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Genome polyprotein [Cleaved into: Leader protease (Lpro) (EC 3.4.22.46); Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Protein VP2 (P1B) (Virion protein 2); Protein VP3 (P1C) (Virion protein 3); Protein VP1 (P1D) (Virion protein 1); Protein 2A (P2A) (P52); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Protein 3B-1 (P3B-1) (Genome-linked protein VPg1); Protein 3B-2 (P3B-2) (Genome-linked protein VPg2); Protein 3B-3 (P3B-3) (Genome-linked protein VPg3); Picornain 3C (EC 3.4.22.28) (Protease 3C) (P3C) (Protease P20B); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48) (P56A)]

 POLG_FMDV1              Reviewed;        2332 AA.
P03306; Q64768; Q84750; Q84751; Q84752; Q84753; Q84754; Q84760;
Q84761; Q84762; Q84763; Q84764; Q84765; Q84766; Q84767; Q84768;
Q84769; Q89824;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-FEB-2005, sequence version 2.
20-JUN-2018, entry version 174.
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 (strain A10-61) (Aphthovirus A) (FMDV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Aphthovirus.
NCBI_TaxID=12112;
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=6324120; DOI=10.1093/nar/12.5.2461;
Carroll A.R., Rowlands D.J., Clarke B.E.;
"The complete nucleotide sequence of the RNA coding for the primary
translation product of foot and mouth disease virus.";
Nucleic Acids Res. 12:2461-2472(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 115-1048.
PubMed=6282711; DOI=10.1016/0378-1119(82)90068-3;
Boothroyd J.C., Harris T.J.R., Rowlands D.J., Lowe P.A.;
"The nucleotide sequence of cDNA coding for the structural proteins of
foot-and-mouth disease virus.";
Gene 17:153-161(1982).
[3]
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).
[4] {ECO:0000244|PDB:2BHG}
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1650-1855, AND ACTIVE SITE.
PubMed=15654079; DOI=10.1074/jbc.M413254200;
Birtley J.R., Knox S.R., Jaulent A.M., Brick P., Leatherbarrow R.J.,
Curry S.;
"Crystal structure of foot-and-mouth disease virus 3C protease. New
insights into catalytic mechanism and cleavage specificity.";
J. Biol. Chem. 280:11520-11527(2005).
[5] {ECO:0000244|PDB:1ZBA, ECO:0000244|PDB:1ZBE}
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 726-937; 287-504; 505-725
AND 202-286.
PubMed=15958669; DOI=10.1099/vir.0.80730-0;
Fry E.E., Newman J.W., Curry S., Najjam S., Jackson T., Blakemore W.,
Lea S.M., Miller L., Burman A., King A.M., Stuart D.I.;
"Structure of Foot-and-mouth disease virus serotype A10 61 alone and
complexed with oligosaccharide receptor: receptor conservation in the
face of antigenic variation.";
J. Gen. Virol. 86:1909-1920(2005).
[6] {ECO:0000244|PDB:2J92}
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1649-1855, AND MUTAGENESIS
OF CYS-1791.
PubMed=17065215; DOI=10.1128/JVI.01587-06;
Sweeney T.R., Roque-Rosell N., Birtley J.R., Leatherbarrow R.J.,
Curry S.;
"Structural and mutagenic analysis of foot-and-mouth disease virus 3C
protease reveals the role of the beta-ribbon in proteolysis.";
J. Virol. 81:115-124(2007).
[7] {ECO:0000244|PDB:2WV4, ECO:0000244|PDB:2WV5}
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1650-1862 AND 931-940.
PubMed=19883658; DOI=10.1016/j.jmb.2009.10.048;
Zunszain P.A., Knox S.R., Sweeney T.R., Yang J., Roque-Rosell N.,
Belsham G.J., Leatherbarrow R.J., Curry S.;
"Insights into cleavage specificity from the crystal structure of
foot-and-mouth disease virus 3C protease complexed with a peptide
substrate.";
J. Mol. Biol. 395:375-389(2010).
-!- FUNCTION: The leader protease autocatalytically cleaves itself
from the polyprotein at the L/VP0 junction. It cleaves the host
translation initiation factors EIF4G1 and EIF4G3, in order to shut
down the capped cellular mRNA transcription. Increases translation
driven by the viral internal ribosome entry site (IRES).
