ID   POLG_FMDVI              Reviewed;        2328 AA.
AC   P03310; Q65066; Q6PMY0;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   24-JAN-2024, entry version 135.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Leader protease;
DE              Short=Lpro;
DE              EC=3.4.22.46;
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     AltName: Full=P52;
DE   Contains:
DE     RecName: Full=Protein 2B;
DE              Short=P2B;
DE   Contains:
DE     RecName: Full=Protein 2C;
DE              Short=P2C;
DE              EC=3.6.1.15;
DE   Contains:
DE     RecName: Full=Protein 3A;
DE              Short=P3A;
DE   Contains:
DE     RecName: Full=Protein 3B-1;
DE              Short=P3B-1;
DE     AltName: Full=Genome-linked protein VPg1;
DE   Contains:
DE     RecName: Full=Protein 3B-2;
DE              Short=P3B-2;
DE     AltName: Full=Genome-linked protein VPg2;
DE   Contains:
DE     RecName: Full=Protein 3B-3;
DE              Short=P3B-3;
DE     AltName: Full=Genome-linked protein VPg3;
DE   Contains:
DE     RecName: Full=Protease 3C;
DE              EC=3.4.22.28;
DE     AltName: Full=Picornain 3C;
DE              Short=P3C;
DE     AltName: Full=Protease P20B;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase 3D-POL;
DE              Short=P3D-POL;
DE              EC=2.7.7.48;
DE     AltName: Full=P56A;
OS   Foot-and-mouth disease virus (isolate -/Brazil/C3Indaial/1971 serotype C)
OS   (FMDV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Caphthovirinae; Aphthovirus;
OC   Foot-and-mouth disease virus.
OX   NCBI_TaxID=12117;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=9925; Capra hircus (Goat).
OH   NCBI_TaxID=9850; Cervidae (Deer).
OH   NCBI_TaxID=9363; Erinaceidae (hedgehogs).
OH   NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH   NCBI_TaxID=9940; Ovis aries (Sheep).
OH   NCBI_TaxID=10116; Rattus norvegicus (Rat).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15858032; DOI=10.1128/jvi.79.10.6487-6504.2005;
RA   Carrillo C., Tulman E.R., Delhon G., Lu Z., Carreno A., Vagnozzi A.,
RA   Kutish G.F., Rock D.L.;
RT   "Comparative genomics of foot-and-mouth disease virus.";
RL   J. Virol. 79:6487-6504(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 202-933.
RX   PubMed=1316467; DOI=10.1128/jvi.66.6.3557-3565.1992;
RA   Martinez M.A., Dopazo J., Hernandez J., Mateu M.G., Sobrino F., Domingo E.,
RA   Knowles N.J.;
RT   "Evolution of the capsid protein genes of foot-and-mouth disease virus:
RT   antigenic variation without accumulation of amino acid substitutions over
RT   six decades.";
RL   J. Virol. 66:3557-3565(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 714-947.
RX   PubMed=6298715; DOI=10.1093/nar/10.24.8285;
RA   Makoff A.J., Paynter C.A., Rowlands D.J., Boothroyd J.C.;
RT   "Comparison of the amino acid sequence of the major immunogen from three
RT   serotypes of foot and mouth disease virus.";
RL   Nucleic Acids Res. 10:8285-8295(1982).
CC   -!- FUNCTION: [Leader protease]: Autocatalytically cleaves itself from the
CC       polyprotein at the L/VP0 junction. Also cleaves the host translation
CC       initiation factors EIF4G1 and EIF4G3, in order to shut off the capped
CC       cellular mRNA transcription. Plays a role in counteracting host innate
CC       antiviral response using diverse mechanisms. Possesses a deubiquitinase
CC       activity acting on both 'Lys-48' and 'Lys-63'-linked polyubiquitin
CC       chains. In turn, inhibits the ubiquitination and subsequent activation
CC       of key signaling molecules of type I IFN response such as host RIGI,
CC       TBK1, TRAF3 and TRAF6. Inhibits host NF-kappa-B activity by inducing a
CC       decrease in RELA mRNA levels. Cleaves a peptide bond in the C-terminus
CC       of host ISG15, resulting in the damaging of this modifier that can no
CC       longer be attached to target proteins. Also cleaves host G3BP1 and
CC       G3BP2 in order to inhibit cytoplasmic stress granules assembly.
