN [9] {ECO:0007744|PDB:4NYZ, ECO:0007744|PDB:4NZ0}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1834-2293, CATALYTIC ACTIVITY
RP (RNA-DIRECTED RNA POLYMERASE), FUNCTION (RNA-DIRECTED RNA POLYMERASE),
RP ACTIVE SITE (RNA-DIRECTED RNA POLYMERASE), AND URIDYLYLATION (VPG).
RX PubMed=24600002; DOI=10.1128/jvi.03502-13;
RA Vives-Adrian L., Lujan C., Oliva B., van der Linden L., Selisko B.,
RA Coutard B., Canard B., van Kuppeveld F.J., Ferrer-Orta C., Verdaguer N.;
RT "The crystal structure of a cardiovirus RNA-dependent RNA polymerase
RT reveals an unusual conformation of the polymerase active site.";
RL J. Virol. 88:5595-5607(2014).
RN [10] {ECO:0007744|PDB:2MMH, ECO:0007744|PDB:2MMI, ECO:0007744|PDB:2MMK, ECO:0007744|PDB:2MML}
RP STRUCTURE BY NMR OF 1-67, PHOSPHORYLATION AT TYR-41 AND THR-47,
RP ZINC-FINGER, AND INTERACTION WITH HOST RAN (LEADER PROTEIN).
RX PubMed=25331866; DOI=10.1073/pnas.1411098111;
RA Bacot-Davis V.R., Ciomperlik J.J., Basta H.A., Cornilescu C.C.,
RA Palmenberg A.C.;
RT "Solution structures of Mengovirus Leader protein, its phosphorylated
RT derivatives, and in complex with nuclear transport regulatory protein,
RT RanGTPase.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:15792-15797(2014).
RN [11] {ECO:0007744|PDB:4Y2C, ECO:0007744|PDB:4Y3C}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1834-2293, AND ACTIVITY
RP REGULATION (RNA-DIRECTED RNA POLYMERASE).
RX PubMed=25799064; DOI=10.1371/journal.ppat.1004733;
RA van der Linden L., Vives-Adrian L., Selisko B., Ferrer-Orta C., Liu X.,
RA Lanke K., Ulferts R., De Palma A.M., Tanchis F., Goris N., Lefebvre D.,
RA De Clercq K., Leyssen P., Lacroix C., Purstinger G., Coutard B., Canard B.,
RA Boehr D.D., Arnold J.J., Cameron C.E., Verdaguer N., Neyts J.,
RA van Kuppeveld F.J.;
RT "The RNA template channel of the RNA-dependent RNA polymerase as a target
RT for development of antiviral therapy of multiple genera within a virus
RT family.";
RL PLoS Pathog. 11:E1004733-E1004733(2015).
CC -!- FUNCTION: [Leader protein]: Forms a complex with host RAN and probably
CC binds to exportins carrying activated MAPK in order to mediate the
CC hyperphosphorylation of host Phe/Gly containing nuclear pore proteins
CC (Nups) resulting in cessation of active nucleocytoplasmic transport (By
CC similarity). Proteins with NLS signals fail to import, cellular mRNAs
CC fail to export, and some proteins small enough for diffusion are not
CC retained anymore (efflux) (By similarity). The resulting inhibition of
CC cellular protein synthesis serves to ensure maximal viral gene
CC expression and to evade host immune response (By similarity).
CC {ECO:0000250|UniProtKB:Q66765}.
CC -!- FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3. Together they form an
CC icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3,
CC with a diameter of approximately 300 Angstroms.VP4 lies on the inner
CC surface of the protein shell formed by VP1, VP2 and VP3. All the three
CC latter proteins contain a beta-sheet structure called beta-barrel jelly
CC roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are
CC located at the quasi-sixfold axes. {ECO:0000269|PubMed:2156078,
CC ECO:0000269|PubMed:3026048}.
CC -!- FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3. Together they form an
CC icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3,
CC with a diameter of approximately 300 Angstroms.VP4 lies on the inner
CC surface of the protein shell formed by VP1, VP2 and VP3. All the three
CC latter proteins contain a beta-sheet structure called beta-barrel jelly
CC roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are
CC located at the quasi-sixfold axes. {ECO:0000269|PubMed:2156078,
CC ECO:0000269|PubMed:3026048}.