{ECO:0000250|UniProtKB:P03305, ECO:0000250|UniProtKB:P03311}.
-!- 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 (alphavbeta1, alphavbeta3, alpha5beta1,
alphavbeta6, alphavbeta8) to provide virion attachment to target
Attachment via host integrins induces virion internalization
predominantly through clathrin-mediated endocytosis (By
similarity). {ECO:0000250}.
-!- 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 with integrins heterodimers alphavbeta6,
alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta8 (By
similarity). This virus has an RGSD motif in place of the
otherwise conserved RGD integrin-binding motif and the potential
to bind heparan sulfate as well (PubMed:15958669). {ECO:0000250,
ECO:0000269|PubMed:15958669}.
-!- 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;
Comment=Both isoforms are able to cleave the L/VP0 junction and
the host translation initiation factor EIF4G1.;
Name=Lab; Synonyms=P20a;
IsoId=P03306-1; Sequence=Displayed;
Name=Lb; Synonyms=P16;
IsoId=P03306-2; Sequence=VSP_018979;
-!- 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. {ECO:0000250}.
-!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA25127.1; Type=Frameshift; Positions=1727, 1739; Evidence={ECO:0000305};
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EMBL; X00429; CAA25127.1; ALT_FRAME; Genomic_RNA.
EMBL; V01130; CAA24361.1; -; Genomic_RNA.
PIR; A93508; GNNY2F.
PDB; 1ZBA; X-ray; 2.00 A; 1=726-937, 2=287-504, 3=505-725, 4=202-286.
PDB; 1ZBE; X-ray; 3.00 A; 1=726-937, 2=287-504, 3=505-725, 4=202-286.
PDB; 2BHG; X-ray; 1.90 A; A/B=1650-1855.
PDB; 2J92; X-ray; 2.20 A; A/B=1649-1855.
PDB; 2WV4; X-ray; 2.50 A; A/B=1650-1862, C/D=931-940.
PDB; 2WV5; X-ray; 2.70 A; A/B/C/D=1650-1862, E/F/G/H=936-940.
PDBsum; 1ZBA; -.
PDBsum; 1ZBE; -.
PDBsum; 2BHG; -.
PDBsum; 2J92; -.
PDBsum; 2WV4; -.
PDBsum; 2WV5; -.
ProteinModelPortal; P03306; -.
SMR; P03306; -.
MEROPS; C03.008; -.
PRIDE; P03306; -.
OrthoDB; VOG090000PJ; -.
EvolutionaryTrace; P03306; -.
Proteomes; UP000008764; 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; ISS: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 complex 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; ISS: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; 2.60.120.20; -; 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; IPR038765; Papain_like_cys_pep_sf.
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.
InterPro; IPR029053; Viral_coat.
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.
SUPFAM; SSF54001; SSF54001; 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-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_0000039816.
CHAIN 1 201 Leader protease. {ECO:0000255}.
/FTId=PRO_0000039817.
CHAIN 202 504 Protein VP0. {ECO:0000255}.
/FTId=PRO_0000374073.
CHAIN 202 286 Protein VP4. {ECO:0000255}.
/FTId=PRO_0000039820.
CHAIN 287 504 Protein VP2. {ECO:0000255}.
/FTId=PRO_0000039821.
CHAIN 505 725 Protein VP3. {ECO:0000255}.
/FTId=PRO_0000039822.
CHAIN 726 935 Protein VP1. {ECO:0000255}.
/FTId=PRO_0000039823.
CHAIN 936 953 Protein 2A. {ECO:0000255}.
/FTId=PRO_0000039824.
CHAIN 954 1107 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000310973.
CHAIN 1108 1425 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000310974.
CHAIN 1426 1578 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000310975.
CHAIN 1579 1601 Protein 3B-1. {ECO:0000255}.
/FTId=PRO_0000039825.
CHAIN 1602 1625 Protein 3B-2. {ECO:0000255}.
/FTId=PRO_0000039826.
CHAIN 1626 1649 Protein 3B-3. {ECO:0000255}.
/FTId=PRO_0000039827.
CHAIN 1650 1862 Picornain 3C. {ECO:0000255}.
/FTId=PRO_0000039828.
CHAIN 1863 2332 RNA-directed RNA polymerase 3D-POL.
{ECO:0000255}.
/FTId=PRO_0000039829.
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 867 870 Cell attachment site.
