POLG_FMDVT
ID POLG_FMDVT Reviewed; 2327 AA.
AC P15072; Q6PMY1; Q84755; Q84756; Q84757; Q84758;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 167.
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 -/Germany/C1Oberbayen/1960 serotype
OS C) (FMDV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Aphthovirus.
OX NCBI_TaxID=12121;
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 1-1011.
RX PubMed=6316275; DOI=10.1093/nar/11.22.7873;
RA Beck E., Forss S., Strebel K., Cattaneo R., Feil G.;
RT "Structure of the FMDV translation initiation site and of the structural
RT proteins.";
RL Nucleic Acids Res. 11:7873-7885(1983).
RN [3]
RP ALTERNATIVE INITIATION.
RX PubMed=3033601; DOI=10.1093/nar/15.8.3305;
RA Sangar D.V., Newton S.E., Rowlands D.J., Clarke B.E.;
RT "All foot and mouth disease virus serotypes initiate protein synthesis at
RT two separate AUGs.";
RL Nucleic Acids Res. 15:3305-3315(1987).
RN [4] {ECO:0007744|PDB:1FMD}
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 287-504 AND 505-723.
RX PubMed=8081743; DOI=10.1016/s0969-2126(00)00014-9;
RA Lea S., Hernandez J., Blakemore W., Brocchi E., Curry S., Domingo E.,
RA Fry E., Abu-Ghazaleh R., King A., Newman J.;
RT "The structure and antigenicity of a type C foot-and-mouth disease virus.";
RL Structure 2:123-139(1994).
RN [5] {ECO:0007744|PDB:1EJO}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 859-873.
RX PubMed=10811933; DOI=10.1099/0022-1317-81-6-1495;
RA Ochoa W.F., Kalko S.G., Mateu M.G., Gomes P., Andreu D., Domingo E.,
RA Fita I., Verdaguer N.;
RT "A multiply substituted G-H loop from foot-and-mouth disease virus in
RT complex with a neutralizing antibody: a role for water molecules.";
RL J. Gen. Virol. 81:1495-1505(2000).
CC -!- FUNCTION: [Leader protease]: Autocatalytically cleaves itself from the
CC polyprotein at the L/VP0 junction. Cleaves also the host translation
CC initiation factors EIF4G1 and EIF4G3, in order to shutoff 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 DDX58,
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 mofidier that can no
CC longer be attached to target proteins. Cleaves also 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. {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 + 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=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=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 VP2]: Virion. Host cytoplasm
CC {ECO:0000305}.
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: [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=P15072-1; Sequence=Displayed;
CC Name=Lb;
CC IsoId=P15072-2; Sequence=VSP_018983;
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 -!- 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 -!- 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 -!- 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=1fmd";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure in complex with a fab fragment of a neutralizing antibody;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1qgc";
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DR EMBL; AY593805; AAT01748.1; -; Genomic_RNA.
DR EMBL; X00130; CAA24960.2; -; Genomic_RNA.
DR PIR; A20288; GNNYC1.
DR PDB; 1EJO; X-ray; 2.30 A; P=859-873.
DR PDB; 1FMD; X-ray; 3.50 A; 2=287-504, 3=505-723.
DR PDB; 1QGC; EM; 30.00 A; 2=287-504, 3=505-723.
DR PDBsum; 1EJO; -.
DR PDBsum; 1FMD; -.
DR PDBsum; 1QGC; -.
DR SMR; P15072; -.
DR MEROPS; C03.008; -.
DR MEROPS; C28.001; -.
DR ABCD; P15072; 1 sequenced antibody.
DR EvolutionaryTrace; P15072; -.
DR Proteomes; UP000012671; Genome.
DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; 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:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:RHEA.
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-directed 5'-3' 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: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:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0039690; P:positive stranded viral RNA replication; ISS:UniProtKB.
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:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
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 CDD; cd00205; rhv_like; 3.
DR Gene3D; 2.40.10.10; -; 2.
