POLG_SVV1
ID POLG_SVV1 Reviewed; 2181 AA.
AC Q155Z9;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Leader protein;
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 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 AltName: Full=Protein 3B;
DE Short=P3B;
DE AltName: Full=Viral protein genome-linked;
DE Contains:
DE RecName: Full=Protease 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE Short=P3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE EC=3.4.19.12 {ECO:0000269|PubMed:30408499};
DE EC=3.4.22.28 {ECO:0000255|PROSITE-ProRule:PRU01222};
DE AltName: Full=Picornain 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE AltName: Full=p22;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase {ECO:0000255|PROSITE-ProRule:PRU00539};
DE Short=RdRp;
DE EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE AltName: Full=3D polymerase;
DE Short=3Dpol;
DE AltName: Full=Protein 3D;
DE Short=3D;
OS Seneca Valley virus (isolate -/United States/SSV-001/2002) (SVV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Senecavirus.
OX NCBI_TaxID=686944 {ECO:0000312|Proteomes:UP000000672};
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], PROTEIN SEQUENCE OF 151-186;
RP 435-470 AND 674-699, FUNCTION (CAPSID PROTEIN VP1), FUNCTION (CAPSID
RP PROTEIN VP2), FUNCTION (CAPSID PROTEIN VP3), AND PROTEOLYTIC CLEAVAGE
RP (GENOME POLYPROTEIN).
RX PubMed=18420805; DOI=10.1099/vir.0.83570-0;
RA Hales L.M., Knowles N.J., Reddy P.S., Xu L., Hay C., Hallenbeck P.L.;
RT "Complete genome sequence analysis of Seneca Valley virus-001, a novel
RT oncolytic picornavirus.";
RL J. Gen. Virol. 89:1265-1275(2008).
RN [2]
RP FUNCTION (PROTEASE 3C), INTERACTION WITH HOST MAVS (PROTEASE 3C),
RP INTERACTION WITH HOST TRIF (PROTEASE 3C), AND INTERACTION WITH HOST TANK
RP (PROTEASE 3C).
RX PubMed=28566380; DOI=10.1128/jvi.00823-17;
RA Qian S., Fan W., Liu T., Wu M., Zhang H., Cui X., Zhou Y., Hu J., Wei S.,
RA Chen H., Li X., Qian P.;
RT "Seneca Valley virus suppresses host type I interferon production by
RT targeting adaptor proteins MAVS, TRIF, and TANK for cleavage.";
RL J. Virol. 91:0-0(2017).
RN [3]
RP FUNCTION (PROTEASE 3C), INTERACTION WITH HOST IRF3 (PROTEASE 3C), AND
RP INTERACTION WITH HOST IRF7 (PROTEASE 3C).
RX PubMed=29427864; DOI=10.1016/j.virol.2018.01.028;
RA Xue Q., Liu H., Zhu Z., Yang F., Ma L., Cai X., Xue Q., Zheng H.;
RT "Seneca Valley Virus 3Cpro abrogates the IRF3- and IRF7-mediated innate
RT immune response by degrading IRF3 and IRF7.";
RL Virology 518:1-7(2018).
RN [4]
RP FUNCTION (PROTEASE 3C), MUTAGENESIS OF HIS-1556 AND CYS-1668, INTERACTION
RP WITH HOST DDX58 (PROTEASE 3C), INTERACTION WITH HOST TBK1 (PROTEASE 3C),
RP INTERACTION WITH HOST TRAF3 (PROTEASE 3C), ACTIVE SITE (PROTEASE 3C), AND
RP CATALYTIC ACTIVITY (PROTEASE 3C).
RX PubMed=30408499; DOI=10.1016/j.antiviral.2018.10.028;
RA Xue Q., Liu H., Zhu Z., Yang F., Xue Q., Cai X., Liu X., Zheng H.;
RT "Seneca Valley Virus 3C protease negatively regulates the type I interferon
RT pathway by acting as a viral deubiquitinase.";
RL Antiviral Res. 160:183-189(2018).
