[1]
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NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate O1k;
DOI=10.1093/nar/12.16.6587; PubMed=6089122 [NCBI, ExPASy, EBI, Israel, Japan]
Forss S.,
Strebel K.,
Beck E.,
Schaller H.;
"Nucleotide sequence and genome organization of foot-and-mouth disease virus.";
Nucleic Acids Res. 12:6587-6601(1984).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate O1BFS;
DOI=10.1093/nar/10.24.8285; PubMed=6298715 [NCBI, ExPASy, EBI, Israel, Japan]
Makoff A.J.,
Paynter C.A.,
Rowlands D.J.,
Boothroyd J.C.;
"Comparison of the amino acid sequence of the major immunogen from three serotypes of foot and mouth disease virus.";
Nucleic Acids Res. 10:8285-8295(1982).
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[3]
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CHARACTERIZATION.
DOI=10.1021/bi049340d; PubMed=15350134 [NCBI, ExPASy, EBI, Israel, Japan]
Kuehnel E.,
Cencic R.,
Foeger N.,
Skern T.;
"Foot-and-mouth disease virus leader proteinase: specificity at the P2 and P3 positions and comparison with other papain-like enzymes.";
Biochemistry 43:11482-11490(2004).
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[4]
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ALTERNATIVE INITIATION.
DOI=10.1093/nar/15.8.3305; PubMed=3033601 [NCBI, ExPASy, EBI, Israel, Japan]
Sangar D.V.,
Newton S.E.,
Rowlands D.J.,
Clarke B.E.;
"All foot and mouth disease virus serotypes initiate protein synthesis at two separate AUGs.";
Nucleic Acids Res. 15:3305-3315(1987).
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[5]
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FUNCTION OF THE LEADER PROTEASE.
DOI=10.1006/viro.1993.1267; PubMed=8386879 [NCBI, ExPASy, EBI, Israel, Japan]
Medina M.,
Domingo E.,
Brangwyn J.K.,
Belsham G.J.;
"The two species of the foot-and-mouth disease virus leader protein, expressed individually, exhibit the same activities.";
Virology 194:355-359(1993).
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[6]
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FUNCTION OF THE LEADER PROTEASE, AND CLEAVAGE OF HOST EIF4G1.
STRAIN=Isolate O1k;
DOI=10.1016/S0014-5793(00)01928-1; PubMed=11034318 [NCBI, ExPASy, EBI, Israel, Japan]
Glaser W.,
Skern T.;
"Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A in vitro.";
FEBS Lett. 480:151-155(2000).
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[7]
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POLYPROTEIN PROCESSING.
PubMed=11297676 [NCBI, ExPASy, EBI, Israel, Japan]
Donnelly M.L.L.,
Luke G.,
Mehrotra A.,
Li X.,
Hughes L.E.,
Gani D.,
Ryan M.D.;
"Analysis of the aphthovirus 2A/2B polyprotein 'cleavage' mechanism indicates not a proteolytic reaction, but a novel translational effect: a putative ribosomal 'skip'.";
J. Gen. Virol. 82:1013-1025(2001).
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[8]
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FUNCTION OF THE LEADER PROTEASE, AND CLEAVAGE OF HOST EIF4G3.
DOI=10.1128/JVI.78.7.3271-3278.2004; PubMed=15016848 [NCBI, ExPASy, EBI, Israel, Japan]
Gradi A.,
Foeger N.,
Strong R.,
Svitkin Y.V.,
Sonenberg N.,
Skern T.,
Belsham G.J.;
"Cleavage of eukaryotic translation initiation factor 4GII within foot-and-mouth disease virus-infected cells: identification of the L-protease cleavage site in vitro.";
J. Virol. 78:3271-3278(2004).
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[9]
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X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
DOI=10.1038/337709a0; PubMed=2537470 [NCBI, ExPASy, EBI, Israel, Japan]
Acharya R.,
Fry E.,
Stuart D.,
Fox G.,
Rowlands D.,
Brown F.;
"The three-dimensional structure of foot-and-mouth disease virus at 2.9-A resolution.";
Nature 337:709-716(1989).
