POLG_TMEVD
ID POLG_TMEVD Reviewed; 2301 AA.
AC P13899; Q88564; Q88565; Q88566; Q88567; Q88568; Q88569; Q88570; Q88571;
AC Q88572; Q88573; Q88574; Q89580; S4UVR9;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 183.
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 DA) (TMEV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Cardiovirus.
OX NCBI_TaxID=12126;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2834872; DOI=10.1016/0042-6822(88)90642-3;
RA Ohara Y., Stein S., Fu J., Stillman L., Klaman L., Roos R.P.;
RT "Molecular cloning and sequence determination of DA strain of Theiler's
RT murine encephalomyelitis viruses.";
RL Virology 164:245-255(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], FUNCTION (LEADER PROTEIN), AND
RP INTERACTION WITH MOUSE RNASEL (LEADER PROTEIN).
RX PubMed=23825954; DOI=10.1371/journal.ppat.1003474;
RA Sorgeloos F., Jha B.K., Silverman R.H., Michiels T.;
RT "Evasion of Antiviral Innate Immunity by Theiler's Virus L* Protein through
RT Direct Inhibition of RNase L.";
RL PLoS Pathog. 9:E1003474-E1003474(2013).
RN [3]
RP ALTERNATIVE INITIATION.
RX PubMed=2033677; DOI=10.1128/jvi.65.6.3395-3399.1991;
RA Kong W.P., Roos R.P.;
RT "Alternative translation initiation site in the DA strain of Theiler's
RT murine encephalomyelitis virus.";
RL J. Virol. 65:3395-3399(1991).
RN [4]
RP FUNCTION (LEADER PROTEIN).
RX PubMed=15047849; DOI=10.1128/jvi.78.8.4357-4362.2004;
RA Delhaye S., van Pesch V., Michiels T.;
RT "The leader protein of Theiler's virus interferes with nucleocytoplasmic
RT trafficking of cellular proteins.";
RL J. Virol. 78:4357-4362(2004).
RN [5]
RP FUNCTION (LEADER PROTEIN).
RX PubMed=19088287; DOI=10.1099/vir.0.005678-0;
RA Ricour C., Delhaye S., Hato S.V., Olenyik T.D., Michel B.,
RA van Kuppeveld F.J., Gustin K.E., Michiels T.;
RT "Inhibition of mRNA export and dimerization of interferon regulatory factor
RT 3 by Theiler's virus leader protein.";
RL J. Gen. Virol. 90:177-186(2009).
RN [6]
RP FUNCTION (LEADER PROTEIN), AND DOMAIN (LEADER PROTEIN).
RX PubMed=19710133; DOI=10.1128/jvi.00829-09;
RA Ricour C., Borghese F., Sorgeloos F., Hato S.V., van Kuppeveld F.J.,
RA Michiels T.;
RT "Random mutagenesis defines a domain of Theiler's virus leader protein that
RT is essential for antagonism of nucleocytoplasmic trafficking and cytokine
RT gene expression.";
RL J. Virol. 83:11223-11232(2009).
RN [7]
RP FUNCTION (LEADER PROTEIN), AND INTERACTION WITH MOUSE RNASEL (LEADER
RP PROTEIN).
RX PubMed=29652922; DOI=10.1371/journal.ppat.1006989;
RA Drappier M., Jha B.K., Stone S., Elliott R., Zhang R., Vertommen D.,
RA Weiss S.R., Silverman R.H., Michiels T.;
RT "A novel mechanism of RNase L inhibition: Theiler's virus L* protein
RT prevents 2-5A from binding to RNase L.";
RL PLoS Pathog. 14:E1006989-E1006989(2018).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=1549565; DOI=10.1073/pnas.89.6.2061;
RA Grant R.A., Filman D.J., Fujinami R.S., Icenogle J.P., Hogle J.M.;
RT "Three-dimensional structure of Theiler virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2061-2065(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 (PubMed:19088287). 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 (PubMed:23825954,
CC PubMed:29652922). {ECO:0000250|UniProtKB:Q66765,
CC ECO:0000269|PubMed:19088287, ECO:0000269|PubMed:23825954,
CC ECO:0000269|PubMed:29652922, ECO:0000305|PubMed:15047849,
CC ECO:0000305|PubMed:19710133}.