CC -!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3. Together they form an
CC icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3,
CC with a diameter of approximately 300 Angstroms.VP4 lies on the inner
CC surface of the protein shell formed by VP1, VP2 and VP3. All the three
CC latter proteins contain a beta-sheet structure called beta-barrel jelly
CC roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are
CC located at the quasi-sixfold axes. {ECO:0000269|PubMed:2156078,
CC ECO:0000269|PubMed:3026048}.
CC -!- FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid
CC shell (PubMed:3026048, PubMed:2156078). After binding to the host
CC receptor, the capsid undergoes conformational changes (By similarity).
CC Capsid protein VP4 is released, capsid protein VP1 N-terminus is
CC externalized, and together, they shape a pore in the host membrane
CC through which the viral genome is translocated into the host cell
CC cytoplasm (By similarity). After genome has been released, the channel
CC shrinks (By similarity). {ECO:0000250|UniProtKB:P03300,
CC ECO:0000269|PubMed:2156078, ECO:0000269|PubMed:3026048}.
CC -!- FUNCTION: [Capsid protein VP0]: VP0 precursor is a component of
CC immature procapsids. {ECO:0000250|UniProtKB:P08617}.
CC -!- FUNCTION: [Protein 2A]: Involved in host translation shutoff by
CC inhibiting cap-dependent mRNA translation (PubMed:12921995). Nuclear
CC localization is required for this function (By similarity). The
CC resulting inhibition of cellular protein synthesis serves to ensure
CC maximal viral gene expression and to evade host immune response (By
CC similarity). Inhibits the phosphorylation of the leader protein (By
CC similarity). Binds to the RNA stem-loop essential for the ribosomal
CC frameshift event and trans-activates the production of protein 2B*
CC (PubMed:28593994). {ECO:0000250|UniProtKB:Q66765,
CC ECO:0000269|PubMed:12921995, ECO:0000269|PubMed:28593994}.
CC -!- FUNCTION: [Protein 2B]: Affects membrane integrity and causes an
CC increase in membrane permeability. {ECO:0000250}.
CC -!- FUNCTION: [Protein 2C]: Associates with and induces structural
CC rearrangements of intracellular membranes (By similarity). It displays
CC RNA-binding, nucleotide binding and NTPase activities (By similarity).
CC Interacts with IFIH1/MDA5 to inhibit the induction of the IFN-beta
CC signal pathway (By similarity). {ECO:0000250|UniProtKB:P03304,
CC ECO:0000250|UniProtKB:P03305, ECO:0000250|UniProtKB:P08545}.
CC -!- FUNCTION: [Protein 3A]: Serves as membrane anchor via its hydrophobic
CC domain. {ECO:0000250}.
CC -!- FUNCTION: [VPg]: Forms a primer, VPg-pU, which is utilized by the
CC polymerase for the initiation of RNA chains.
CC {ECO:0000250|UniProtKB:P03304}.
CC -!- FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral
CC proteins from the precursor polyprotein (PubMed:8972564). In addition
CC to its proteolytic activity, it binds to viral RNA, and thus influences
CC viral genome replication. RNA and substrate cooperatively bind to the
CC protease. Cleaves host PABP1, this cleavage is important for viral
CC replication (By similarity). Cleaves host TANK and disrupts the TANK-
CC TBK1-IKKepsilon-IRF3 complex, thereby inhibiting the induction of the
CC IFN-beta signal pathway (By similarity). {ECO:0000250|UniProtKB:P03304,
CC ECO:0000269|PubMed:8972564}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the genomic and
CC antigenomic RNAs by recognizing replications specific signals
CC (Probable). Performs VPg uridylylation (PubMed:24600002).
CC {ECO:0000269|PubMed:24600002, ECO:0000305|PubMed:24600002}.
CC -!- CATALYTIC ACTIVITY:
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 ECO:0000269|PubMed:24600002};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
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 ECO:0000269|PubMed:8972564};
CC -!- ACTIVITY REGULATION: RNA-dependent RNA polymerase: Inhibited by GPC-
CC N114. {ECO:0000269|PubMed:25799064}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0 for protease 3C. {ECO:0000269|PubMed:8972564};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius for protease 3C.
CC {ECO:0000269|PubMed:8972564};
CC -!- SUBUNIT: [Protease 3C]: Interacts with host TRIM22; this interaction
CC leads to the ubiquitination of protease 3C and may restrict the virus
CC replication (By similarity). {ECO:0000250|UniProtKB:Q66765}.