{ECO:0000269|PubMed:15958669}.
ACT_SITE 51 51 For leader protease activity.
{ECO:0000250}.
ACT_SITE 148 148 For leader protease activity.
{ECO:0000250}.
ACT_SITE 163 163 For leader protease activity.
{ECO:0000250}.
ACT_SITE 1695 1695 For picornain 3C activity. {ECO:0000255}.
ACT_SITE 1695 1695 For picornain 3C activity; Proton
donor/acceptor. {ECO:0000244|PDB:2BHG,
ECO:0000255}.
ACT_SITE 1733 1733 For picornain 3C activity.
{ECO:0000244|PDB:2BHG}.
ACT_SITE 1812 1812 For picornain 3C activity.
{ECO:0000244|PDB:2BHG, 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 725 726 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 1831 1831 Important for catalytic activity.
{ECO:0000244|PDB:2BHG}.
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 511 511 Interchain; in VP3 dimer. {ECO:0000250}.
VAR_SEQ 1 28 Missing (in isoform Lb). {ECO:0000305}.
/FTId=VSP_018979.
MUTAGEN 1791 1791 C->S: Almost complete loss of picornain
3C activity.
{ECO:0000269|PubMed:17065215}.
CONFLICT 396 396 S -> C (in Ref. 2; CAA24361).
{ECO:0000305}.
CONFLICT 632 632 P -> L (in Ref. 2; CAA24361).
{ECO:0000305}.
HELIX 229 232 {ECO:0000244|PDB:1ZBA}.
HELIX 268 274 {ECO:0000244|PDB:1ZBA}.
STRAND 301 305 {ECO:0000244|PDB:1ZBA}.
STRAND 308 314 {ECO:0000244|PDB:1ZBA}.
HELIX 332 334 {ECO:0000244|PDB:1ZBA}.
HELIX 342 344 {ECO:0000244|PDB:1ZBA}.
STRAND 348 355 {ECO:0000244|PDB:1ZBA}.
STRAND 364 370 {ECO:0000244|PDB:1ZBA}.
HELIX 376 383 {ECO:0000244|PDB:1ZBA}.
STRAND 384 397 {ECO:0000244|PDB:1ZBA}.
STRAND 404 414 {ECO:0000244|PDB:1ZBA}.
HELIX 422 428 {ECO:0000244|PDB:1ZBA}.
STRAND 429 434 {ECO:0000244|PDB:1ZBA}.
TURN 436 438 {ECO:0000244|PDB:1ZBA}.
STRAND 440 446 {ECO:0000244|PDB:1ZBA}.
STRAND 450 455 {ECO:0000244|PDB:1ZBA}.
TURN 457 459 {ECO:0000244|PDB:1ZBA}.
STRAND 463 474 {ECO:0000244|PDB:1ZBA}.
STRAND 477 479 {ECO:0000244|PDB:1ZBE}.
STRAND 483 499 {ECO:0000244|PDB:1ZBA}.
HELIX 548 554 {ECO:0000244|PDB:1ZBA}.
TURN 562 564 {ECO:0000244|PDB:1ZBA}.
STRAND 565 569 {ECO:0000244|PDB:1ZBA}.
STRAND 572 574 {ECO:0000244|PDB:1ZBA}.
STRAND 577 583 {ECO:0000244|PDB:1ZBA}.
HELIX 588 590 {ECO:0000244|PDB:1ZBA}.
HELIX 594 599 {ECO:0000244|PDB:1ZBA}.
STRAND 602 607 {ECO:0000244|PDB:1ZBA}.
STRAND 609 615 {ECO:0000244|PDB:1ZBA}.
STRAND 622 630 {ECO:0000244|PDB:1ZBA}.
STRAND 632 636 {ECO:0000244|PDB:1ZBA}.
HELIX 641 644 {ECO:0000244|PDB:1ZBA}.
STRAND 647 653 {ECO:0000244|PDB:1ZBA}.
STRAND 659 664 {ECO:0000244|PDB:1ZBA}.
STRAND 669 671 {ECO:0000244|PDB:1ZBA}.
STRAND 673 676 {ECO:0000244|PDB:1ZBA}.
STRAND 688 698 {ECO:0000244|PDB:1ZBA}.
STRAND 703 710 {ECO:0000244|PDB:1ZBA}.