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; 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; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF56672; SSF56672; 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 1: Evidence at protein level;
KW 3D-structure; 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..2327
FT /note="Genome polyprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000039891"
FT CHAIN 1..201
FT /note="Leader protease"
FT /id="PRO_0000039892"
FT CHAIN 202..504
FT /note="Capsid protein VP0"
FT /evidence="ECO:0000255"
FT /id="PRO_0000374077"
FT CHAIN 202..286
FT /note="Capsid protein VP4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039895"
FT CHAIN 287..504
FT /note="Capsid protein VP2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039896"
FT CHAIN 505..723
FT /note="Capsid protein VP3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039897"
FT CHAIN 724..930
FT /note="Capsid protein VP1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039898"
FT CHAIN 931..948
FT /note="Protein 2A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039899"
FT CHAIN 949..1102
FT /note="Protein 2B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000310980"
FT CHAIN 1103..1420
FT /note="Protein 2C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000422519"
FT CHAIN 1421..1573
FT /note="Protein 3A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000422520"
FT CHAIN 1574..1596
FT /note="Protein 3B-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000422521"
FT CHAIN 1597..1620
FT /note="Protein 3B-2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000422522"
FT CHAIN 1621..1644
FT /note="Protein 3B-3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000422523"
FT CHAIN 1645..1857
FT /note="Protease 3C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000422524"
FT CHAIN 1858..2327
FT /note="RNA-directed RNA polymerase 3D-POL"
FT /evidence="ECO:0000255"
FT /id="PRO_0000422525"
FT TOPO_DOM 1..1475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1476..1496
FT /evidence="ECO:0000255"
FT TOPO_DOM 1497..2327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..201
FT /note="Peptidase C28"
FT DOMAIN 1184..1348
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1647..1843
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 2091..2209
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 1524..1579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 864..866
FT /note="Cell attachment site"
FT COMPBIAS 200..218
FT /note="Polar 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 1690
FT /note="For protease 3C activity; Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1728
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1807
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 2195
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT BINDING 1212..1219
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 930..931
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000255"
FT SITE 948..949
FT /note="Cleavage; by ribosomal skip"
FT /evidence="ECO:0000255"
FT SITE 1102..1103
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000255"
FT SITE 1420..1421
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000255"
FT SITE 1573..1574
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000255"
FT SITE 1596..1597
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000255"
FT SITE 1620..1621
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000255"
FT SITE 1644..1645
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000255"
FT SITE 1857..1858
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000255"
FT MOD_RES 1576
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 1599
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 1623
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_018983"
FT VARIANT 8
FT /note="I -> T"
FT VARIANT 48
FT /note="H -> Q"
FT VARIANT 307
FT /note="H -> Q"
FT VARIANT 408..409
FT /note="LV -> QA"
FT VARIANT 726
FT /note="A -> T"
FT VARIANT 852
FT /note="A -> G"
FT VARIANT 867
FT /note="S -> L"
FT VARIANT 876
FT /note="R -> G"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:1FMD"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:1FMD"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 364..372
FT /evidence="ECO:0007829|PDB:1FMD"
FT HELIX 375..383