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[10]
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X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 29-201 OF MUTANT ALA-51.
DOI=10.1093/emboj/17.24.7469; PubMed=9857201 [NCBI, ExPASy, EBI, Israel, Japan]
Guarne A.,
Tormo J.,
Kirchweger R.,
Pfistermueller D.,
Fita I.,
Skern T.;
"Structure of the foot-and-mouth disease virus leader protease: a papain-like fold adapted for self-processing and eIF4G recognition.";
EMBO J. 17:7469-7479(1998).
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[11]
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X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-195 OF MUTANT ALA-51/SER-133.
DOI=10.1006/jmbi.2000.4115; PubMed=11183785 [NCBI, ExPASy, EBI, Israel, Japan]
Guarne A.,
Hampoelz B.,
Glaser W.,
Carpena X.,
Tormo J.,
Fita I.,
Skern T.;
"Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes.";
J. Mol. Biol. 302:1227-1240(2000).
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- FUNCTION: The leader protease autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. It also cleaves the host translation initiation factor EIF4G1 and EIF4G3, in order to shut down the capped cellular mRNA transcription.
- FUNCTION: Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (By similarity).
- FUNCTION: VP0 precursor is a component of immature procapsids (By similarity).
- FUNCTION: Protein 2B affects membrane integrity and cause an increase in membrane permeability (By similarity).
- FUNCTION: Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).
- FUNCTION: Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity).
- FUNCTION: Protein 3B-1, 3B-2 and 3B-3 are covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. They acts as a genome-linked replication primer (By similarity).
- FUNCTION: Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).
- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).
- CATALYTIC ACTIVITY: Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.
- CATALYTIC ACTIVITY: NTP + H2O = NDP + phosphate.
- CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
- SUBCELLULAR LOCATION: Protein VP2: Virion. Cytoplasm (Potential).
- SUBCELLULAR LOCATION: Protein VP3: Virion. Cytoplasm (Potential).
- SUBCELLULAR LOCATION: Protein VP1: Virion. Cytoplasm (Potential).
- SUBCELLULAR LOCATION: Protein 2B: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
- SUBCELLULAR LOCATION: Protein 2C: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
- SUBCELLULAR LOCATION: Protein 3A: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
- SUBCELLULAR LOCATION: Protein 3B-1: Virion (Potential).
- SUBCELLULAR LOCATION: Protein 3B-2: Virion (Potential).
- SUBCELLULAR LOCATION: Protein 3B-3: Virion (Potential).
- SUBCELLULAR LOCATION: Picornain 3C: Cytoplasm (Potential).
- SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
- ALTERNATIVE PRODUCTS:
2 named isoforms [FASTA] produced by alternative initiation.
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| Name | Lb |
| Isoform ID | P03305-2 |
| Features which should be applied to build the isoform sequence: VSP_018982. |
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- PTM: Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle. The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip from one codon to the next without formation of a peptide bond. This process would release the L-P1-2A peptide from the translational complex (By similarity).
- PTM: Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle (By similarity).
- PTM: VPg is covalently linked to the genomic RNA (By similarity).
- MISCELLANEOUS: The strain O1K sequence is shown.
- MISCELLANEOUS: The Capsid protein VP1 contains the main antigenic determinants of the virion; therefore, changes in its sequence must be responsible for the high antigenic variability of the virus.
- SIMILARITY: Belongs to the picornaviruses polyprotein family.
- SIMILARITY: Contains 1 peptidase C28 domain [view classification].
- SIMILARITY: Contains 1 peptidase C3 domain [view classification].
- SIMILARITY: Contains 1 RdRp catalytic domain.
- SIMILARITY: Contains 1 SF3 helicase domain.
- WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure; URL="http://viperdb.scripps.edu/info_page.php?VDB=1bbt";.
- WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure; URL="http://viperdb.scripps.edu/info_page.php?VDB=1fod";.
- WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure complexed with oligosaccharide receptor; URL="http://viperdb.scripps.edu/info_page.php?VDB=1qqp";.
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