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 (By
CC similarity). {ECO:0000250|UniProtKB:Q66765}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P08544, 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 (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 (By similarity).
CC Interacts with host RNASEL; this interaction prevents RNASEL activation
CC by its substrate 2'-5' oligoadenylates (PubMed:29652922,
CC PubMed:23825954). {ECO:0000250|UniProtKB:P08544,
CC ECO:0000250|UniProtKB:Q66765, ECO:0000269|PubMed:29652922}.
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:0000269|PubMed:19710133}.
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=1tme";
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DR EMBL; M20301; AAA47928.1; -; Genomic_RNA.
DR EMBL; JX443418; AGM61326.1; -; Genomic_RNA.
DR PIR; A31228; GNNYTN.
DR PDB; 1TME; X-ray; 2.80 A; 1=647-920, 2=148-414, 3=415-650, 4=77-147.
DR PDB; 1TMF; X-ray; 3.50 A; 4=90-130.
DR PDBsum; 1TME; -.
DR PDBsum; 1TMF; -.
DR SMR; P13899; -.
DR MEROPS; C03.010; -.
DR PRIDE; P13899; -.
DR EvolutionaryTrace; P13899; -.
DR Proteomes; UP000000283; Genome.
DR Proteomes; UP000098676; 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..2301
FT /note="Genome polyprotein"
FT /id="PRO_0000446098"
FT CHAIN 1..76
FT /note="Leader protein"
FT /id="PRO_0000040180"
FT CHAIN 77..414
FT /note="Capsid protein VP0"
FT /id="PRO_0000310971"
FT CHAIN 77..147
FT /note="Capsid protein VP4"
FT /id="PRO_0000040181"
FT CHAIN 148..414
FT /note="Capsid protein VP2"
FT /id="PRO_0000040182"
FT CHAIN 415..646
FT /note="Capsid protein VP3"
FT /id="PRO_0000040183"
FT CHAIN 647..920
FT /note="Capsid protein VP1"
FT /id="PRO_0000040184"
FT CHAIN 921..1053
FT /note="Protein 2A"
FT /id="PRO_0000040185"
FT CHAIN 1054..1189
FT /note="Protein 2B"
FT /id="PRO_0000040186"
FT CHAIN 1190..1515
FT /note="Protein 2C"
FT /id="PRO_0000040187"
FT CHAIN 1516..1603
FT /note="Protein 3A"
FT /id="PRO_0000040188"
FT CHAIN 1604..1623
FT /note="VPg"
FT /id="PRO_0000040189"
FT CHAIN 1624..1840
FT /note="Protease 3C"
FT /id="PRO_0000040190"
FT CHAIN 1841..2301
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000040191"
FT DOMAIN 1281..1446
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1634..1827
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 2069..2187
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:0000269|PubMed:19710133"
FT REGION 1039..1045
FT /note="Host EIF4E binding"
FT /evidence="ECO:0000250|UniProtKB:Q66765"
FT ACT_SITE 1678
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1712
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1791
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 2075
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT ACT_SITE 2173
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT BINDING 1310..1317
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 920..921
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1053..1054
FT /note="Cleavage; by ribosomal skip"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1189..1190
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1515..1516
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1603..1604
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1623..1624
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1840..1841
