POLG_TMEVB
ID POLG_TMEVB Reviewed; 2303 AA.
AC P08544; Q88583; Q88584; Q88585; Q88586; Q88587; Q88588; Q88589; Q88590;
AC Q88591; Q88592;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 179.
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=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=Protein 2A;
DE Short=P2A;
DE Contains:
DE RecName: Full=Protein 2B;
DE Short=P2B;
DE Contains:
DE RecName: Full=Protein 2C;
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=Protein 3B;
DE Contains:
DE RecName: Full=Protease 3C;
DE Short=P3C;
DE EC=3.4.22.28 {ECO:0000250|UniProtKB:P12296};
DE AltName: Full=Picornain 3C;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
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;
DE Flags: Precursor;
OS Theiler's murine encephalomyelitis virus (strain BeAn 8386) (TMEV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Cardiovirus.
OX NCBI_TaxID=12125;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3033278; DOI=10.1128/jvi.61.5.1507-1516.1987;
RA Pevear D.C., Calenoff M., Rozhon E., Lipton H.L.;
RT "Analysis of the complete nucleotide sequence of the picornavirus Theiler's
RT murine encephalomyelitis virus indicates that it is closely related to
RT cardioviruses.";
RL J. Virol. 61:1507-1516(1987).
RN [2]
RP INTERACTION WITH THE LEADER PROTEIN (PROTEIN 2A), INTERACTION WITH PROTEIN
RP 2A (LEADER PROTEIN), AND FUNCTION (PROTEIN 2A).
RX PubMed=25210192; DOI=10.1128/jvi.02148-14;
RA Petty R.V., Basta H.A., Bacot-Davis V.R., Brown B.A., Palmenberg A.C.;
RT "Binding interactions between the encephalomyocarditis virus leader and
RT protein 2A.";
RL J. Virol. 88:13503-13509(2014).
RN [3]
RP FUNCTION (LEADER PROTEIN).
RX PubMed=26115166; DOI=10.1016/j.virol.2015.06.004;
RA Ciomperlik J.J., Basta H.A., Palmenberg A.C.;
RT "Three cardiovirus leader proteins equivalently inhibit four different
RT nucleocytoplasmic trafficking pathways.";
RL Virology 484:194-202(2015).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 148-922.
RX PubMed=1312722; DOI=10.1073/pnas.89.6.2409;
RA Luo M., He C., Toth K.S., Zhang C.X., Lipton H.L.;
RT "Three-dimensional structure of Theiler murine encephalomyelitis virus
RT (BeAn strain).";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2409-2413(1992).
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
CC (Probable). 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). The
CC leader protein also inhibits host interferon regulatory factor 3 (IRF3)
CC dimerization, thereby blocking the transcriptional activation of IFN
CC genes (By similarity). Binds to host RNase L thereby preventing its
CC activation by 2'-5' oligoadenylates in order to counteract the
CC antiviral interferon-inducible OAS/RNase L pathway (By similarity).
CC {ECO:0000250|UniProtKB:P13899, ECO:0000250|UniProtKB:Q66765,
CC ECO:0000305|PubMed:26115166}.
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:0000250|UniProtKB:C0MHL9}.
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:0000250|UniProtKB:C0MHL9}.
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:0000250|UniProtKB:C0MHL9}.
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). After
CC genome has been released, the channel shrinks (By similarity).
CC {ECO:0000250|UniProtKB:C0MHL9, ECO:0000250|UniProtKB:P03300}.
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 (By similarity). 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
CC (PubMed:25210192). {ECO:0000250|UniProtKB:Q66765,
CC ECO:0000269|PubMed:25210192}.
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 {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 (By similarity). In addition to
CC 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). {ECO:0000250|UniProtKB:P03304,
CC ECO:0000250|UniProtKB:P12296}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the genomic and
CC antigenomic RNAs by recognizing replications specific signals (By
CC similarity). Performs VPg uridylylation (By similarity).
CC {ECO:0000250|UniProtKB:P12296}.