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 384..398
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 404..413
FT /evidence="ECO:0007829|PDB:1FMD"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 429..434
FT /evidence="ECO:0007829|PDB:1FMD"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 440..446
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 450..455
FT /evidence="ECO:0007829|PDB:1FMD"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 463..474
FT /evidence="ECO:0007829|PDB:1FMD"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 483..499
FT /evidence="ECO:0007829|PDB:1FMD"
FT HELIX 548..554
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 571..574
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 576..581
FT /evidence="ECO:0007829|PDB:1FMD"
FT TURN 587..591
FT /evidence="ECO:0007829|PDB:1FMD"
FT HELIX 593..598
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 601..605
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 608..614
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 621..629
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 631..633
FT /evidence="ECO:0007829|PDB:1FMD"
FT HELIX 639..642
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 645..651
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 659..662
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 667..669
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 671..674
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 686..696
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 701..708
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 713..717
FT /evidence="ECO:0007829|PDB:1FMD"
FT STRAND 863..865
FT /evidence="ECO:0007829|PDB:1EJO"
SQ SEQUENCE 2327 AA; 258119 MW; A81AB150E79617DD CRC64;
MNTTDCFIAV VNAIREIRAL FLPRTTGKME FTLHDGEKKV FYSRPNNHDN CWLNTILQLF
RYVDEPFFDW VYNSPENLTL EAIKQLEELT GLELREGGPP ALVIWNIKHL LHTGIGTASR
PSEVCMVDGT DMCLADFHAG IFMKGQEHAV FACVTSNGWY AIDDEDFYPW TPDPSDVLVF
VPYDQEPLNE GWKANVQRKL KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG
DNAISGGSNE GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI
LTTRNGHTTS TTQSSVGVTF GYATAEDSTS GPNTSGLETR VHQAERFFKM ALFDWVPSQN
FGHMHKVVLP HEPKGVYGGL VKSYAYMRNG WDVEVTAVGN QFNGGCLLVA LVPEMGDISD
REKYQLTLYP HQFINPRTNM TAHITVPYVG VNRYDQYKQH RPWTLVVMVV APLTTNTAGA
QQIKVYANIA PTNVHVAGEL PSKEGIFPVA CSDGYGNMVT TDPKTADPAY GKVYNPPRTA
LPGRFTNYLD VAEACPTFLM FENVPYVSTR TDGQRLLAKF DVSLAAKHMS NTYLAGLAQY
YTQYTGTINL HFMFTGPTDA KARYMVAYVP PGMDAPDNPE EAAHCIHAEW DTGLNSKFTF
SIPYISAADY AYTASHEAET TCVQGWVCVY QITHGKADAD ALVVSASAGK DFELRLPVDA
RQQTTATGES ADPVTTTVEN YGGETQVQRR HHTDVAFVLD RFVKVTVSGN QHTLDVMQAH
KDNIVGALLR AATYYFSDLE IAVTHTGKLT WVPNGAPVSA LDNTTNPTAY HKGPLTRLAL
PYTAPHRVLA TAYTGTTTYT ASTRGDSAHL TATRARHLPT SFNFGAVKAE TITELLVRMK
RAELYCPRPI LPIQPTGDRH KQPLVAPAKQ LLNFDLLKLA GDVESNPGPF FFSDVRSNFS
KLVETINQMQ EDMSTKHGPD FNRLVSAFEE LASGVKAIRT GLDEAKPWYK LIKLLSRLSC
MAAVAARSKD PVLVAIMLAD TGLEILDSTF VVKKISDSLS SLFHVPAPAF SFGAPILLAG
LVKVASSFFR STPEDLERAE KQLKARDIND IFAILKNGEW LVKLILAIRD WIKAWIASEE
KFVTMTDLVP GILEKQRDLN DPSKYKDAKE WLDNTRQACL KSGNVHIANL CKVVAPAPSK
SRPEPVVVCL RGKSGQGKSF LANVLAQAIS THLTGRTDSV WYCPPDPDHF DGYNQQTVVV
MDDLGQNPDG KDFKYFAQMV STTGFIPPMA SLEDKGKPFS SKVIIATTNL YSGFTPKTMV
CPDALNRRFH FDIDVSAKDG YKINNKLDII KALEDTHTNP VAMFQYDCAL LNGMAVEMKR
LQQDMFKPQP PLQNVYQLVQ EVIERVELHE KVSSHPIFKQ ISIPSQKSVL YFLIEKGQHE
AAIEFFEGMV HDSIKEELRP LIQQTSFVKR AFKRLKENFE IVALCLTLLA NIVIMIRETH
KRQKMVDDAV NEYIEKANIT TDDKTLDEAE KNPLETSGAS TVGFRERTLP GQKARDDVNS
EPAQPTEEQP QAEGPYAGPL ERQRPLKVRA KLPQQEGPYA GPMERQKPLK VKARAPVVKE
GPYEGPVKKP VALKVKAKNL IVTESGAPPT DLQKMVMGNT KPVELILDGK TVAICCATGV
FGTAYLVPRH LFAEKYDKIM LDGRALTDSD YRVFEFEIKV KGQDMLSDAA LMVLHRGNRV
RDITKHFRDV ARMKKGTPVV GVINNADVGR LIFSGEALTY KDIVVCMDGD TMPGLFAYKA
ATKAGYCGGA VLAKDGADTF IVGTHSAGGN GVGYCSCVSR SMLLKMKAHI DPEPHHEGLI
VDTRDVEERV HVMRKTKLAP TVAHGVFNPE FGPAALSNKD PRLNEGVVLD EVIFSKHKGD
TKMSEEDKAL FRRCAADYAS RLHSVLGTAN APLSIYEAIK GVDGLDAMEP DTAPGLPWAL
QGKRRGALID FENGTVGPEV EAALKLMEKR EYKFACQTFL KDEIRPMEKV RAGKTRIVDV
LPVEHILYTR MMIGRFCAQM HSNNGPQIGS AVGCNPDVDW QRFGTHFAQY RNVWDVDYSA
FDANHCSDAM NIMFEEVFRT EFGFHPNAEW ILKTLVNTEH AYENKRITVE GGMPSGCSAT
SIINTILNNI YVLYALRRHY EGVELDTYTM ISYGDDIVVA SDYDLDFEAL KPHFKSLGQT
ITPADKSDKG FVLGHSITDV TFLKRHFHMD YGTGFYKPVM ASKTLEAILS FARRGTIQEK
LISVAGLAVH SGPDEYRRLF EPFQGLFEIP SYRSLYLRWV NAVCGDA
