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 POLG_FMDVO              Reviewed;        2332 AA.
P03305;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
22-NOV-2017, entry version 177.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Leader protease;
Short=Lpro;
EC=3.4.22.46;
Contains:
RecName: Full=Protein VP0;
AltName: Full=VP4-VP2;
Contains:
RecName: Full=Protein VP4;
AltName: Full=P1A;
AltName: Full=Virion protein 4;
Contains:
RecName: Full=Protein VP2;
AltName: Full=P1B;
AltName: Full=Virion protein 2;
Contains:
RecName: Full=Protein VP3;
AltName: Full=P1C;
AltName: Full=Virion protein 3;
Contains:
RecName: Full=Protein VP1;
AltName: Full=P1D;
AltName: Full=Virion protein 1;
Contains:
RecName: Full=Protein 2A;
Short=P2A;
AltName: Full=P52;
Contains:
RecName: Full=Protein 2B;
Short=P2B;
Contains:
RecName: Full=Protein 2C;
Short=P2C;
EC=3.6.1.15;
Contains:
RecName: Full=Protein 3A;
Short=P3A;
Contains:
RecName: Full=Protein 3B-1;
Short=P3B-1;
AltName: Full=Genome-linked protein VPg1;
Contains:
RecName: Full=Protein 3B-2;
Short=P3B-2;
AltName: Full=Genome-linked protein VPg2;
Contains:
RecName: Full=Protein 3B-3;
Short=P3B-3;
AltName: Full=Genome-linked protein VPg3;
Contains:
RecName: Full=Picornain 3C;
EC=3.4.22.28;
AltName: Full=Protease 3C;
Short=P3C;
AltName: Full=Protease P20B;
Contains:
RecName: Full=RNA-directed RNA polymerase 3D-POL;
Short=P3D-POL;
EC=2.7.7.48;
AltName: Full=P56A;
Foot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/1966
serotype O) (FMDV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Aphthovirus.
NCBI_TaxID=73482;
NCBI_TaxID=9913; Bos taurus (Bovine).
NCBI_TaxID=9925; Capra hircus (Goat).
NCBI_TaxID=9850; Cervidae (deer).
NCBI_TaxID=9363; Erinaceidae (hedgehogs).
NCBI_TaxID=9785; Loxodonta africana (African elephant).
NCBI_TaxID=9940; Ovis aries (Sheep).
NCBI_TaxID=10116; Rattus norvegicus (Rat).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6089122; DOI=10.1093/nar/12.16.6587;
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).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate O1BFS/Britain/1968;
PubMed=6298715; DOI=10.1093/nar/10.24.8285;
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).
[3]
CHARACTERIZATION.
PubMed=15350134; DOI=10.1021/bi049340d;
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).
[4]
ALTERNATIVE INITIATION.
PubMed=3033601; DOI=10.1093/nar/15.8.3305;
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).
[5]
FUNCTION OF THE LEADER PROTEASE.
PubMed=8386879; DOI=10.1006/viro.1993.1267;
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).
[6]
FUNCTION OF THE LEADER PROTEASE, AND CLEAVAGE OF HOST EIF4G1.
STRAIN=Isolate O1k;
PubMed=11034318; DOI=10.1016/S0014-5793(00)01928-1;
Glaser W., Skern T.;
"Extremely efficient cleavage of eIF4G by picornaviral proteinases L
and 2A in vitro.";
FEBS Lett. 480:151-155(2000).
[7]
POLYPROTEIN PROCESSING.
PubMed=11297676;
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).
[8]
FUNCTION OF THE LEADER PROTEASE, AND CLEAVAGE OF HOST EIF4G3.
PubMed=15016848; DOI=10.1128/JVI.78.7.3271-3278.2004;
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).
[9]
COVALENT RNA LINKAGE OF 3B PROTEINS, AND URIDYLYLATION.
PubMed=15919922; DOI=10.1128/JVI.79.12.7698-7706.2005;
Nayak A., Goodfellow I.G., Belsham G.J.;
"Factors required for the uridylylation of the foot-and-mouth disease
virus 3B1, 3B2, and 3B3 peptides by the RNA-dependent RNA polymerase
(3Dpol) in vitro.";
J. Virol. 79:7698-7706(2005).
[10]
FUNCTION OF CAPSID PROTEINS.