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 -!- 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 -!- SUBUNIT: [Protein 2A]: Interacts with host EIF4E (By similarity).
CC Interacts with the leader protein (PubMed:25210192).
CC {ECO:0000250|UniProtKB:P13899, ECO:0000250|UniProtKB:Q66765,
CC ECO:0000269|PubMed:25210192}.
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 (By similarity). The complex
CC L-RAN can further bind to the host exportins XPO1/CRM1 and CSE1L/CAS
CC (By similarity). Interacts with the protein 2A (PubMed:25210192).
CC Interacts with host RNASEL; this interaction prevents RNASEL activation
CC by its substrate 2'-5' oligoadenylates (By similarity).
CC {ECO:0000250|UniProtKB:P13899, ECO:0000250|UniProtKB:Q66765,
CC ECO:0000269|PubMed:25210192}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion
CC {ECO:0000250|UniProtKB:C0MHL9}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
CC {ECO:0000250|UniProtKB:C0MHL9}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC {ECO:0000250|UniProtKB:C0MHL9}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein 2A]: Host nucleus, host nucleolus
CC {ECO:0000250|UniProtKB:Q66765}.
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 -!- DOMAIN: [Leader protein]: The Theilo and zinc-finger regions may both
CC play a role in the inhibition of host nucleocytoplasmic trafficking and
CC IRF-3 dimerization antagonism by the L protein.
CC {ECO:0000250|UniProtKB:P13899}.
CC -!- PTM: [Leader protein]: Phosphorylated. {ECO:0000250|UniProtKB:Q66765}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral
CC protease in vivo yield a variety of precursors and mature proteins (By
CC similarity). The polyprotein seems to be cotranslationally cleaved at
CC 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 -!- 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:0000250|UniProtKB:P12296}.
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: Persistent strains of Theiler's virus (e.g. DA, TO,
CC BeAn) cause persistent demyelinating disease whereas neurovirulent
CC strains (such as GDVII) cause acute encephalitis.
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=1tmf";
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DR EMBL; M16020; AAA47930.1; -; Genomic_RNA.
DR PIR; A29535; GNNYTM.
DR PDB; 1TMF; X-ray; 3.50 A; 1=647-922, 2=148-414, 3=415-646.
DR PDBsum; 1TMF; -.
DR SMR; P08544; -.
DR MEROPS; C03.010; -.
DR EvolutionaryTrace; P08544; -.
DR Proteomes; UP000007538; 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; IEA:UniProtKB-KW.
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; 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: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: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; IDA:UniProtKB.
DR GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 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: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; -; 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; 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 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 PRINTS; PR00918; CALICVIRUSNS.
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 IRF3 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; 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 RNA replication; Virion;
KW Virus entry into host cell; Zinc; Zinc-finger.
FT CHAIN 1..2303
FT /note="Genome polyprotein"
FT /id="PRO_0000446097"
FT CHAIN 1..76
FT /note="Leader protein"
FT /id="PRO_0000040168"
FT CHAIN 77..414
FT /note="Capsid protein VP0"
FT /id="PRO_0000310970"
FT CHAIN 77..147
FT /note="Capsid protein VP4"
FT /id="PRO_0000040169"
FT CHAIN 148..414
FT /note="Capsid protein VP2"
FT /id="PRO_0000040170"
FT CHAIN 415..646
FT /note="Capsid protein VP3"