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT MOD_RES 1606
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 CONFLICT 288
FT /note="K -> N (in Ref. 2; AGM61326)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="F -> L (in Ref. 2; AGM61326)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="T -> P (in Ref. 2; AGM61326)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="C -> R (in Ref. 2; AGM61326)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="A -> T (in Ref. 2; AGM61326)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="A -> V (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="S -> T (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1104
FT /note="F -> V (in Ref. 2; AGM61326)"
FT /evidence="ECO:0000305"
FT CONFLICT 1458
FT /note="P -> S (in Ref. 2; AGM61326)"
FT /evidence="ECO:0000305"
FT CONFLICT 1967
FT /note="N -> D (in Ref. 2; AGM61326)"
FT /evidence="ECO:0000305"
FT CONFLICT 2060
FT /note="P -> R (in Ref. 2; AGM61326)"
FT /evidence="ECO:0000305"
FT CONFLICT 2132
FT /note="L -> P (in Ref. 2; AGM61326)"
FT /evidence="ECO:0000305"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1TMF"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1TME"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1TME"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:1TME"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:1TME"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1TME"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 250..262
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 270..279
FT /evidence="ECO:0007829|PDB:1TME"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:1TME"
FT HELIX 330..335
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:1TME"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:1TME"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 370..381
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 390..406
FT /evidence="ECO:0007829|PDB:1TME"
FT TURN 423..426
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:1TME"
FT HELIX 458..463
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 477..486
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 492..497
FT /evidence="ECO:0007829|PDB:1TME"
FT TURN 503..506
FT /evidence="ECO:0007829|PDB:1TME"
FT HELIX 508..513
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 516..521
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 523..529
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 536..544
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:1TME"
FT HELIX 554..557
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 560..566
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 572..577
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 582..584
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 586..589
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 601..611
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 618..628
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 633..637
FT /evidence="ECO:0007829|PDB:1TME"
FT HELIX 651..653
FT /evidence="ECO:0007829|PDB:1TME"
FT TURN 661..664
FT /evidence="ECO:0007829|PDB:1TME"
FT HELIX 679..683
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 687..692
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 710..715
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 721..723