CC -!- SUBUNIT: [Protein 2A]: Interacts with host EIF4E (By similarity).
CC Interacts with the leader protein (By similarity).
CC {ECO:0000250|UniProtKB:Q66765}.
CC -!- SUBUNIT: [Leader protein]: Interacts with host RAN; the complex L-RAN
CC recruits cellular kinases responsible for the L-induced
CC nucleocytoplasmic trafficking inhibition (PubMed:25331866). The complex
CC L-RAN can further bind to the host exportins XPO1/CRM1 and CSE1L/CAS
CC (Probable). Interacts with the protein 2A (By similarity).
CC {ECO:0000250|UniProtKB:P03304, ECO:0000250|UniProtKB:Q66765,
CC ECO:0000269|PubMed:25331866, ECO:0000305|PubMed:25331866}.
CC -!- SUBUNIT: [Protein 2C]: Interacts with host IFIH1/MDA5; this interaction
CC inhibits the induction of the IFN-beta signal pathway (By similarity).
CC {ECO:0000250|UniProtKB:Q66765}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion
CC {ECO:0000269|PubMed:2156078, ECO:0000269|PubMed:3026048}. Host
CC cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
CC {ECO:0000269|PubMed:2156078, ECO:0000269|PubMed:3026048}. Host
CC cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC {ECO:0000269|PubMed:2156078, ECO:0000269|PubMed:3026048}. Host
CC cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein 2A]: Host nucleus, host nucleolus
CC {ECO:0000269|PubMed:12921995}.
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 probably
CC autophagosome-like vesicles. {ECO:0000305}.
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 probably
CC autophagosome-like vesicles. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P03304}; 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 probably autophagosome-like vesicles.
CC {ECO:0000250|UniProtKB:P03304}.
CC -!- SUBCELLULAR LOCATION: [VPg]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000305}.
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 probably autophagosome-like vesicles. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Genome polyprotein;
CC IsoId=P12296-1; Sequence=Displayed;
CC Name=2B*;
CC IsoId=P0DJX8-1; Sequence=External;
CC -!- PTM: [Leader protein]: Phosphorylated. {ECO:0000269|PubMed:25331866}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral
CC protease in vivo yield a variety of precursors and mature proteins
CC (PubMed:8972564). The polyprotein seems to be cotranslationally cleaved
CC at the 2A/2B junction by a ribosomal skip from one codon to the next
CC without formation of a peptide bond (By similarity). This process would
CC release the P1-2A peptide from the translational complex (By
CC similarity). {ECO:0000250|UniProtKB:P03304,
CC ECO:0000269|PubMed:8972564}.
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 is followed by a conformational
CC change of the particle. {ECO:0000250|UniProtKB:P03300}.
CC -!- PTM: [VPg]: Uridylylated by the polymerase and is covalently linked to
CC the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-
CC peptide primer for the polymerase. {ECO:0000269|PubMed:24600002}.
CC -!- PTM: [Capsid protein VP4]: Myristoylation is required during RNA
CC encapsidation and formation of the mature virus particle.
CC {ECO:0000250|UniProtKB:Q66282}.
CC -!- MISCELLANEOUS: [Isoform Genome polyprotein]: Produced by conventional
CC translation. {ECO:0000269|PubMed:22025686}.
CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2mev";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1mec";
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DR EMBL; DQ294633; ABB97066.1; -; Genomic_RNA.
DR PDB; 1MEC; X-ray; 3.20 A; 1=625-898, 2=138-393, 3=394-624, 4=68-137.
DR PDB; 2M7Y; NMR; -; A=1-67.
DR PDB; 2MEV; X-ray; 3.00 A; 1=625-901, 2=138-393, 3=394-624, 4=68-137.
DR PDB; 2MMH; NMR; -; A=1-67.
DR PDB; 2MMI; NMR; -; A=1-67.
DR PDB; 2MMK; NMR; -; A=1-67.
DR PDB; 2MML; NMR; -; A=1-67.
DR PDB; 4NYZ; X-ray; 2.15 A; A=1834-2293.
DR PDB; 4NZ0; X-ray; 2.80 A; A/B/C/D/E/F=1834-2293.
DR PDB; 4Y2C; X-ray; 2.20 A; A=1834-2293.