CC       {ECO:0000250|UniProtKB:P03305, ECO:0000250|UniProtKB:P03308}.
CC   -!- FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid
CC       shell. After binding to the host receptor, the capsid undergoes
CC       conformational changes. Capsid protein VP4 is released, capsid protein
CC       VP1 N-terminus is externalized, and together, they shape a pore in the
CC       host membrane through which the viral genome is translocated into the
CC       host cell cytoplasm. After genome has been released, the channel
CC       shrinks. {ECO:0000250|UniProtKB:P03300}.
CC   -!- FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo
CC       T=3 symmetry with capsid proteins VP1 and VP3. The capsid is composed
CC       of 60 copies of each capsid protein organized in the form of twelve
CC       pentamers and encloses the viral positive strand RNA genome.
CC       {ECO:0000250|UniProtKB:P03305}.
CC   -!- FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo
CC       T=3 symmetry with capsid proteins VP2 and VP3. The capsid is composed
CC       of 60 copies of each capsid protein organized in the form of twelve
CC       pentamers and encloses the viral positive strand RNA genome. Mediates
CC       cell entry by attachment to an integrin receptor, usually host
CC       ITGAV/ITGB6. In addition, targets host MAVS to suppress type I IFN
CC       pathway. {ECO:0000250|UniProtKB:P03305}.
CC   -!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
CC       T=3 symmetry with capsid proteins VP0 and VP3. The capsid is composed
CC       of 60 copies of each capsid protein organized in the form of twelve
CC       pentamers and encloses the viral positive strand RNA genome.
CC       {ECO:0000250|UniProtKB:P03305}.
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. In the case of foot-and-mouth disease
CC       virus, the 2A oligopeptide is post-translationally 'trimmed' from the
CC       C-terminus of the upstream protein 1D by 3C proteinase.
CC       {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. Triggers host autophagy by
CC       interacting with host BECN1 and thereby promotes viral replication.
CC       Participates in viral replication and interacts with host DHX9.
CC       Displays RNA-binding, nucleotide binding and NTPase activities. May
CC       play a role in virion morphogenesis and viral RNA encapsidation by
CC       interacting with the capsid protein VP3.
CC       {ECO:0000250|UniProtKB:P03305}.
CC   -!- FUNCTION: [Protein 3A]: Plays important roles in virus replication,
CC       virulence and host range. Cooperates with host DDX56 to inhibit IRF3
CC       nuclear translocation and subsequent type I interferon production.
CC       {ECO:0000250|UniProtKB:P03305}.
CC   -!- FUNCTION: [Protein 3B-1]: Covalently linked to the 5'-end of both the
CC       positive-strand and negative-strand genomic RNAs. Acts as a genome-
CC       linked replication primer. {ECO:0000250|UniProtKB:P03305}.
CC   -!- FUNCTION: [Protein 3B-2]: Covalently linked to the 5'-end of both the
CC       positive-strand and negative-strand genomic RNAs. Acts as a genome-
CC       linked replication primer. {ECO:0000250|UniProtKB:P03305}.
CC   -!- FUNCTION: [Protein 3B-3]: Covalently linked to the 5'-end of both the
CC       positive-strand and negative-strand genomic RNAs. Acts as a genome-
CC       linked replication primer. {ECO:0000250|UniProtKB:P03305}.
CC   -!- FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral
CC       proteins from the precursor polyprotein. In addition to its proteolytic
CC       activity, binds to viral RNA and thus influences viral genome
CC       replication. RNA and substrate bind cooperatively to the protease.
CC       {ECO:0000250|UniProtKB:P03305}.
CC   -!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic and
CC       antigenomic RNA by recognizing replications specific signals.