PubMed=18614639; DOI=10.1128/JVI.00732-08;
O'Donnell V., Larocco M., Baxt B.;
"Heparan sulfate-binding foot-and-mouth disease virus enters cells via
caveola-mediated endocytosis.";
J. Virol. 82:9075-9085(2008).
[11]
REVIEW.
PubMed=19556802; DOI=10.1159/000226121;
Ruiz-Saenz J., Goez Y., Tabares W., Lopez-Herrera A.;
"Cellular receptors for foot and mouth disease virus.";
Intervirology 52:201-212(2009).
[12]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
PubMed=2537470; DOI=10.1038/337709a0;
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).
[13]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 29-201 OF MUTANT ALA-51.
PubMed=9857201; DOI=10.1093/emboj/17.24.7469;
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).
[14]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-195 OF MUTANT
ALA-51/SER-133.
PubMed=11183785; DOI=10.1006/jmbi.2000.4115;
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).
-!- 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. Increases
translation driven by the viral internal ribosome entry site
(IRES) (By similarity). {ECO:0000250|UniProtKB:P03311,
ECO:0000269|PubMed:11034318, ECO:0000269|PubMed:15016848,
ECO:0000269|PubMed:8386879}.
-!- 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. The capsid interacts with host heparan sulfate and
various integrins (alphavbeta6, alphavbeta1, alphavbeta3,
alpha5beta1, alphavbeta8) to provide virion attachment to target
Attachment via host integrins induces virion internalization
predominantly through clathrin-mediated endocytosis. In strains
adapted to cell culture, attachment to heparan sulfate can also be
used and induces virion internalization through clathrin- and
caveolin-independent endocytosis.
-!- FUNCTION: Protein VP0: VP0 precursor is a component of immature
procapsids. {ECO:0000250}.
-!- FUNCTION: Protein 2B: Affects membrane integrity and cause an
increase in membrane permeability. {ECO:0000250}.
-!- FUNCTION: Protein 2C: Associates with and induces structural
rearrangements of intracellular membranes. It displays RNA-
binding, nucleotide binding and NTPase activities (By similarity).
{ECO:0000250}.
-!- FUNCTION: Protein 3A, via its hydrophobic domain, serves as
membrane anchor. {ECO:0000250}.
-!- 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). {ECO:0000250}.
-!- FUNCTION: Protease 3C: 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 cooperatively to
the protease (By similarity). {ECO:0000250}.
-!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic
and antigenomic RNA by recognizing replications specific signals.
{ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- 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 + H(2)O = 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). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- SUBUNIT: VP1 interacts (via RGD) with integrins heterodimers
alphavbeta6, alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta8.
-!- SUBCELLULAR LOCATION: Protein VP2: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP3: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP1: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 2B: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. 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). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 2C: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. 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). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3A: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. 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). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3B-1: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 3B-2: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 3B-3: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Picornain 3C: Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Host
cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane
protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
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). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Lab;
IsoId=P03305-1; Sequence=Displayed;
Name=Lb;
IsoId=P03305-2; Sequence=VSP_018982;
-!- 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).
{ECO:0000250}.
-!- PTM: Myristoylation of VP4 is required during RNA encapsidation
and formation of the mature virus particle. {ECO:0000250}.
-!- PTM: Protein 3B-1, 3B-2 and 3B-3 are uridylylated by the
polymerase and are covalently linked to the 5'-end of genomic RNA.
These uridylylated forms act as a nucleotide-peptide primer for
the polymerase (By similarity). {ECO:0000250}.
-!- 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.
{ECO:0000305}.
-!- 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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EMBL; X00871; CAA25416.1; -; Genomic_RNA.
EMBL; J02185; AAA42635.1; -; Genomic_RNA.
PDB; 1QMY; X-ray; 1.90 A; A/B/C=29-195.
PDB; 1QOL; X-ray; 3.00 A; A/B/C/D/E/F/G/H=29-201.
PDB; 1QQP; X-ray; 1.90 A; 1=725-937, 2=287-504, 3=505-724, 4=202-286.
PDB; 2JQF; NMR; -; R/S=29-201.
PDB; 2JQG; NMR; -; R=29-195.