DR PDB; 4Y3C; X-ray; 3.20 A; A/B/C/D/E/F=1834-2293.
DR PDB; 7BNY; X-ray; 2.62 A; A/B/C/D=902-1044.
DR PDB; 7NWT; EM; 2.66 A; AA/BB/CC=902-1044.
DR PDBsum; 1MEC; -.
DR PDBsum; 2M7Y; -.
DR PDBsum; 2MEV; -.
DR PDBsum; 2MMH; -.
DR PDBsum; 2MMI; -.
DR PDBsum; 2MMK; -.
DR PDBsum; 2MML; -.
DR PDBsum; 4NYZ; -.
DR PDBsum; 4NZ0; -.
DR PDBsum; 4Y2C; -.
DR PDBsum; 4Y3C; -.
DR PDBsum; 7BNY; -.
DR PDBsum; 7NWT; -.
DR BMRB; P12296; -.
DR SMR; P12296; -.
DR iPTMnet; P12296; -.
DR PRIDE; P12296; -.
DR EvolutionaryTrace; P12296; -.
DR Proteomes; UP000008663; Genome.
DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044196; C:host cell nucleolus; 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; IDA:UniProtKB.
DR GO; GO:0019028; C:viral capsid; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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: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: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:0039540; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
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; -; 1.
DR Gene3D; 2.60.120.20; -; 3.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 4.10.90.10; -; 1.
DR InterPro; IPR015031; Capsid_VP4_Picornavir.
DR InterPro; IPR037080; Capsid_VP4_sf_Picornavirus.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR021573; Leader_pept_picornaV.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
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 InterPro; IPR037243; Viral_lead_polypep_zc_finger.
DR Pfam; PF00548; Peptidase_C3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00073; Rhv; 2.
DR Pfam; PF00910; RNA_helicase; 1.
DR Pfam; PF08935; VP4_2; 1.
DR Pfam; PF11475; VP_N-CPKC; 1.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF144251; SSF144251; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56672; SSF56672; 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; ATP-binding; Capsid protein; Covalent protein-RNA linkage;
KW Disulfide bond; 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 nucleus; Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host RIG-I by virus; Inhibition of host RLR pathway by virus;
KW Ion channel; Ion transport; Lipoprotein; Membrane; Metal-binding;
KW Myristate; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW Protease; Ribosomal frameshifting; RNA-binding;
KW RNA-directed RNA polymerase; T=pseudo3 icosahedral capsid protein;
KW Thiol protease; Transferase; Transport; Viral attachment to host cell;
KW Viral immunoevasion; Viral ion channel; Viral RNA replication; Virion;
KW Virus entry into host cell; Zinc; Zinc-finger.
FT CHAIN 1..2293
FT /note="Genome polyprotein"
FT /id="PRO_0000446090"
FT CHAIN 1..67
FT /note="Leader protein"
FT /id="PRO_5000141082"
FT CHAIN 68..393
FT /note="Capsid protein VP0"
FT /id="PRO_0000310965"
FT CHAIN 68..137
FT /note="Capsid protein VP4"
FT /id="PRO_5000141083"
FT CHAIN 138..393
FT /note="Capsid protein VP2"
FT /id="PRO_5000141084"
FT CHAIN 394..624
FT /note="Capsid protein VP3"
FT /id="PRO_5000141085"
FT CHAIN 625..901
FT /note="Capsid protein VP1"
FT /id="PRO_5000141086"
FT CHAIN 902..1044
FT /note="Protein 2A"
FT /id="PRO_5000141087"
FT CHAIN 1045..1195
FT /note="Protein 2B"
FT /id="PRO_5000141088"
FT CHAIN 1196..1520
FT /note="Protein 2C"
FT /id="PRO_5000141089"
FT CHAIN 1521..1608
FT /note="Protein 3A"
FT /id="PRO_5000141090"
FT CHAIN 1609..1628
FT /note="VPg"
FT /id="PRO_5000141091"
FT CHAIN 1629..1833
FT /note="Protease 3C"
FT /id="PRO_5000141092"
FT CHAIN 1834..2293
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_5000141093"
FT DOMAIN 1282..1448
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1631..1823
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 2062..2180
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ZN_FING 10..22
FT /evidence="ECO:0000269|PubMed:25331866"
FT REGION 37..61