RN [5] {ECO:0007744|PDB:3CJI}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 80-150; 151-434; 435-673 AND
RP 674-936, FUNCTION (CAPSID PROTEIN VP1), FUNCTION (CAPSID PROTEIN VP2),
RP FUNCTION (CAPSID PROTEIN VP3), AND FUNCTION (CAPSID PROTEIN VP4).
RX PubMed=18940610; DOI=10.1016/j.str.2008.07.013;
RA Venkataraman S., Reddy S.P., Loo J., Idamakanti N., Hallenbeck P.L.,
RA Reddy V.S.;
RT "Structure of Seneca Valley Virus-001: an oncolytic picornavirus
RT representing a new genus.";
RL Structure 16:1555-1561(2008).
CC -!- FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3 (PubMed:18940610).
CC Together they form an icosahedral capsid composed of 60 copies of each
CC VP1, VP2, and VP3, with a diameter of approximately 325 Angstroms
CC (Probable). VP4 lies on the inner surface of the protein shell formed
CC by VP1, VP2 and VP3 (By similarity). All the three latter proteins
CC contain a beta-sheet structure called beta-barrel jelly roll (By
CC similarity). VP1 is situated at the 12 fivefold axes, whereas VP2 and
CC VP3 are located at the quasi-sixfold axes (PubMed:18940610).
CC {ECO:0000250|UniProtKB:P12296, ECO:0000269|PubMed:18940610,
CC ECO:0000305|PubMed:18420805}.
CC -!- FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3 (PubMed:18940610).
CC Together they form an icosahedral capsid composed of 60 copies of each
CC VP1, VP2, and VP3, with a diameter of approximately 270 Angstroms
CC (Probable). VP4 lies on the inner surface of the protein shell formed
CC by VP1, VP2 and VP3 (By similarity). All the three latter proteins
CC contain a beta-sheet structure called beta-barrel jelly roll (By
CC similarity). VP1 is situated at the 12 fivefold axes, whereas VP2 and
CC VP3 are located at the quasi-sixfold axes (PubMed:18940610).
CC {ECO:0000250|UniProtKB:P12296, ECO:0000269|PubMed:18940610,
CC ECO:0000305|PubMed:18420805}.
CC -!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3 (Probable). Together they
CC form an icosahedral capsid composed of 60 copies of each VP1, VP2, and
CC VP3, with a diameter of approximately 270 Angstroms (PubMed:18420805).
CC VP4 lies on the inner surface of the protein shell formed by VP1, VP2
CC and VP3. All the three latter proteins contain a beta-sheet structure
CC called beta-barrel jelly roll (By similarity). VP1 is situated at the
CC 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold
CC axes (By similarity). {ECO:0000250|UniProtKB:P12296,
CC ECO:0000305|PubMed:18420805}.
CC -!- FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid
CC shell (PubMed:18940610). 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:P12296, ECO:0000305|PubMed:18940610}.
CC -!- FUNCTION: [Capsid protein VP0]: VP0 precursor is a component of
CC immature procapsids. {ECO:0000250|UniProtKB:P08617}.
CC -!- FUNCTION: [Protein 2A]: Mediates self-processing of the polyprotein by
CC a translational effect termed 'ribosome skipping'. Mechanistically, 2A-
CC mediated cleavage occurs between the C-terminal glycine and the proline
CC of the downstream protein 2B. {ECO:0000250|UniProtKB:P03305}.
CC -!- FUNCTION: [Protein 2B]: Plays an essential role in the virus
CC replication cycle by acting as a viroporin. Creates a pore in the host
CC reticulum endoplasmic and as a consequence releases Ca2+ in the
CC cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium
CC may trigger membrane trafficking and transport of viral ER-associated
CC proteins to viroplasms, sites of viral genome replication.
CC {ECO:0000250|UniProtKB:P03305}.
CC -!- FUNCTION: [Protein 2C]: Associates with and induces structural
CC rearrangements of intracellular membranes.
CC {ECO:0000250|UniProtKB:P03305}.