CC       Covalently attaches UMP to a tyrosine of VPg, which is used to prime
CC       RNA synthesis. The positive stranded RNA genome is first replicated at
CC       virus induced membranous vesicles, creating a dsRNA genomic replication
CC       form. This dsRNA is then used as template to synthesize positive
CC       stranded RNA genomes. ss(+)RNA genomes are either translated,
CC       replicated or encapsidated. {ECO:0000250|UniProtKB:P03305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Autocatalytically cleaves itself from the polyprotein of the
CC         foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but
CC         then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-
CC         Arg- and -Lys-|-Arg-.; EC=3.4.22.46;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC   -!- 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   -!- SUBUNIT: [Leader protease]: Interacts with host ISG15. Capsid protein
CC       VP1: Interacts (via R-G-D motif) with host ITGAV/ITGB6. Interacts with
CC       host MAVS; this interaction inhibits binding of host TRAF3 to MAVS,
CC       thereby suppressing interferon-mediated responses.
CC       {ECO:0000250|UniProtKB:P03305}.
CC   -!- SUBUNIT: [Protein 2B]: Forms homooligomers.
CC       {ECO:0000250|UniProtKB:P03305}.
CC   -!- SUBUNIT: [Protein 2C]: Interacts with host VIM. Interacts with host
CC       BECN1. {ECO:0000250|UniProtKB:P03305}.
CC   -!- SUBUNIT: [Protein 3A]: Interacts with host DCTN3.
CC       {ECO:0000250|UniProtKB:P03305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion. Host cytoplasm
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion. Host cytoplasm
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion. Host cytoplasm
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC       side {ECO:0000305}. Note=Probably localizes to the surface of
CC       intracellular membrane vesicles that are induced after virus infection
CC       as the site for viral RNA replication. These vesicles are derived from
CC       the endoplasmic reticulum (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC       side {ECO:0000305}. Note=Probably localizes to the surface of
CC       intracellular membrane vesicles that are induced after virus infection
CC       as the site for viral RNA replication. These vesicles are derived from
CC       the endoplasmic reticulum (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC       side {ECO:0000305}. Note=Probably localizes to the surface of
CC       intracellular membrane vesicles that are induced after virus infection
CC       as the site for viral RNA replication. These vesicles are derived from
CC       the endoplasmic reticulum (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Protein 3B-1]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Protein 3B-2]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Protein 3B-3]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase 3D-POL]: Host
CC       cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes
CC       to the surface of intracellular membrane vesicles that are induced
CC       after virus infection as the site for viral RNA replication. These
CC       vesicles are derived from the endoplasmic reticulum (By similarity).
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Lab;
CC         IsoId=P03310-1; Sequence=Displayed;
CC       Name=Lb;
CC         IsoId=P03310-2; Sequence=VSP_046531;
CC   -!- PTM: Specific enzymatic cleavages in vivo by the viral proteases yield
CC       a variety of precursors and mature proteins. Polyprotein processing
CC       intermediates such as VP0 which is a VP4-VP2 precursor are produced.
CC       During virion maturation, non-infectious particles are rendered
CC       infectious following cleavage of VP0. This maturation cleavage is
CC       followed by a conformational change of the particle. The polyprotein
CC       seems to be cotranslationally cleaved at the 2A/2B junction by a
CC       ribosomal skip from one codon to the next without formation of a
CC       peptide bond. This process would release the L-P1-2A peptide from the
CC       translational complex (By similarity). {ECO:0000250}.
CC   -!- PTM: Myristoylation of VP4 is required during RNA encapsidation and
CC       formation of the mature virus particle. {ECO:0000250}.
CC   -!- PTM: Protein 3B-1, 3B-2 and 3B-3 are uridylylated by the polymerase and
CC       are covalently linked to the 5'-end of genomic RNA. These uridylylated
CC       forms act as a nucleotide-peptide primer for the polymerase (By
CC       similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: The capsid protein VP1 contains the main antigenic
CC       determinants of the virion; therefore, changes in its sequence must be
CC       responsible for the high antigenic variability of the virus.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AY593806; AAT01749.1; -; Genomic_RNA.
DR   EMBL; M90376; AAA91492.1; -; Genomic_RNA.
DR   EMBL; J02184; AAA42618.1; -; Genomic_RNA.
DR   PIR; A03912; A03912.
DR   SMR; P03310; -.
DR   MEROPS; C28.001; -.
DR   Proteomes; UP000012668; Genome.
DR   GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0039520; P:induction by virus of host autophagy; ISS:UniProtKB.
DR   GO; GO:0039525; P:modulation by virus of host chromatin organization; 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:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039707; P:virus-mediated pore formation in host cell membrane; IEA:UniProtKB-KW.