FT /note="Acidic"
FT /evidence="ECO:0000305"
FT REGION 1030..1036
FT /note="Host EIF4E binding"
FT /evidence="ECO:0000250|UniProtKB:Q66765"
FT MOTIF 995..1003
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q66765"
FT ACT_SITE 1674
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1708
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1787
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 2068
FT /note="For RdRp activity"
FT /evidence="ECO:0000269|PubMed:24600002"
FT ACT_SITE 2166
FT /note="For RdRp activity"
FT /evidence="ECO:0000269|PubMed:24600002"
FT BINDING 1314..1321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 137..138
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 393..394
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 624..625
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 901..902
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1044..1045
FT /note="Cleavage; by ribosomal skip"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1195..1196
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1520..1521
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1608..1609
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1628..1629
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1833..1834
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT MOD_RES 41
FT /note="Phosphotyrosine; by host SYK"
FT /evidence="ECO:0000269|PubMed:25331866"
FT MOD_RES 47
FT /note="Phosphothreonine; by host CK2"
FT /evidence="ECO:0000269|PubMed:25331866"
FT MOD_RES 1611
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT LIPID 68
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q66282"
FT DISULFID 479..481
FT /evidence="ECO:0000269|PubMed:2156078"
FT HELIX 1..3
FT /evidence="ECO:0007829|PDB:2MMH"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:2M7Y"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:2M7Y"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:2M7Y"
FT HELIX 20..24
FT /evidence="ECO:0007829|PDB:2M7Y"
FT TURN 26..30
FT /evidence="ECO:0007829|PDB:2MMI"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:2M7Y"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:2MMH"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:2MMH"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:2M7Y"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:2MMI"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2M7Y"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2M7Y"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1MEC"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1MEC"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:2MEV"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1MEC"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:2MEV"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:2MEV"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:2MEV"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:2MEV"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:2MEV"
FT HELIX 231..237
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 240..252
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 260..269
FT /evidence="ECO:0007829|PDB:2MEV"
FT TURN 286..290
FT /evidence="ECO:0007829|PDB:2MEV"
FT HELIX 309..314
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:2MEV"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:2MEV"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 349..360
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 368..385
FT /evidence="ECO:0007829|PDB:2MEV"
FT TURN 402..405
FT /evidence="ECO:0007829|PDB:2MEV"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:2MEV"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 455..460
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:1MEC"
FT STRAND 470..476
FT /evidence="ECO:0007829|PDB:2MEV"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:2MEV"