CC -!- FUNCTION: [VPg]: Covalently linked to the 5'-end of both the positive-
CC strand and negative-strand genomic RNAs. Acts as a genome-linked
CC replication primer. {ECO:0000250|UniProtKB:P03305}.
CC -!- FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral
CC proteins from the precursor polyprotein (By similarity). Inactivates
CC crucial host adapter molecules in order to suppress antiviral type-I
CC interferon (type-I IFN) and NF-kappaB production to escape host
CC antiviral innate immune responses (PubMed:30408499, PubMed:29427864,
CC PubMed:28566380). Deubiquitinase that acts on both lysine-48- and
CC lysine-63-linked polyubiquitin chains and inhibits the ubiquitination
CC of the ATP-dependent RNA helicase DDX58/RIG-I, TANK-binding kinase 1
CC (TBK1), and TNF receptor-associated factor 3 (TRAF3), thereby blocking
CC the expression of IFN-beta and IFN stimulated gene 54 (ISG54)
CC (PubMed:30408499). Induces host IRF3 and IRF7 degradation thereby
CC suppressing IRF3- and IRF7-induced type-I IFN production
CC (PubMed:29427864). Also decreases host IRF3 phosphorylation leading to
CC negligible IRF3 activation (PubMed:29427864). Cleaves host MAVS, TRIF
CC and TANK, which are then unable to regulate pattern recognition
CC receptor (PRR)-mediated type-I IFN production (PubMed:28566380).
CC {ECO:0000250|UniProtKB:P12296, ECO:0000269|PubMed:28566380,
CC ECO:0000269|PubMed:29427864, ECO:0000269|PubMed:30408499}.
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=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 -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:30408499};
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 -!- SUBUNIT: [Protease 3C]: Interacts with host IRF3; this interaction is
CC involved in the suppression of IRF3 and IRF7 expression and
CC phosphorylation by the virus (PubMed:29427864). Interacts with host
CC IRF7; this interaction is involved in the suppression of IRF3 and IRF7
CC expression and phosphorylation by the virus (PubMed:29427864).
CC Interacts with host MAVS; this interaction allows the cleavage of MAVS
CC and subsequent suppression of host immunity (PubMed:28566380).
CC Interacts with host TRIF; this interaction allows the cleavage of TRIF
CC and subsequent suppression of host immunity (PubMed:28566380).
CC Interacts with host TANK; this interaction allows the cleavage of TANK
CC and subsequent suppression of host immunity (PubMed:28566380).
CC Interacts with host DDX58 (PubMed:30408499). Interacts with host TBK1
CC (PubMed:30408499). Interacts with host TRAF3 (PubMed:30408499).
CC {ECO:0000269|PubMed:28566380, ECO:0000269|PubMed:29427864,
CC ECO:0000269|PubMed:30408499}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion
CC {ECO:0000250|UniProtKB:P12296}. Host cytoplasm
CC {ECO:0000250|UniProtKB:B8XTP8}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
CC {ECO:0000250|UniProtKB:P12296}. Host cytoplasm
CC {ECO:0000250|UniProtKB:B8XTP8}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC {ECO:0000250|UniProtKB:P12296}. Host cytoplasm
CC {ECO:0000250|UniProtKB:B8XTP8}.
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:0000250|UniProtKB:Q66765}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q66765}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q66765}. Note=Probably localizes to the surface
CC of intracellular membrane vesicles that are induced after virus
CC infection as the site for viral RNA replication. These vesicles are
CC probably autophagosome-like vesicles. {ECO:0000250|UniProtKB:B8XTP8}.
CC -!- SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q66765}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q66765}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q66765}. Note=Probably localizes to the surface
CC of intracellular membrane vesicles that are induced after virus
CC infection as the site for viral RNA replication. These vesicles are
CC probably autophagosome-like vesicles. {ECO:0000250|UniProtKB:B8XTP8}.