PDB; 4QBB; X-ray; 1.60 A; A/B/C=29-195.
PDBsum; 1QMY; -.
PDBsum; 1QOL; -.
PDBsum; 1QQP; -.
PDBsum; 2JQF; -.
PDBsum; 2JQG; -.
PDBsum; 4QBB; -.
DisProt; DP00573; -.
ProteinModelPortal; P03305; -.
SMR; P03305; -.
ELM; P03305; -.
MEROPS; C03.008; -.
KEGG; ag:CAA25416; -.
OrthoDB; VOG090000RV; -.
BRENDA; 3.4.22.46; 2315.
EvolutionaryTrace; P03305; -.
Proteomes; UP000008765; Genome.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0019030; C:icosahedral viral capsid; IEA:InterPro.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IDA:UniProtKB.
GO; GO:0039525; P:modulation by virus of host chromatin organization; IEA:UniProtKB-KW.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0039690; P:positive stranded viral RNA replication; ISS:UniProtKB.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd00205; rhv_like; 3.
Gene3D; 4.10.90.10; -; 1.
InterPro; IPR015031; Capsid_VP4_Picornavir.
InterPro; IPR037080; Capsid_VP4_sf_Picornavirus.
InterPro; IPR004080; FMDV_VP1_coat.
InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008739; Peptidase_C28.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001676; Picornavirus_capsid.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
Pfam; PF05408; Peptidase_C28; 1.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00073; Rhv; 3.
Pfam; PF00910; RNA_helicase; 1.
Pfam; PF08935; VP4_2; 1.
PRINTS; PR00918; CALICVIRUSNS.
PRINTS; PR01542; FMDVP1COAT.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; ATP-binding; Capsid protein;
Clathrin- and caveolin-independent endocytosis of virus by host;
Clathrin-mediated endocytosis of virus by host; Complete proteome;
Covalent protein-RNA linkage; Disulfide bond; Helicase;
Host cytoplasm; Host cytoplasmic vesicle; Host membrane;
Host-virus interaction; Hydrolase; Ion channel; Ion transport;
Lipoprotein; Membrane; Modulation of host chromatin by virus;
Myristate; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
Protease; RNA-binding; RNA-directed RNA polymerase; Thiol protease;
Transferase; Translation regulation; Transport;
Viral attachment to host cell; Viral ion channel;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus endocytosis by host; Virus entry into host cell.
CHAIN 1 2332 Genome polyprotein.
/FTId=PRO_0000039872.
CHAIN 1 201 Leader protease.
/FTId=PRO_0000039873.
CHAIN 202 504 Protein VP0. {ECO:0000255}.
/FTId=PRO_0000374076.
CHAIN 202 286 Protein VP4. {ECO:0000255}.
/FTId=PRO_0000039876.
CHAIN 287 504 Protein VP2. {ECO:0000255}.
/FTId=PRO_0000039877.
CHAIN 505 724 Protein VP3. {ECO:0000255}.
/FTId=PRO_0000039878.
CHAIN 725 935 Protein VP1.
/FTId=PRO_0000039879.
CHAIN 936 953 Protein 2A. {ECO:0000255}.
/FTId=PRO_0000039880.
CHAIN 954 1107 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000310976.
CHAIN 1108 1425 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000039881.
CHAIN 1426 1578 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000039882.
CHAIN 1579 1601 Protein 3B-1. {ECO:0000255}.
/FTId=PRO_0000039883.
CHAIN 1602 1625 Protein 3B-2. {ECO:0000255}.
/FTId=PRO_0000310977.
CHAIN 1626 1649 Protein 3B-3. {ECO:0000255}.
/FTId=PRO_0000310978.
CHAIN 1650 1862 Picornain 3C. {ECO:0000255}.
/FTId=PRO_0000039884.
CHAIN 1863 2332 RNA-directed RNA polymerase 3D-POL.
{ECO:0000255}.
/FTId=PRO_0000039885.
TOPO_DOM 1 1480 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1481 1501 {ECO:0000255}.
TOPO_DOM 1502 2332 Cytoplasmic. {ECO:0000255}.
DOMAIN 1 201 Peptidase C28.
DOMAIN 1189 1353 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1652 1836 Peptidase C3.