DR   CDD; cd23210; Aphthovirus_RdRp; 1.
DR   CDD; cd00205; rhv_like; 3.
DR   Gene3D; 1.20.960.20; -; 1.
DR   Gene3D; 2.60.120.20; -; 3.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 4.10.90.10; Capsid protein VP4 superfamily, Picornavirus; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR015031; Capsid_VP4_Picornavir.
DR   InterPro; IPR037080; Capsid_VP4_sf_Picornavirus.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR004080; FMDV_VP1_coat.
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; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR044067; PCV_3C_PRO.
DR   InterPro; IPR008739; Peptidase_C28.
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; PF05408; Peptidase_C28; 1.
DR   Pfam; PF00548; Peptidase_C3; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   Pfam; PF00073; Rhv; 3.
DR   Pfam; PF00910; RNA_helicase; 1.
DR   Pfam; PF08935; VP4_2; 1.
DR   PRINTS; PR00918; CALICVIRUSNS.
DR   PRINTS; PR01542; FMDVP1COAT.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF88633; Positive stranded ssRNA viruses; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51887; APHTHOVIRUS_LPRO; 1.
DR   PROSITE; PS51874; PCV_3C_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51218; SF3_HELICASE_2; 1.
PE   3: Inferred from homology;
KW   Alternative initiation; ATP-binding; Capsid protein;
KW   Clathrin- and caveolin-independent endocytosis of virus by host;
KW   Clathrin-mediated endocytosis of virus by host;
KW   Covalent protein-RNA linkage; Disulfide bond; Helicase; Host cytoplasm;
KW   Host cytoplasmic vesicle; Host membrane; Host-virus interaction; Hydrolase;
KW   Ion channel; Ion transport; Lipoprotein; Membrane;
KW   Modulation of host chromatin by virus; Myristate; Nucleotide-binding;
KW   Nucleotidyltransferase; Phosphoprotein; Protease; RNA-binding;
KW   RNA-directed RNA polymerase; T=pseudo3 icosahedral capsid protein;
KW   Thiol protease; Transferase; Translation regulation; Transport;
KW   Viral attachment to host cell; Viral ion channel;
KW   Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW   Virus endocytosis by host; Virus entry into host cell.
FT   CHAIN           1..2328
FT                   /note="Genome polyprotein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000422504"
FT   CHAIN           1..201
FT                   /note="Leader protease"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000422505"
FT   CHAIN           202..504
FT                   /note="Capsid protein VP0"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000422506"
FT   CHAIN           202..286
FT                   /note="Capsid protein VP4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000422507"
FT   CHAIN           287..504
FT                   /note="Capsid protein VP2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000422508"
FT   CHAIN           505..723
FT                   /note="Capsid protein VP3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000039869"
FT   CHAIN           724..931
FT                   /note="Capsid protein VP1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000039870"
FT   CHAIN           932..949
FT                   /note="Protein 2A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000039871"
FT   CHAIN           950..1103
FT                   /note="Protein 2B"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000422509"
FT   CHAIN           1104..1421
FT                   /note="Protein 2C"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000422510"
FT   CHAIN           1422..1574
FT                   /note="Protein 3A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000422511"
FT   CHAIN           1575..1597
FT                   /note="Protein 3B-1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000422512"
FT   CHAIN           1598..1621
FT                   /note="Protein 3B-2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000422513"
FT   CHAIN           1622..1645