STRAND 715 719 {ECO:0000244|PDB:1ZBA}.
HELIX 730 732 {ECO:0000244|PDB:1ZBA}.
HELIX 740 743 {ECO:0000244|PDB:1ZBA}.
HELIX 753 755 {ECO:0000244|PDB:1ZBA}.
HELIX 757 761 {ECO:0000244|PDB:1ZBA}.
STRAND 763 767 {ECO:0000244|PDB:1ZBE}.
STRAND 772 775 {ECO:0000244|PDB:1ZBA}.
HELIX 778 780 {ECO:0000244|PDB:1ZBA}.
HELIX 786 792 {ECO:0000244|PDB:1ZBA}.
STRAND 794 809 {ECO:0000244|PDB:1ZBA}.
STRAND 811 814 {ECO:0000244|PDB:1ZBA}.
HELIX 820 824 {ECO:0000244|PDB:1ZBA}.
STRAND 828 831 {ECO:0000244|PDB:1ZBA}.
STRAND 838 842 {ECO:0000244|PDB:1ZBA}.
STRAND 847 853 {ECO:0000244|PDB:1ZBA}.
STRAND 890 892 {ECO:0000244|PDB:1ZBA}.
STRAND 894 911 {ECO:0000244|PDB:1ZBA}.
STRAND 921 923 {ECO:0000244|PDB:1ZBA}.
STRAND 936 938 {ECO:0000244|PDB:2WV5}.
HELIX 1657 1664 {ECO:0000244|PDB:2BHG}.
STRAND 1665 1672 {ECO:0000244|PDB:2BHG}.
STRAND 1675 1687 {ECO:0000244|PDB:2BHG}.
STRAND 1689 1693 {ECO:0000244|PDB:2BHG}.
HELIX 1694 1697 {ECO:0000244|PDB:2BHG}.
STRAND 1702 1706 {ECO:0000244|PDB:2BHG}.
STRAND 1709 1711 {ECO:0000244|PDB:2BHG}.
HELIX 1713 1715 {ECO:0000244|PDB:2BHG}.
STRAND 1716 1719 {ECO:0000244|PDB:2BHG}.
STRAND 1722 1725 {ECO:0000244|PDB:2WV4}.
STRAND 1726 1728 {ECO:0000244|PDB:2BHG}.
STRAND 1733 1742 {ECO:0000244|PDB:2BHG}.
HELIX 1749 1751 {ECO:0000244|PDB:2BHG}.
STRAND 1752 1755 {ECO:0000244|PDB:2J92}.
STRAND 1763 1770 {ECO:0000244|PDB:2BHG}.
TURN 1771 1773 {ECO:0000244|PDB:2BHG}.
STRAND 1774 1784 {ECO:0000244|PDB:2BHG}.
STRAND 1800 1804 {ECO:0000244|PDB:2BHG}.
STRAND 1815 1820 {ECO:0000244|PDB:2BHG}.
STRAND 1823 1834 {ECO:0000244|PDB:2BHG}.
STRAND 1837 1842 {ECO:0000244|PDB:2BHG}.
HELIX 1845 1853 {ECO:0000244|PDB:2BHG}.