DOMAIN 2096 2214 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1217 1224 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
MOTIF 869 871 Cell attachment site. {ECO:0000250}.
ACT_SITE 51 51 For leader protease activity.
ACT_SITE 148 148 For leader protease activity.
ACT_SITE 163 163 For leader protease activity.
ACT_SITE 1695 1695 For picornain 3C activity; Proton
donor/acceptor.
{ECO:0000250|UniProtKB:P03306,
ECO:0000255}.
ACT_SITE 1733 1733 For picornain 3C activity.
{ECO:0000250|UniProtKB:P03306}.
ACT_SITE 1812 1812 For picornain 3C activity.
{ECO:0000250|UniProtKB:P03306,
ECO:0000255}.
SITE 201 202 Cleavage; by leader protease.
{ECO:0000255}.
SITE 286 287 Cleavage. {ECO:0000255}.
SITE 504 505 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 724 725 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 935 936 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 953 954 Cleavage; by ribosomal skip.
{ECO:0000255}.
SITE 1107 1108 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1425 1426 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1578 1579 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1601 1602 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1625 1626 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1649 1650 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1862 1863 Cleavage; by picornain 3C. {ECO:0000255}.
MOD_RES 1581 1581 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
MOD_RES 1604 1604 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
MOD_RES 1628 1628 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
LIPID 202 202 N-myristoyl glycine; by host.
{ECO:0000250}.
DISULFID 406 858 Interchain (between VP2 and VP1 chains).
DISULFID 511 511 Interchain; in VP3 dimer.
VAR_SEQ 1 28 Missing (in isoform Lb). {ECO:0000305}.
/FTId=VSP_018982.
VARIANT 780 780 I -> V (in strain: Isolate O1BFS).
VARIANT 808 808 G -> R (in strain: Isolate O1BFS).
VARIANT 861 861 N -> S (in strain: Isolate O1BFS).
STRAND 30 32 {ECO:0000244|PDB:4QBB}.
STRAND 38 40 {ECO:0000244|PDB:4QBB}.
STRAND 47 49 {ECO:0000244|PDB:4QBB}.
HELIX 51 63 {ECO:0000244|PDB:4QBB}.
HELIX 66 68 {ECO:0000244|PDB:1QOL}.
HELIX 69 72 {ECO:0000244|PDB:4QBB}.
STRAND 73 76 {ECO:0000244|PDB:2JQG}.
HELIX 79 90 {ECO:0000244|PDB:4QBB}.
HELIX 100 106 {ECO:0000244|PDB:4QBB}.
HELIX 107 110 {ECO:0000244|PDB:4QBB}.
STRAND 111 113 {ECO:0000244|PDB:2JQF}.
STRAND 115 120 {ECO:0000244|PDB:4QBB}.
STRAND 123 125 {ECO:0000244|PDB:4QBB}.
STRAND 129 131 {ECO:0000244|PDB:2JQG}.
HELIX 134 136 {ECO:0000244|PDB:4QBB}.
STRAND 137 145 {ECO:0000244|PDB:4QBB}.
STRAND 149 153 {ECO:0000244|PDB:4QBB}.
STRAND 158 163 {ECO:0000244|PDB:4QBB}.
STRAND 166 169 {ECO:0000244|PDB:4QBB}.
HELIX 174 176 {ECO:0000244|PDB:4QBB}.
STRAND 177 185 {ECO:0000244|PDB:4QBB}.
TURN 195 197 {ECO:0000244|PDB:1QOL}.
HELIX 229 232 {ECO:0000244|PDB:1QQP}.
HELIX 268 274 {ECO:0000244|PDB:1QQP}.
HELIX 297 299 {ECO:0000244|PDB:1QQP}.
STRAND 301 305 {ECO:0000244|PDB:1QQP}.
STRAND 308 314 {ECO:0000244|PDB:1QQP}.
HELIX 332 334 {ECO:0000244|PDB:1QQP}.
HELIX 342 344 {ECO:0000244|PDB:1QQP}.
STRAND 348 355 {ECO:0000244|PDB:1QQP}.
STRAND 364 370 {ECO:0000244|PDB:1QQP}.
HELIX 376 383 {ECO:0000244|PDB:1QQP}.
STRAND 384 397 {ECO:0000244|PDB:1QQP}.