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 744..749
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 751..755
FT /evidence="ECO:0007829|PDB:1TME"
FT HELIX 758..762
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 766..779
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 786..792
FT /evidence="ECO:0007829|PDB:1TME"
FT HELIX 810..812
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 813..816
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 818..823
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 828..833
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 838..845
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 869..875
FT /evidence="ECO:0007829|PDB:1TME"
FT STRAND 878..892
FT /evidence="ECO:0007829|PDB:1TME"
SQ SEQUENCE 2301 AA; 256161 MW; 0B6095DF153DBFDF CRC64;
MACKHGYPDV CPICTAVDVT PGFEYLLLAD GEWFPTDLLC VDLDDDVFWP SNSSNQSETM
EWTDLPLVRD IVMEPQGNAS SSDKSNSQSS GNEGVIINNF YSNQYQNSID LSASGGNAGD
APQNNGQLSN ILGGAANAFA TMAPLLLDQN TEEMENLSDR VASDKAGNSA TNTQSTVGRL
CGYGEAHHGE HPASCADTAT DKVLAAERYY TIDLASWTTT QEAFSHIRIP LPHVLAGEDG
GVFGATLRRH YLCKTGWRVQ VQCNASQFHA GSLLVFMAPE FYTGKGTKTG DMEPTDPFTM
DTTWRAPQGA PTGYRYDSRT GFFAMNHQNQ WQWTVYPHQI LNLRTNTTVD LEVPYVNIAP
TSSWTQHANW TLVVAVFSPL QYASGSSSDV QITASIQPVN PVFNGLRHET VIAQSPIAVT
VREHKGCFYS TNPDTTVPIY GKTISTPNDY MCGEFSDLLE LCKLPTFLGN PNSNNKRYPY
FSATNSVPTT SLVDYQVALS CSCMCNSMLA AVARNFNQYR GSLNFLFVFT GAAMVKGKFL
IAYTPPGAGK PTTRDQAMQA TYAIWDLGLN SSFVFTAPFI SPTHYRQTSY TSATIASVDG
WVTVWQLTPL TYPSGAPVNS DILTLVSAGD DFTLRMPISP TKWAPQGSDN AEKGKVSNDD
ASVDFVAEPV KLPENQTRVA FFYDRAVPIG MLRPGQNIES TFVYQENDLR LNCLLLTPLP
SFCPDSTSGP VKTKAPVQWR WVRSGGTTNF PLMTKQDYAF LCFSPFTYYK CDLEVTVSAL
GTDTVASVLR WAPTGAPADV TDQLIGYTPS LGETRNPHMW LVGAGNTQIS FVVPYNSPLS
VLPAAWFNGW SDFGNTKDFG VAPNADFGRL WIQGNTSASV RIRYKKMKVF CPRPTLFFPW
PVSTRSKINA DNPVPILELE NPAAFYRIDL FITFIDEFIT FDYKVHGRPV LTFRIPGFGL
TPAGRMLVCM GEKPAHGPFT SSRSLYHVIF TATCSSFSFS IYKGRYRSWK KPIHDELVDR
GYTTFGEFFR AVRAYHADYY KQRLIHDVEM NPGPVQSVFQ PQGAVLTKSL APQAGIQNLL
LRLLGIDGDC SEVSKAITVV TDLFAAWERA KTTLVSPEFW SKLILKTTKF IAASVLYLHN
PDFTTTVCLS LMTGVDLLTN DSVFDWLKNK LSSFFRTPPP VCPNVLQPQG PLREANEGFT
FAKNIEWAMK TIQSIVNWLT SWFKQEEDHP QSKLDKFLME FPDHCRNIMD MRNGRKAYCE
CTASFKYFDE LYNLAVTCKR IPLASLCEKF KNRHDHSVTR PEPVVVVLRG AAGQGKSVTS
QIIAQSVSKM AFGRQSVYSM PPDSEYFDGY ENQFSVIMDD LGQNPDGEDF TVFCQMVSST
NFLPNMAHLE RKGTPFTSSF IVATTNLPKF RPVTVAHYPA VDRRITFDFT VTAGPHCTTS
NGMLDIEKAF DEIPGSKPQL ACFSADCPLL HKRGVMFTCN RTKAVYNLQQ VVKMVNDTIT
RKTENVKKMN SLVAQSPPDW EHFENILTCL RQNNAALQDQ LDELQEAFAQ ARERSDFLSD
WLKVSAIIFA GIASLSAVIK LASKFKESIW PSPVRVELSE GEQAAYAGRA RAQKQALQVL
DIQGGGKVLA QAGNPVMDFE LFCAKNMVAP ITFYYPDKAE VTQSCLLLRA HLFVVNRHVA
ETEWTAFKLK DVRHERDTVV TRSVNRSGAE TDLTFIKVTK GPLFKDNVNK FCSNKDDFPA
RNDAVTGIMN TGLAFVYSGN FLIGNQPVNT TTGACFNHCL HYRAQTRRGW CGSAVICNVN
GKKAVYGMHS AGGGGLAAAT IITRELIEAA EKSMLALEPQ GAIVDISTGS VVHVPRKTKL
RRTVAHDVFQ PKFEPAVLSR YDPRTDKDVD VVAFSKHTTN MESLPPVFDI VCDEYANRVF
TILGKDNGLL TVEQAVLGLP GMDPMEKDTS PGLPYTQQGL RRTDLLNFNT AKMTPQLDYA
HSKLVLGVYD DVVYQSFLKD EIRPLEKIHE AKTRIVDVPP FAHCIWGRQL LGRFASKFQT
KPGLELGSAI GTDPDVDWTP YAAELSGFNY VYDVDYSNFD ASHSTAMFEC LIKNFFTEQN
GFDRRIAEYL RSLAVSRHAY EDRRVLIRGG LLSGCAATSM LNTIMNNVII RAALYLTYSN
FEFDDIKVLS YGDDLLIGTN YQIDFNLVKE RLAPFGYKIT PANKTTTFPL TSHLQDVTFL
KRRFVRFNSY LFRPQMDAVN LKAMVSYCKP GTLKEKLMSI ALLAVHSGPD IYDEIFLPFR
NVGIVVPTYS SMLYRWLSLF R