SEQUENCE 2332 AA; 259319 MW; FE8A553569F1A6DD CRC64;
MNTTNCFIAL VYLIREIKTL FRSRTKGKME FTLHNGEKKT FYSRPNNHDN CWLNTILQLF
RYVDEPFFDW VYNSPENLTL DAIKQLENFT GLELHEGGPP ALVIWNIKHL LQTGIGTASR
PSEVCMVDGT DMCLADFHAG IFMKGQEHAV FACVTSDGWY AIDDEDFYPW TPDPSDVLVF
VPYDQEPLNG DWKTQVQKKL KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMSTQLG
DNTISGGSNE GSTDTTSTHT TNTQNNDWFS KLASSAFTGL FGALLADKKT EETTLLEDRI
LTTRNGHTTS TTQSSVGVTY GYSTEEDHVA GPNTSGLETR VVQAERFFKK FLFDWTTDKP
FGYLTKLELP TDHHGVFGHL VDSYAYMRNG WDVEVSAVGN QFNGGCLLVA MVPEWKAFDT
REKYQLTLFP HQFISPRTNM TAHITVPYLG VNRYDQYKKH KPWTLVVMVL SPLTVSNTAA
PQIKVYANIA PTYVHVAGEL PSKEGIFPVA CADGYGGLVT TDPKTADPVY GKVYNPPKTN
YPGRFTNLLD VAEACPTFLR FDDGKPYVVT RADDTRLLAK FDVSLAAKHM SNTYLSGIAQ
YYTQYSGTIN LHFMFTGSTD SKARYMVAYI PPGVETPPDT PEEAAHCIHA EWDTGLNSKF
TFSIPYVSAA DYAYTASDTA ETTNVQGWVC VYQITHGKAE NDTLLVSASA GKDFELRLPI
DPRTQTTTTG ESADPVTTTV ENYGGDTQVQ RRHHTDVGFI MDRFVKINSL SPTHVIDLMQ
THKHGIVGAL LRAATYYFSD LEIVVRHDGN LTWVPNGAPE AALSNTSNPT AYNKAPFTRL
ALPYTAPHRV LATVYDGTNK YSASDSRSGD LGSIAARVAT QLPASFNYGA IQAQAIHELL
VRMKRAELYC PRPLLAIKVT SQDRYKQKII APAKQLLNFD LLKLAGDVES NLGPFFFADV
RSNFSKLVDT INQMQEDMST KHGPDFNRLV SAFEELATGV KAIRTGLDEA KPWYKLIKLL
SRLSCMAAVA ARSKDPVLVA IMLADTGLEI LDSTFVVKKS SDSLSSLFHV PAPAFSFGAP
VLLAGLVKVA SSFFRSTPED LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW
IASEEKFVTM TDLVPGILEK QRDLNDPGKY KEAKEWLDNA RQACLKSGNV HIANLCKVVA
PAPSKSRPEP VVVCLRGKSG QGKSFLANVL AQAISTHFTG RIDSVWYCPP DPDHFDGYNQ
QTVVVMDDLG QNPDGKDFKY FAQMVSTTGF IPPMASLEDK GKPFNSKVII ATTNLYSGFT
PRTMVCPDAL NRRFHFDIDV SAKDGYKINN KLDIIKALED THTNPVAMFQ YDCALLNGMA
VEMKRLQQDM FKPQPPLQNV YQLVQEVIER VELHEKVSSH PIFKQISIPS QKSVLYFLIE
KGQHEAAIEF FEGMVHDSVK EELRPLIQQT SFVKRAFKRL KENFEIVALC LTLLANIVIM
IRETRKRQKM VDDAVNEYIE RANITTDDKT LDEAEKNPLE TSGASTVGFR ERSLTGQKVR
DDVSSEPAQP AEDQPQAEGP YSGPLERQKP LKVRAKLPQQ EGPYAGPMER QKPLKVKVKA
PVVKEGPYEG PVKKPVALKV KARNLIVTES GAPPTDLQKM VMGNTKPVEL NLDGKTVAIC
CATGVFGTAY LVPRHLFAEK YDKIMLDGRA MTDSDYRVFE FEIKVKGQDM LSDAALIVLH
RGNCVRDITK HFRDTARMKK GTPVVGVVNN ADVGRLIFSG EALTYKDIVV CMDGDTMPGL
FAYKAATRAG YCGGAVLAKD GADTFIVGTH SAGGNGVGYC SCVSRSMLQK MKAHVDPEPH
HEGLIVDTRD VEERVHVMRK TKLAPTVAYG VFNPEFGPAA LSNKDPRLNE GVVLDDVIFS
KHKGDAKMTE EDKALFRRCA ADYASRLHSV LGTANAPLSI YEAIKGVDGL DAMEPDTAPG
LPWALQGKRR GALIDFENGT VGPEVEAALK LMEKREYKFA CQTFLKDEIR PMEKVRAGKT
RIVDVLPVEH ILYTKMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD
VDYSAFDANH CSDAMNIMFE EVFRTDFGFH PNAEWILKTL VNTEHAYENK RITVEGGMPS
GCSATSIINT ILNNIYVLYA LRRHYEGVEL DTYTMISYGD DIVVASDYDL DFEALKPHFK
SLGQTITPAD KSDKGFVLGQ SITDVTFLKR HFHMDYGTGF YKPVMASKTL EAILSFARRG
TIQEKLISVA GLAVHSGPDE YRRLFEPFQG LFEIPSYRSL YLRWVNAVCG DA


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