STRAND 404 413 {ECO:0000244|PDB:1QQP}.
HELIX 421 428 {ECO:0000244|PDB:1QQP}.
STRAND 429 434 {ECO:0000244|PDB:1QQP}.
TURN 436 438 {ECO:0000244|PDB:1QQP}.
STRAND 440 446 {ECO:0000244|PDB:1QQP}.
STRAND 451 455 {ECO:0000244|PDB:1QQP}.
TURN 457 459 {ECO:0000244|PDB:1QQP}.
STRAND 463 474 {ECO:0000244|PDB:1QQP}.
TURN 476 478 {ECO:0000244|PDB:1QQP}.
STRAND 483 499 {ECO:0000244|PDB:1QQP}.
HELIX 548 554 {ECO:0000244|PDB:1QQP}.
TURN 562 564 {ECO:0000244|PDB:1QQP}.
STRAND 565 569 {ECO:0000244|PDB:1QQP}.
STRAND 577 583 {ECO:0000244|PDB:1QQP}.
HELIX 588 590 {ECO:0000244|PDB:1QQP}.
HELIX 594 599 {ECO:0000244|PDB:1QQP}.
STRAND 602 607 {ECO:0000244|PDB:1QQP}.
STRAND 609 615 {ECO:0000244|PDB:1QQP}.
STRAND 622 630 {ECO:0000244|PDB:1QQP}.
HELIX 640 643 {ECO:0000244|PDB:1QQP}.
STRAND 646 652 {ECO:0000244|PDB:1QQP}.
STRAND 658 663 {ECO:0000244|PDB:1QQP}.
STRAND 668 670 {ECO:0000244|PDB:1QQP}.
STRAND 672 675 {ECO:0000244|PDB:1QQP}.
STRAND 687 697 {ECO:0000244|PDB:1QQP}.
STRAND 702 709 {ECO:0000244|PDB:1QQP}.
STRAND 714 718 {ECO:0000244|PDB:1QQP}.
HELIX 739 742 {ECO:0000244|PDB:1QQP}.
HELIX 752 754 {ECO:0000244|PDB:1QQP}.
HELIX 756 760 {ECO:0000244|PDB:1QQP}.
STRAND 762 766 {ECO:0000244|PDB:1QQP}.
HELIX 777 779 {ECO:0000244|PDB:1QQP}.
HELIX 785 791 {ECO:0000244|PDB:1QQP}.
STRAND 793 808 {ECO:0000244|PDB:1QQP}.
STRAND 810 813 {ECO:0000244|PDB:1QQP}.
HELIX 819 823 {ECO:0000244|PDB:1QQP}.
STRAND 827 830 {ECO:0000244|PDB:1QQP}.
STRAND 837 841 {ECO:0000244|PDB:1QQP}.
STRAND 846 852 {ECO:0000244|PDB:1QQP}.
STRAND 891 893 {ECO:0000244|PDB:1QQP}.
STRAND 895 912 {ECO:0000244|PDB:1QQP}.
STRAND 921 924 {ECO:0000244|PDB:1QQP}.