FT /id="PRO_0000040171"
FT CHAIN 647..922
FT /note="Capsid protein VP1"
FT /id="PRO_0000040172"
FT CHAIN 923..1055
FT /note="Protein 2A"
FT /id="PRO_0000040173"
FT CHAIN 1056..1191
FT /note="Protein 2B"
FT /id="PRO_0000040174"
FT CHAIN 1192..1517
FT /note="Protein 2C"
FT /id="PRO_0000040175"
FT CHAIN 1518..1605
FT /note="Protein 3A"
FT /id="PRO_0000040176"
FT CHAIN 1606..1625
FT /note="VPg"
FT /id="PRO_0000040177"
FT CHAIN 1626..1842
FT /note="Protease 3C"
FT /id="PRO_0000040178"
FT CHAIN 1843..2303
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000040179"
FT DOMAIN 1283..1448
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1636..1829
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 2071..2189
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ZN_FING 3..14
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT REGION 30..46
FT /note="Acidic"
FT /evidence="ECO:0000305"
FT REGION 60..73
FT /note="Theilo"
FT /evidence="ECO:0000250|UniProtKB:P13899"
FT REGION 74..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1047
FT /note="Host EIF4E binding"
FT /evidence="ECO:0000250|UniProtKB:Q66765"
FT ACT_SITE 1680
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1714
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1793
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 2077
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT ACT_SITE 2175
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT BINDING 1312..1319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 147..148
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 414..415
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 646..647
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 922..923
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1055..1056
FT /note="Cleavage; by ribosomal skip"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1191..1192
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1517..1518
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1605..1606
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1625..1626
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1842..1843
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT MOD_RES 1608
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT LIPID 77
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q66282"
FT DISULFID 501..503
FT /evidence="ECO:0000250|UniProtKB:C0MHL9"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:1TMF"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:1TMF"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 272..280
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:1TMF"
FT TURN 330..334
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:1TMF"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:1TMF"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 369..378
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 390..400
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 403..406
FT /evidence="ECO:0007829|PDB:1TMF"
FT TURN 459..463
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 492..495
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 501..504
FT /evidence="ECO:0007829|PDB:1TMF"
FT HELIX 508..511
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 515..521
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 524..529
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 536..543
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:1TMF"
FT HELIX 554..557
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 572..575
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 582..587
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 602..611
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 622..627
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 633..636