CC -!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P03304}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:B8XTP8}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:B8XTP8}. Note=Probably localizes to the surface
CC of intracellular membrane vesicles that are induced after virus
CC infection as the site for viral RNA replication. These vesicles are
CC probably autophagosome-like vesicles. {ECO:0000250|UniProtKB:B8XTP8}.
CC -!- SUBCELLULAR LOCATION: [VPg]: Virion {ECO:0000250|UniProtKB:B8XTP8}.
CC -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm
CC {ECO:0000250|UniProtKB:B8XTP8}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic
CC vesicle membrane {ECO:0000250|UniProtKB:Q66765}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q66765}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q66765}. Note=Probably localizes to the surface
CC of intracellular membrane vesicles that are induced after virus
CC infection as the site for viral RNA replication. These vesicles are
CC probably autophagosome-like vesicles. {ECO:0000250|UniProtKB:B8XTP8}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral
CC protease in vivo yield a variety of precursors and mature proteins
CC (Probable). 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 ECO:0000305|PubMed:18420805}.
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: [Capsid protein VP4]: Myristoylation is required during RNA
CC encapsidation and formation of the mature virus particle.
CC {ECO:0000250|UniProtKB:Q66282}.
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}.
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DR EMBL; DQ641257; ABG23522.1; -; Genomic_RNA.
DR RefSeq; YP_002268402.1; NC_011349.1.
DR PDB; 3CJI; X-ray; 2.30 A; A=674-936, B=435-673, C=151-434, D=80-150.
DR PDB; 6ADL; EM; 3.08 A; B=182-427.
DR PDB; 6L0T; X-ray; 1.90 A; A/B=1509-1719.
DR PDBsum; 3CJI; -.
DR PDBsum; 6ADL; -.
DR PDBsum; 6L0T; -.
DR SMR; Q155Z9; -.
DR DIP; DIP-46244N; -.
DR GeneID; 6966369; -.
DR KEGG; vg:6966369; -.
DR EvolutionaryTrace; Q155Z9; -.
DR Proteomes; UP000000672; 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:0039617; C:T=3 icosahedral viral capsid; IDA:UniProtKB.
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:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
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:1990380; F:Lys48-specific deubiquitinase activity; IMP:UniProtKB.
DR GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IMP:UniProtKB.
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: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:0039722; P:suppression by virus of host toll-like receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0039547; P:suppression by virus of host TRAF activity; IEA:UniProtKB-KW.
DR GO; GO:0039540; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity; IDA:UniProtKB.
DR GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IDA:UniProtKB.
DR GO; GO:0039557; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF7 activity; IDA:UniProtKB.
DR GO; GO:0039545; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; IDA:UniProtKB.
DR GO; GO:0039723; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity; IDA:UniProtKB.
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; 2.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.60.120.20; -; 3.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 4.10.90.10; -; 1.
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; IPR027417; P-loop_NTPase.
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 PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 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 Direct protein sequencing; Helicase; Host cytoplasm;
KW Host cytoplasmic vesicle; Host membrane; Host nucleus;
KW Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host IRF3 by virus; Inhibition of host IRF7 by virus;
KW Inhibition of host MAVS by virus; Inhibition of host RIG-I by virus;
KW Inhibition of host RLR pathway by virus; Inhibition of host TBK1 by virus;
KW Inhibition of host TLR pathway by virus; Inhibition of host TRAFs by virus;
KW Ion channel; Ion transport; Lipoprotein; Membrane; Myristate;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
KW Reference proteome; RNA-binding; RNA-directed RNA polymerase;
KW T=pseudo3 icosahedral capsid protein; Thiol protease; Transferase;
KW Transport; Ubl conjugation pathway; Viral attachment to host cell;
KW Viral immunoevasion; Viral ion channel; Viral RNA replication; Virion;
KW Virus entry into host cell.