SEQUENCE 2332 AA; 258927 MW; 4A83176F43447D68 CRC64;
MNTTDCFIAL VQAIREIKAL FLSRTTGKME LTLYNGEKKT FYSRPNNHDN CWLNAILQLF
RYVEEPFFDW VYSSPENLTL EAIKQLEDLT GLELHEGGPP ALVIWNIKHL LHTGIGTASR
PSEVCMVDGT DMCLADFHAG IFLKGQEHAV FACVTSNGWY AIDDEDFYPW TPDPSDVLVF
VPYDQEPLNG EWKAKVQRKL KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG
DNAISGGSNE GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI
LTTRNGHTTS TTQSSVGVTY GYATAEDFVS GPNTSGLETR VVQAERFFKT HLFDWVTSDS
FGRCHLLELP TDHKGVYGSL TDSYAYMRNG WDVEVTAVGN QFNGGCLLVA MVPELYSIQK
RELYQLTLFP HQFINPRTNM TAHITVPFVG VNRYDQYKVH KPWTLVVMVV APLTVNTEGA
PQIKVYANIA PTNVHVAGEF PSKEGIFPVA CSDGYGGLVT TDPKTADPVY GKVFNPPRNQ
LPGRFTNLLD VAEACPTFLR FEGGVPYVTT KTDSDRVLAQ FDMSLAAKQM SNTFLAGLAQ
YYTQYSGTIN LHFMFTGPTD AKARYMVAYA PPGMEPPKTP EAAAHCIHAE WDTGLNSKFT
FSIPYLSAAD YAYTASGVAE TTNVQGWVCL FQITHGKADG DALVVLASAG KDFELRLPVD
ARAETTSAGE SADPVTTTVE NYGGETQIQR RQHTDVSFIM DRFVKVTPQN QINILDLMQI
PSHTLVGALL RASTYYFSDL EIAVKHEGDL TWVPNGAPEK ALDNTTNPTA YHKAPLTRLA
LPYTAPHRVL ATVYNGECRY NRNAVPNLRG DLQVLAQKVA RTLPTSFNYG AIKATRVTEL
LYRMKRAETY CPRPLLAIHP TEARHKQKIV APVKQTLNFD LLKLAGDVES NPGPFFFSDV
RSNFSKLVET INQMQEDMST KHGPDFNRLV SAFEELAIGV KAIRTGLDEA KPWYKLIKLL
SRLSCMAAVA ARSKDPVLVA IMLADTGLEI LDSTFVVKKI SDSLSSLFHV PAPVFSFGAP
VLLAGLVKVA SSFFRSTPED LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW
IASEEKFVTM TDLVPGILEK QRDLNDPSKY KEAKEWLDNA RQACLKSGNV HIANLCKVVA
PAPSKSRPEP VVVCLRGKSG QGKSFLANVL AQAISTHFTG RIDSVWYCPP DPDHFDGYNQ
QTVVVMDDLG QNPDGKDFKY FAQMVSTTGF IPPMASLEDK GKPFNSKVII ATTNLYSGFT
PRTMVCPDAL NRRFHFDIDV SAKDGYKINS KLDIIKALED THANPVAMFQ YDCALLNGMA
VEMKRMQQDM FKPQPPLQNV YQLVQEVIDR VELHEKVSSH PIFKQISIPS QKSVLYFLIE
KGQHEAAIEF FEGMVHDSIK EELRPLIQQT SFVKRAFKRL KENFEIVALC LTLLANIVIM
IRETRKRQKM VDDAVNEYIE KANITTDDKT LDEAEKSPLE TSGASTVGFR ERTLPGQKAC
DDVNSEPAQP VEEQPQAEGP YAGPLERQKP LKVRAKLPQQ EGPYAGPMER QKPLKVKAKA
PVVKEGPYEG PVKKPVALKV KAKNLIVTES GAPPTDLQKM VMGNTKPVEL ILDGKTVAIC
CATGVFGTAY LVPRHLFAEK YDKIMVDGRA MTDSDYRVFE FEIKVKGQDM LSDAALMVLH
RGNRVRDITK HFRDTARMKK GTPVVGVINN ADVGRLIFSG EALTYKDIVV CMDGDTMPGL
FAYRAATKAG YCGGAVLAKD GADTFIVGTH SAGGNGVGYC SCVSRSMLLK MKAHIDPEPH
HEGLIVDTRD VEERVHVMRK TKLAPTVAHG VFNPEFGPAA LSNKDPRLNE GVVLDEVIFS
KHKGDTKMSE EDKALFRRCA ADYASRLHSV LGTANAPLSI YEAIKGVDGL DAMEPDTAPG
LPWALQGKRR GALIDFENGT VGPEVEAALK LMEKREYKFV CQTFLKDEIR PLEKVRAGKT
RIVDVLPVEH ILYTRMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD
VDYSAFDANH CSDAMNIMFE EVFRTEFGFH PNAEWILKTL VNTEHAYENK RITVGGGMPS
GCSATSIINT ILNNIYVLYA LRRHYEGVEL DTYTMISYGD DIVVASDYDL DFEALKPHFK
SLGQTITPAD KSDKGFVLGH SITDVTFLKR HFHMDYGTGF YKPVMASKTL EAILSFARRG
TIQEKLISVA GLAVHSGPDE YRRLFEPFQG LFEIPSYRSL YLRWVNAVCG DA


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