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 661..666
FT /evidence="ECO:0007829|PDB:1TMF"
FT TURN 680..684
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 698..700
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 712..714
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 717..719
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 727..729
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 732..734
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 747..749
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:1TMF"
FT TURN 760..764
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 769..780
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 791..794
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 807..809
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 820..822
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 831..835
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 842..847
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 853..856
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 861..863
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 871..874
FT /evidence="ECO:0007829|PDB:1TMF"
FT STRAND 880..893
FT /evidence="ECO:0007829|PDB:1TMF"
SQ SEQUENCE 2303 AA; 256282 MW; E2C7737DFDBEB786 CRC64;
MACKHGYPDV CPICTAVDAT PGFEYLLMAD GEWYPTDLLC VDLDDDVFWP SDTSNQSQTM
DWTDVPLIRD IVMEPQGNSS SSDKSNSQSS GNEGVIINNF YSNQYQNSID LSASGGNAGD
APQTNGQLSN ILGGAANAFA TMAPLLLDQN TEEMENLSDR VASDKAGNSA TNTQSTVGRL
CGYGKSHHGE HPASCADTAT DKVLAAERYY TIDLASWTTS QEAFSHIRIP LPHVLAGEDG
GVFGATLRRH YLCKTGWRVQ VQCNASQFHA GSLLVFMAPE FYTGKGTKTG TMEPSDPFTM
DTEWRSPQGA PTGYRYDSRT GFFATNHQNQ WQWTVYPHQI LNLRTNTTVD LEVPYVNVAP
SSSWTQHANW TLVVAVLSPL QYATGSSPDV QITASLQPVN PVFNGLRHET VIAQSPIPVT
VREHKGCFYS TNPDTTVPIY GKTISTPSDY MCGEFSDLLE LCKLPTFLGN PNTNNKRYPY
FSATNSVPAT SMVDYQVALS CSCMANSMLA AVARNFNQYR GSLNFLFVFT GAAMVKGKFL
IAYTPPGAGK PTTRDQAMQS TYAIWDLGLN SSFNFTAPFI SPTHYRQTSY TSPTITSVDG
WVTVWKLTPL TYPSGTPTNS DILTLVSAGD DFTLRMPISP TKWVPQGVDN AEKGKVSNDD
ASVDFVAEPV KLPENQTRVA FFYDRAVPIG MLRPGQNMET TFNYQENDYR LNCLLLTPLP
SFCPDSSSGP QKTKAPVQWR WVRSGGVNGA NFPLMTKQDY AFLCFSPFTF YKCDLEVTVS
ALGMTRVASV LRWAPTGAPA DVTDQLIGYT PSLGETRNPH MWLVGAGNSQ VSFVVPYNSP
LSVLPAAWFN GWSDFGNTKD FGVAPNADFG RLWIQGNTSA SVRIRYKKMK VFCPRPTLFF
PWPTPTTTKI NADNPVPILE LENPAALYRI DLFITFTDEF ITFDYKVHGR PVLTFRIPGF
GLTPAGRMLV CMGEQPAHGP FTSSRSLYHV IFTATCSSFS FSIYKGRYRS WKKPIHDELV
DRGYTTFGEF FKAVRGYHAD YYRQRLIHDV ETNPGPVQSV FQPQGAVLTK SLAPQAGIQN
LLLRLLGIDG DCSEVSKAIT VVTDLVAAWE KAKTTLVSPE FWSKLILKTT KFIAASVLYL
HNPDFTTTVC LSLMTGVDLL TNDSVFDWLK QKLSSFFRTP PPACPNVMQP QGPLREANEG
FTFAKNIEWA MKTIQSVVNW LTSWFKQEED HPQSKLDKLL MEFPDHCRNI MDMRNGRKAY
CECTASFKYF DELYNLAVTC KRIPLASLCE KFKNRHDHSV TRPEPVVVVL RGAAGQGKSV
TSQIIAQSVS KMAFGRQSVY SMPPDSEYFD GYENQFSVIM DDLGQNPDGE DFTVFCQMVS
STNFLPNMAH LERKGTPFTS SFIVATTNLP KFRPVTVAHY PAVDRRITFD FTVTAGPHCK
TPAGMLDVEK AFDEIPGSKP QLACFSADCP LLHKRGVMFT CNRTQTVYNL QQVVKMVNDT
ITRKTENVKK MNSLVAQSPP DWEHFENILT CLRQNNAALQ DQLDELQEAF AQARERSDFL
SDWLKVSAII FAGIASLSAV IKLASKFKES IWPTPVRVEL SEGEQAAYAG RARAQKQALQ
VLDIQGGGKV LAQAGNPVMD FELFCAKNIV APITFYYPDK AEVTQSCLLL RAHLFVVNRH
VAETDWTAFK LKDVRHERHT VALRSVNRSG AKTDLTFIKV TKGPLFKDNV NKFCSNKDDF
PARNDTVTGI MNTGLAFVYS GNFLIGNQPV NTTTGACFNH CLHYRAQTRR GWCGSAIICN
VNGKKAVYGM HSAGGGGLAA ATIITKELIE AAEKSMLALE PQGAIVDIAT GSVVHVPRKT
KLRRTVAHDV FQPKFEPAVL SRYDPRTDKD VDVVAFSKHT TNMESLPPIF DVVCGEYANR
VFTILGKENG LLTVEQAVLG LPGMDPMEKD TSPGLPYTQQ GLRRTDLLNF ITAKMTPQLD
YAHSKLVIGV YDDVVYQSFL KDEIRPIEKI HEAKTRIVDV PPFAHCIWGR QLLGRFASKF
QTKPGLELGS AIGTDPDVDW TRYAVELSGF NYVYDVDYSN FDASHSTAMF ECLINNFFTE
QNGFDRRIAE YLRSLAVSRH AYEDRRVLIR GGLPSGCAAT SMLNTIMNNV IIRAALYLTY
SNFDFDDIKV LSYGDDLLIG TNYQIDFNLV KERLAPFGYK ITPANKTTTF PLTSHLQDVT
FLKRRFVRFN SYLFRPQMDA VNLKAMVSYC KPGTLKEKLM SIALLAVHSG PDIYDEIFLP
FRNVGIVVPT YSSMLYRWLS LFR