FT HELIX 486..491
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 494..499
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 501..507
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 514..522
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:2MEV"
FT HELIX 532..535
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 538..544
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 550..555
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 560..567
FT /evidence="ECO:0007829|PDB:2MEV"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:1MEC"
FT STRAND 579..589
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 598..606
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 611..615
FT /evidence="ECO:0007829|PDB:2MEV"
FT HELIX 629..631
FT /evidence="ECO:0007829|PDB:2MEV"
FT TURN 639..642
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 654..656
FT /evidence="ECO:0007829|PDB:1MEC"
FT HELIX 657..661
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 665..670
FT /evidence="ECO:0007829|PDB:2MEV"
FT HELIX 676..678
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 685..688
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 690..694
FT /evidence="ECO:0007829|PDB:2MEV"
FT HELIX 703..705
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 727..729
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 731..733
FT /evidence="ECO:0007829|PDB:2MEV"
FT HELIX 736..740
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 745..758
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 765..770
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 788..790
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 792..794
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 796..799
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 808..812
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 817..824
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 848..854
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 860..873
FT /evidence="ECO:0007829|PDB:2MEV"
FT STRAND 894..896
FT /evidence="ECO:0007829|PDB:1MEC"
FT STRAND 914..922
FT /evidence="ECO:0007829|PDB:7BNY"
FT STRAND 925..932
FT /evidence="ECO:0007829|PDB:7BNY"
FT STRAND 935..942
FT /evidence="ECO:0007829|PDB:7BNY"
FT HELIX 949..958
FT /evidence="ECO:0007829|PDB:7BNY"
FT STRAND 974..983
FT /evidence="ECO:0007829|PDB:7BNY"
FT STRAND 988..996
FT /evidence="ECO:0007829|PDB:7BNY"
FT STRAND 1004..1010
FT /evidence="ECO:0007829|PDB:7BNY"
FT HELIX 1016..1026
FT /evidence="ECO:0007829|PDB:7BNY"
FT TURN 1027..1030
FT /evidence="ECO:0007829|PDB:7BNY"
FT STRAND 1836..1838
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 1859..1862
FT /evidence="ECO:0007829|PDB:4NYZ"
FT STRAND 1865..1868
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 1882..1885
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 1886..1890
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 1899..1916
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 1925..1930
FT /evidence="ECO:0007829|PDB:4NYZ"
FT STRAND 1933..1935
FT /evidence="ECO:0007829|PDB:4NYZ"
FT STRAND 1940..1942
FT /evidence="ECO:0007829|PDB:4NYZ"
FT TURN 1946..1952
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 1955..1958
FT /evidence="ECO:0007829|PDB:4NYZ"
FT TURN 1961..1964
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 1968..1978
FT /evidence="ECO:0007829|PDB:4NYZ"
FT STRAND 1987..1991
FT /evidence="ECO:0007829|PDB:4NYZ"
FT STRAND 1994..1997
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 1998..2002
FT /evidence="ECO:0007829|PDB:4NYZ"
FT STRAND 2008..2011
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 2014..2031
FT /evidence="ECO:0007829|PDB:4NYZ"
FT TURN 2037..2040
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 2047..2058
FT /evidence="ECO:0007829|PDB:4NYZ"
FT STRAND 2061..2068
FT /evidence="ECO:0007829|PDB:4NYZ"
FT TURN 2072..2075