FT CHAIN 1..2181
FT /note="Genome polyprotein"
FT /id="PRO_0000446923"
FT CHAIN 1..79
FT /note="Leader protein"
FT /id="PRO_0000446924"
FT CHAIN 80..434
FT /note="Capsid protein VP0"
FT /id="PRO_0000446925"
FT CHAIN 80..150
FT /note="Capsid protein VP4"
FT /id="PRO_0000446926"
FT CHAIN 151..434
FT /note="Capsid protein VP2"
FT /id="PRO_0000446927"
FT CHAIN 435..?673
FT /note="Capsid protein VP3"
FT /id="PRO_0000446928"
FT CHAIN ?674..937
FT /note="Capsid protein VP1"
FT /id="PRO_0000446929"
FT CHAIN 938..946
FT /note="Protein 2A"
FT /id="PRO_0000446930"
FT CHAIN 947..1074
FT /note="Protein 2B"
FT /id="PRO_0000446931"
FT CHAIN 1075..1396
FT /note="Protein 2C"
FT /id="PRO_0000446932"
FT CHAIN 1397..?1486
FT /note="Protein 3A"
FT /id="PRO_0000446933"
FT CHAIN ?1487..1508
FT /note="VPg"
FT /id="PRO_0000446934"
FT CHAIN 1509..1719
FT /note="Protease 3C"
FT /id="PRO_0000446935"
FT CHAIN 1720..2181
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000446936"
FT DOMAIN 1165..1333
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1511..1704
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1950..2068
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 1472..1500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1556
FT /note="For protease 3C activity and deubiquitinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222,
FT ECO:0000269|PubMed:30408499"
FT ACT_SITE 1592
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1668
FT /note="For protease 3C activity and deubiquitinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222,
FT ECO:0000269|PubMed:30408499"
FT ACT_SITE 1956
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT ACT_SITE 2054
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT BINDING 1197..1204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 79..80
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000305|PubMed:18420805"
FT SITE 150..151
FT /note="Cleavage"
FT /evidence="ECO:0000305|PubMed:18420805"
FT SITE 434..435
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000305|PubMed:18420805"
FT SITE 937..938
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000305|PubMed:18420805"
FT SITE 946..947
FT /note="Cleavage; by ribosomal skip"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1074..1075
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000305|PubMed:18420805"
FT SITE 1396..1397
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000305|PubMed:18420805"
FT SITE 1508..1509
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000305|PubMed:18420805"
FT SITE 1719..1720
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000305|PubMed:18420805"
FT MOD_RES 1489
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT LIPID 80
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q66282"
FT MUTAGEN 1556
FT /note="H->A: Complete loss of protease 3C deubiquitinating
FT activity and ability to block IFN-beta induction."
FT /evidence="ECO:0000269|PubMed:30408499"
FT MUTAGEN 1668
FT /note="C->A: Complete loss of protease 3C deubiquitinating
FT activity and ability to block IFN-beta induction."
FT /evidence="ECO:0000269|PubMed:30408499"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:3CJI"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:3CJI"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:3CJI"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:3CJI"
FT HELIX 249..255