FT                   /note="Protein 3B-3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000422514"
FT   CHAIN           1646..1858
FT                   /note="Protease 3C"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000422515"
FT   CHAIN           1859..2328
FT                   /note="RNA-directed RNA polymerase 3D-POL"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000422516"
FT   TOPO_DOM        1..1476
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        1477..1497
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1498..2328
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1..201
FT                   /note="Peptidase C28"
FT   DOMAIN          1185..1349
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1648..1844
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          2092..2210
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          199..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1525..1580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           865..867
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        200..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1549..1563
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        51
FT                   /note="For leader protease activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        148
FT                   /note="For leader protease activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        163
FT                   /note="For leader protease activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        1691
FT                   /note="For protease 3C activity; Proton donor/acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1729
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1808
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        2196
FT                   /note="For RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   BINDING         1213..1220
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   SITE            201..202
FT                   /note="Cleavage; by leader protease"
FT                   /evidence="ECO:0000255"
FT   SITE            286..287
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            504..505
FT                   /note="Cleavage; by picornain 3C"
FT                   /evidence="ECO:0000255"
FT   SITE            723..724
FT                   /note="Cleavage; by picornain 3C"
FT                   /evidence="ECO:0000255"
FT   SITE            931..932
FT                   /note="Cleavage; by picornain 3C"
FT                   /evidence="ECO:0000255"
FT   SITE            949..950
FT                   /note="Cleavage; by ribosomal skip"
FT                   /evidence="ECO:0000255"
FT   SITE            1103..1104
FT                   /note="Cleavage; by picornain 3C"
FT                   /evidence="ECO:0000255"
FT   SITE            1421..1422
FT                   /note="Cleavage; by picornain 3C"
FT                   /evidence="ECO:0000255"
FT   SITE            1574..1575
FT                   /note="Cleavage; by picornain 3C"
FT                   /evidence="ECO:0000255"
FT   SITE            1597..1598
FT                   /note="Cleavage; by picornain 3C"
FT                   /evidence="ECO:0000255"
FT   SITE            1621..1622
FT                   /note="Cleavage; by picornain 3C"
FT                   /evidence="ECO:0000255"
FT   SITE            1645..1646
FT                   /note="Cleavage; by picornain 3C"
FT                   /evidence="ECO:0000255"
FT   SITE            1858..1859
FT                   /note="Cleavage; by picornain 3C"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1577
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1600
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1624
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250"
FT   LIPID           202
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250"
FT   DISULFID        511
FT                   /note="Interchain; in VP3 dimer"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..28