FT /evidence="ECO:0007829|PDB:4NZ0"
FT HELIX 2078..2087
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 2091..2093
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 2099..2107
FT /evidence="ECO:0007829|PDB:4NYZ"
FT STRAND 2108..2113
FT /evidence="ECO:0007829|PDB:4NYZ"
FT STRAND 2116..2122
FT /evidence="ECO:0007829|PDB:4NYZ"
FT STRAND 2126..2128
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 2131..2150
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 2156..2158
FT /evidence="ECO:0007829|PDB:4NYZ"
FT STRAND 2160..2164
FT /evidence="ECO:0007829|PDB:4NYZ"
FT STRAND 2167..2174
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 2178..2186
FT /evidence="ECO:0007829|PDB:4NYZ"
FT TURN 2187..2189
FT /evidence="ECO:0007829|PDB:4NYZ"
FT STRAND 2195..2197
FT /evidence="ECO:0007829|PDB:4NYZ"
FT TURN 2207..2209
FT /evidence="ECO:0007829|PDB:4NYZ"
FT STRAND 2215..2220
FT /evidence="ECO:0007829|PDB:4NYZ"
FT STRAND 2223..2228
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 2230..2238
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 2245..2256
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 2257..2259
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 2261..2273
FT /evidence="ECO:0007829|PDB:4NYZ"
FT HELIX 2281..2290
FT /evidence="ECO:0007829|PDB:4NYZ"
SQ SEQUENCE 2293 AA; 255528 MW; 0394484E477B94E7 CRC64;
MATTMEQEIC AHSMTFEECP KCSALQYRNG FYLLKYDEEW YPEELLTDGE DDVFDPDLDM
EVVFETQGNS TSSDKNNSSS EGNEGVIINN FYSNQYQNSI DLSANATGSD PPKTYGQFSN
LLSGAVNAFS NMLPLLADQN TEEMENLSDR VSQDTAGNTV TNTQSTVGRL VGYGTVHDGE
HPASCADTAS EKILAVERYY TFKVNDWTST QKPFEYIRIP LPHVLSGEDG GVFGATLRRH
YLVKTGWRVQ VQCNASQFHA GSLLVFMAPE YPTLDVFAMD NRWSKDNLPN GTRTQTNRKG
PFAMDHQNFW QWTLYPHQFL NLRTNTTVDL EVPYVNIAPT SSWTQHASWT LVIAVVAPLT
YSTGASTSLD ITASIQPVRP VFNGLRHEVL SRQSPIPVTI REHAGTWYST LPDSTVPIYG
KTPVAPANYM VGEYKDFLEI AQIPTFIGNK VPNAVPYIEA SNTAVKTQPL AVYQVTLSCS
CLANTFLAAL SRNFAQYRGS LVYTFVFTGT AMMKGKFLIA YTPPGAGKPT SRDQAMQATY
AIWDLGLNSS YSFTVPFISP THFRMVGTDQ ANITNVDGWV TVWQLTPLTY PPGCPTSAKI
LTMVSAGKDF SLKMPISPAP WSPQGVENAE KGVTENTDAT ADFVAQPVYL PENQTKVAFF
YDRSSPIGAF AVKSGSLESG FAPFSNKACP NSVILTPGPQ FDPAYDQLRP QRLTEIWGNG
NEETSEVFPL KTKQDYSFCL FSPFVYYKCD LEVTLSPHTS GAHGLLVRWC PTGTPTKPTT
QVLHEVSSLS EGRTPQVYSA GPGTSNQISF VVPYNSPLSV LPAVWYNGHK RFDNTGDLGI
APNSDFGTLF FAGTKPDIKF TVYLRYKNMR VFCPRPTVFF PWPTSGDKID MTPRAGVLML
ESPNPLDVSK TYPTLHILLQ FNHRGLEARI FRHGQLWAET HAEVVLRSKT KQISFLSNGS
YPSMDATTPL NPWKSTYQAV LRAEPHRVTM DVYHKRIRPF RLPLVQKEWR TCEENVFGLY
HVFETHYAGY FSDLLIHDVE TNPGPFTFKP RQRPVFQTQG AAVSSMAQTL LPNDLASKAM
GSAFTALLDA NEDAQKAMKI IKTLSSLSDA WENVKGTLNN PEFWKQLLSR CVQLIAGMTI
AVMHPDPLTL LCLGVLTAAE ITSQTSLCEE IAAKFKTIFT TPPPRFPVIS LFQQQSPLKQ
VNDVFSLAKN LDWAVKTVEK VVDWFGTWVA QEEREQTLDQ LLQRFPEHAK RISDLRNGMA
AYVECKESFD FFEKLYNQAV KEKRTGIAAV CEKFRQKHDH ATARCEPVVI VLRGDAGQGK
SLSSQIIAQA VSKTIFGRQS VYSLPPDSDF FDGYENQFAA IMDDLGQNPD GSDFTTFCQM
VSTTNLLPNM ASLERKGTPF TSQLVVATTN LPEFRPVTIA HYPAVERRIT FDYSVSAGPV
CSKTEAGCKV LDVERAFRPT GDAPLPCFQN NCLFLEKAGL QFRDNRSKEI LSLVDVIERA
VTRIERKKKV LTAVQTLVAQ GPVDEVSFYS VVQQLKARQE ATDEQLEELQ EAFARVQERS
SVFSDWMKIS AMLCAATLAL TQVVKMAKAV KQMVRPDLVR VQLDEQEQGP YNETTRIKPK
TLQLLDVQGP NPTMDFEKFV AKFVTAPIGF VYPTGVSTQT CLLVKGRTLA VNRHMAESDW
TSIVVRGVSH TRSSVKIIAI AKAGKETDVS FIRLSSGPLF RDNTSKFVKA SDVLPHSSSP
LIGIMNVDIP MMYTGTFLKA GVSVPVETGQ TFNHCIHYKA NTRKGWCGSA ILADLGGSKK
ILGFHSAGSM GVAAASIISQ EMIDAVVQAF EPQGALERLP DGPRIHVPRK TALRPTVARQ
VFQPAFAPAV LSKFDPRTDA DVDEVAFSKH TSNQETLPPV FRMVAREYAN RVFALLGRDN
GRLSVKQALD GLEGMDPMDK NTSPGLPYTT LGMRRTDVVD WETATLIPFA AERLEKMNNK
DFSDIVYQTF LKDELRPIEK VQAAKTRIVD VPPFEHCILG RQLLGKFASK FQTQPGLELG
SAIGCDPDVH WTAFGVAMQG FERVYDVDYS NFDSTHSVAV FRLLAEEFFS EENGFDPLVK
DYLESLAISK HAYEEKRYLI TGGLPSGCAA TSMLNTIMNN IIIRAGLYLT YKNFEFDDVK
VLSYGDDLLV ATNYQLNFDR VRTSLAKTGY KITPANKTST FPLESTLEDV VFLKRKFKKE
GPLYRPVMNR EALEAMLSYY RPGTLSEKLT SITMLAVHSG KQEYDRLFAP FREVGVIVPT
FESVEYRWRS LFW