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 258..270
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 278..288
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:6ADL"
FT HELIX 302..308
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:3CJI"
FT HELIX 315..319
FT /evidence="ECO:0007829|PDB:3CJI"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:6ADL"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:6ADL"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:3CJI"
FT HELIX 346..351
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 352..358
FT /evidence="ECO:0007829|PDB:3CJI"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 363..369
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:3CJI"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 385..397
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 408..422
FT /evidence="ECO:0007829|PDB:3CJI"
FT TURN 443..446
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:3CJI"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 498..501
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 503..508
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 518..523
FT /evidence="ECO:0007829|PDB:3CJI"
FT TURN 528..532
FT /evidence="ECO:0007829|PDB:3CJI"
FT HELIX 534..539
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 542..547
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 549..555
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 562..570
FT /evidence="ECO:0007829|PDB:3CJI"
FT HELIX 580..583
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 586..592
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 594..596
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 598..603
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 608..615
FT /evidence="ECO:0007829|PDB:3CJI"
FT TURN 621..623
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 627..637
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 647..654
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 659..663
FT /evidence="ECO:0007829|PDB:3CJI"
FT HELIX 668..671
FT /evidence="ECO:0007829|PDB:3CJI"
FT HELIX 678..680
FT /evidence="ECO:0007829|PDB:3CJI"
FT TURN 688..691
FT /evidence="ECO:0007829|PDB:3CJI"
FT HELIX 706..710
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 714..724
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 760..764
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 770..773
FT /evidence="ECO:0007829|PDB:3CJI"
FT HELIX 781..786
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 789..804
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 810..814
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 824..827
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 830..833
FT /evidence="ECO:0007829|PDB:3CJI"
FT HELIX 834..836
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 837..840
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 842..844
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 851..855
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 859..867
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 872..876
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 889..893
FT /evidence="ECO:0007829|PDB:3CJI"
FT HELIX 898..900
FT /evidence="ECO:0007829|PDB:3CJI"
FT STRAND 907..922
FT /evidence="ECO:0007829|PDB:3CJI"
FT HELIX 1515..1523
FT /evidence="ECO:0007829|PDB:6L0T"
FT STRAND 1525..1531