FT                   /note="Missing (in isoform Lb)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_046531"
FT   VARIANT         330
FT                   /note="S -> A"
FT   VARIANT         376
FT                   /note="V -> A"
FT   VARIANT         420
FT                   /note="D -> E"
FT   VARIANT         458
FT                   /note="N -> K"
FT   VARIANT         515
FT                   /note="Y -> F"
FT   VARIANT         560
FT                   /note="T -> M"
FT   VARIANT         638
FT                   /note="N -> S"
FT   VARIANT         677
FT                   /note="E -> D"
FT   VARIANT         722
FT                   /note="Q -> L"
FT   VARIANT         747
FT                   /note="T -> I"
FT   VARIANT         766
FT                   /note="Q -> H"
FT   VARIANT         805
FT                   /note="H -> Q"
FT   VARIANT         825
FT                   /note="T -> A"
FT   VARIANT         852
FT                   /note="A -> T"
FT   VARIANT         861..863
FT                   /note="TGV -> ASA"
FT   VARIANT         917
FT                   /note="A -> T"
SQ   SEQUENCE   2328 AA;  258282 MW;  B2D0CE9A4BA94622 CRC64;
     MNTTDCFIAL VHAIREIKTH FFSRYTGRME FTLHNGEKKI FYSRPNNHDN CWLNTILQLF
     RYVDEPFFDW VYNSPENLTL SAIEQLEKLT GLELREGGPP ALVIWNIKHL LHTGIGTASR
     PSEVCMVDGT DMCLADFHAG IFLKGQEHAV FACVTSDGWY AIDDEDFYPW TPDPSDVLVF
     VPYDQEPLNG GWKANVQRKL KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG
     DNAISGGSNE GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI
     LTTRNGHTTS TTQSSVGVTY GYATTEDSTS GPNTSGLETR VHQAERFFKM TLFEWVPSQS
     FGHMHKVVLP SEPKGVYGGL VKSYAYMRNG WDVEVTAVGN QFNGGCLLVA LVPEMGDISD
     REKYQLTLYP HQFINPRTNM TAHITVPYVG VNRYDQYNQH KPWTLVVMVV APLTVNTSGA
     QQIKVYANIA PTNVHVAGEL PSKEGIFPVA CADGYGNMVT TDPKTADPAY GKVYNPPRTA
     LPGRFTNYLD VAEACPTLLT FENVPYVSTR TDGQRLLAKF DVSLAAKHMS NTYLAGLAQY
     YTQYAGTINL HFMFTGPTDA KARYMVAYVP PGMEAPDNPE EAAHCIHAEW DTGLNSKFTF
     SIPYISAADY AYTASSEAET TSVQGWVCVY QITHGKADAD ALVVSASAGK DFELRLPVDA
     RQQTTTTGES ADPVTTTVEN YGGETQTQRR HHTDVAFVLD RFVKVQVSGN QHTLDVMQVH
     KDSIVGALLR AATYYFSDLE IAVTHTGKLT WVPNGAPVSA LDNTTNPTAY HKGPLTRLAL
     PYTAPHRVLA TAYTGTTAYT TGVRRGDLAH LAAAHARHLP TSFNFGAVKA ETITELLVRM
     KRAELYCPRP VLPVQPAGDR HKQPLIAPAK QLLNFDLLKL AGDVESNPGP FFFSDVRSNF
     SKLVETINQM QEDMSTKHGP DFNRLVSAFE ELATGVKAIR TGLDEAKPWY KLIKLLSRLS
     CMAAVAARSK DPVLVAIMLA DTGLEILDST FVVKKISDSL SSLFHVPAPV FSFGAPILLA
     GLVKVASSFF RSTPEDLERA EKQLKARDIN DIFAILKNGE WLVKLILAIR DWIKAWIASE
     EKFVTMTDLV PGILEKQRDL NDPSKYKEAK EWLDNARQAC LKNGNTHIAN LCKVVAPAPS
     KSRPEPVVVC LRGKSGQGKS FLANVLAQAI STHFTGRTDS VWYCPPDPDH FDGYNQQTVV
     VMDDLGQNPD GKDFKYFAQM VSTTGFIPPM ASLEDKGKPF NSKVIIATTN LYSGFTPRTM
     VCPDALNRRF HFDIDVSAKD GYKINNKLDI IKALEDTHTN PVAMFQYDCA LLNGMAVEMK
     RMQQDMFKPQ PPLQNVYQLV QEVIERVELH EKVSSHPIFK QISIPSQKSV LYFLIEKGQH
     EAAIEFFEGM VHDSIKEELR PLIQQTSFVK RAFKRLKENF EIVALCLTLL ANIVIMIRET
     RKRQQMVDDA VNEYIEKANI TTDDKTLDEA EKNPLETSGA STVGFRERTL PGHKARDDVN
     SEPAQPVEEQ PQAEGPYAGP LERQKPLKVR AKLPQQEGPY AGPMERQKPL KVKAKAPVVK
     EGPYEGPVKK PVALKVKAKN LIVTESGAPP TDLQKMVMGN TKPVELILDG KTVAICCATG
     VFGTAYLVPR HLFAEKYDKI MLDGRAMTDS DYRVFEFEIK VKGQDMLSDA ALMVLHRGNR
     VRDITKHFRD TARMKKGTPV VGVINNADVG RLIFSGEALT YKDIVVCMDG DTMPGLFAYR
     AATKAGYCGG AVLAKDGADT FIVGTHSAGG NGVGYCSCVS RSMLLKMKAH IDPEPHHEGL
     IVDTRDVEER VHVMRKTKLA PTVAHGVFNP DFGPAALSNR DPRLNEGVVL DEVIFSKHKG
     DTKMSEEDKA LFRRCAADYA SRLHSVLGTA NAPLSIYEAI KGVDGLDAME PDTAPGLPWA
     LQGKRRGALI DFENGTVGPE VEAALKLMEK REYKFACQTF LKDEIRPMEK VRAGKTRIVD
     VLPVEHILYT RMMIGRFCAQ MHSNNGPQIG SAVGCNPDVD WQRFGTHFAQ YRNVWDVDYS
     AFDANHCSDA MNIMFEEVFR TEFGFHPNAE WILKTLVNTE HAYENKRITV EGGMPSGCSA
     TSIINTILNN IYVLYALRRH YEGVELDTYT MISYGDDIVV ASDYDLDFEA LKPHFKSIGQ
     TITPADKSDK GFVLGHSITD VTFLKRHFHM DYGTGFYKPV MASKTLEAIL SFARRGTIQE
     KLISVAGLAV HSGPDEYRRL FEPFQGLFEI PSYRSLYLRW VNAVCGDA
//