FT /evidence="ECO:0007829|PDB:6L0T"
FT STRAND 1539..1548
FT /evidence="ECO:0007829|PDB:6L0T"
FT STRAND 1550..1553
FT /evidence="ECO:0007829|PDB:6L0T"
FT HELIX 1555..1559
FT /evidence="ECO:0007829|PDB:6L0T"
FT STRAND 1564..1568
FT /evidence="ECO:0007829|PDB:6L0T"
FT STRAND 1571..1574
FT /evidence="ECO:0007829|PDB:6L0T"
FT STRAND 1580..1586
FT /evidence="ECO:0007829|PDB:6L0T"
FT STRAND 1589..1597
FT /evidence="ECO:0007829|PDB:6L0T"
FT HELIX 1608..1610
FT /evidence="ECO:0007829|PDB:6L0T"
FT STRAND 1622..1627
FT /evidence="ECO:0007829|PDB:6L0T"
FT STRAND 1631..1648
FT /evidence="ECO:0007829|PDB:6L0T"
FT STRAND 1651..1661
FT /evidence="ECO:0007829|PDB:6L0T"
FT HELIX 1665..1667
FT /evidence="ECO:0007829|PDB:6L0T"
FT STRAND 1671..1676
FT /evidence="ECO:0007829|PDB:6L0T"
FT STRAND 1679..1690
FT /evidence="ECO:0007829|PDB:6L0T"
FT STRAND 1693..1698
FT /evidence="ECO:0007829|PDB:6L0T"
FT HELIX 1701..1710
FT /evidence="ECO:0007829|PDB:6L0T"
SQ SEQUENCE 2181 AA; 240620 MW; FA8BF3068931AB9A CRC64;
MQNSHFSFDT ASGTFEDVTG TKVKIVEYPR SVNNGVYDSS THLEILNLQG EIEILRSFNE
YQIRAAKQQL GLDIVYELQG NVQTTSKNDF DSRGNNGNMT FNYYANTYQN SVDFSTSSSA
SGAGPGNSRG GLAGLLTNFS GILNPLGYLK DHNTEEMENS ADRVTTQTAG NTAINTQSSL
GVLCAYVEDP TKSDPPSSST DQPTTTFTAI DRWYTGRLNS WTKAVKTFSF QAVPLPGAFL
SRQGGLNGGA FTATLHRHFL MKCGWQVQVQ CNLTQFHQGA LLVAMVPETT LDVKPDGKAK
SLQELNEEQW VEMSDDYRTG KNMPFQSLGT YYRPPNWTWG PNFINPYQVT VFPHQILNAR
TSTSVDINVP YIGETPTQSS ETQNSWTLLV MVLVPLDYKE GATTDPEITF SVRPTSPYFN
GLRNRYTAGT DEEQGPIPTA PRENSLMFLS TLPDDTVPAY GNVRTPPVNY LPGEITDLLQ
LARIPTLMAF ERVPEPVPAS DTYVPYVAVP TQFDDRPLIS FPITLSDPVY QNTLVGAISS
NFANYRGCIQ ITLTFCGPMM ARGKFLLSYS PPNGTQPQTL SEAMQCTYSI WDIGLNSSWT
FVVPYISPSD YRETRAITNS VYSADGWFSL HKLTKITLPP DCPQSPCILF FASAGEDYTL
RLPVDCNPSY VFHSTDNAET GVIEAGNTDT DFSGELAAPG SNHTNVKFLF DRSRLLNVIK
VLEKDAVFPR PFPTQEGAQQ DDGYFCLLTP RPTVASRPAT RFGLYANPSG SGVLANTSLD
FNFYSLACFT YFRSDLEVTV VSLEPDLEFA VGWFPSGSEY QASSFVYDQL HVPFHFTGRT
PRAFASKGGK VSFVLPWNSV SSVLPVRWGG ASKLSSATRG LPAHADWGTI YAFVPRPNEK
KSTAVKHVAV YIRYKNARAW CPSMLPFRSY KQKMLMQSGD IETNPGPASD NPILEFLEAE
NDLVTLASLW KMVHSVQQTW RKYVKNDDFW PNLLSELVGE GSVALAATLS NQASVKALLG
LHFLSRGLNY TDFYSLLIEK CSSFFTVEPP PPPAENLMTK PSVKSKFRKL FKMQGPMDKV
KDWNQIAAGL KNFQFVRDLV KEVVDWLQAW INKEKASPVL QYQLEMKKLG PVALAHDAFM
AGSGPPLSDD QIEYLQNLKS LALTLGKTNL AQSLTTMINA KQSSAQRVEP VVVVLRGKPG
CGKSLASTLI AQAVSKRLYG SQSVYSLPPD PDFFDGYKGQ FVTLMDDLGQ NPDGQDFSTF
CQMVSTAQFL PNMADLAEKG RPFTSNLIIA TTNLPHFSPV TIADPSAVSR RINYDLTLEV
SEAYKKHTRL NFDLAFRRTD APPIYPFAAH VPFVDVAVRF KNGHQNFNLL ELVDSICTDI
RAKQQGARNM QTLVLQSPNE NDDTPVDEAL GRVLSPAAVD EALVDLTPEA DPVGRLAILA
KLGLALAAVT PGLIILAVGL YRYFSGSDAD QEETESEGSV KAPRSENAYD GPKKNSKPPG
ALSLMEMQQP NVDMGFEAAV AKKVVVPITF MVPNRPSGLT QSALLVTGRT FLINEHTWSN
PSWTSFTIRG EVHTRDEPFQ TVHFTHHGIP TDLMMVRLGP GNSFPNNLDK FGLDQMPARN
SRVVGVSSSY GNFFFSGNFL GFVDSITSEQ GTYARLFRYR VTTYKGWCGS ALVCEAGGVR
RIIGLHSAGA AGIGAGTYIS KLGLIKALKH LGEPLATMQG LMTELEPGIT VHVPRKSKLR
KTTAHAVYKP EFEPAVLSKF DPRLNKDVDL DEVIWSKHTA NVPYQPPLFY TYMSEYAHRV
FSFLGKDNDI LTVKEAILGI PGLDPMDPHT APGLPYAING LRRTDLVDFV NGTVDAALAV
QIQKFLDGDY SDHVFQTFLK DEIRPSEKVR AGKTRIVDVP SLAHCIVGRM LLGRFAAKFQ
SHPGFLLGSA IGSDPDVFWT VIGAQLEGRK NTYDVDYSAF DSSHGTGSFE ALISHFFTVD
NGFSPALGPY LRSLAVSVHA YGERRIKITG GLPSGCAATS LLNTVLNNVI IRTALALTYK
EFEYDMVDII AYGDDLLVGT DYDLDFNEVA RRAAKLGYKM TPANKGSVFP PTSSLSDAVF
LKRKFVQNND GLYKPVMDLK NLEAMLSYFK PGTLLEKLQS VSMLAQHSGK EEYDRLMHPF
ADYGAVPSHE YLQARWRALF D
