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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_FMDVO              Reviewed;        2332 AA.
P03305;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
10-OCT-2018, entry version 184.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Leader protease;
Short=Lb(pro);
EC=3.4.22.46 {ECO:0000269|PubMed:11034318};
Contains:
RecName: Full=Capsid protein VP0;
AltName: Full=VP4-VP2;
Contains:
RecName: Full=Capsid protein VP4;
AltName: Full=P1A;
AltName: Full=Virion protein 4;
Contains:
RecName: Full=Capsid protein VP2;
AltName: Full=P1B;
AltName: Full=Virion protein 2;
Contains:
RecName: Full=Capsid protein VP3;
AltName: Full=P1C;
AltName: Full=Virion protein 3;
Contains:
RecName: Full=Capsid 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=Protease 3C;
EC=3.4.22.28 {ECO:0000269|PubMed:3041041};
AltName: Full=Picornain 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 (PROTEASE 3C).
PubMed=3041041;
Vakharia V.N., Devaney M.A., Moore D.M., Dunn J.J., Grubman M.J.;
"Proteolytic processing of foot-and-mouth disease virus polyproteins
expressed in a cell-free system from clone-derived transcripts.";
J. Virol. 61:3199-3207(1987).
[6]
FUNCTION (CAPSID PROTEIN VP1).
PubMed=2543752; DOI=10.1099/0022-1317-70-3-625;
Fox G., Parry N.R., Barnett P.V., McGinn B., Rowlands D.J., Brown F.;
"The cell attachment site on foot-and-mouth disease virus includes the
amino acid sequence RGD (arginine-glycine-aspartic acid).";
J. Gen. Virol. 70:625-637(1989).
[7]
FUNCTION (PROTEIN 2A).
PubMed=1658199; DOI=10.1099/0022-1317-72-11-2727;
Ryan M.D., King A.M., Thomas G.P.;
"Cleavage of foot-and-mouth disease virus polyprotein is mediated by
residues located within a 19 amino acid sequence.";
J. Gen. Virol. 72:2727-2732(1991).
[8]
FUNCTION (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).
[9]
FUNCTION (LEADER PROTEASE).
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).
[10]
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).
[11]
FUNCTION (LEADER PROTEASE).
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).
[12]
COVALENT RNA LINKAGE OF 3B PROTEINS, URIDYLYLATION, AND FUNCTION
(RNA-DIRECTED RNA POLYMERASE 3D-POL).
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).
[13]
FUNCTION (LEADER PROTEASE), AND SUBCELLULAR LOCATION (LEADER
PROTEASE).
PubMed=17881445; DOI=10.1128/JVI.01467-07;
de Los Santos T., Diaz-San Segundo F., Grubman M.J.;
"Degradation of nuclear factor kappa B during foot-and-mouth disease
virus infection.";
J. Virol. 81:12803-12815(2007).
[14]
FUNCTION (CAPSID PROTEIN VP2), FUNCTION (CAPSID PROTEIN VP3), AND
FUNCTION (CAPSID PROTEIN VP1).
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).
[15]
FUNCTION (CAPSID PROTEIN VP1).
PubMed=18045932; DOI=10.1128/JVI.01480-07;
Dicara D., Burman A., Clark S., Berryman S., Howard M.J., Hart I.R.,
Marshall J.F., Jackson T.;
"Foot-and-mouth disease virus forms a highly stable, EDTA-resistant
complex with its principal receptor, integrin alphavbeta6:
implications for infectiousness.";
J. Virol. 82:1537-1546(2008).
[16]
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).
[17]
FUNCTION (PROTEIN 2C).
PubMed=20507978; DOI=10.1074/jbc.M110.129940;
Sweeney T.R., Cisnetto V., Bose D., Bailey M., Wilson J.R., Zhang X.,
Belsham G.J., Curry S.;
"Foot-and-mouth disease virus 2C is a hexameric AAA+ protein with a
coordinated ATP hydrolysis mechanism.";
J. Biol. Chem. 285:24347-24359(2010).
[18]
FUNCTION (LEADER PROTEASE).
PubMed=21307201; DOI=10.1128/JVI.02589-10;
Wang D., Fang L., Li P., Sun L., Fan J., Zhang Q., Luo R., Liu X.,
Li K., Chen H., Chen Z., Xiao S.;
"The leader proteinase of foot-and-mouth disease virus negatively
regulates the type I interferon pathway by acting as a viral
deubiquitinase.";
J. Virol. 85:3758-3766(2011).
[19]
FUNCTION (PROTEIN 2C), AND INTERACTION WITH HOST BECN1 (PROTEIN 2C).
PubMed=22933281; DOI=10.1128/JVI.01610-12;
Gladue D.P., O'Donnell V., Baker-Branstetter R., Holinka L.G.,
Pacheco J.M., Fernandez-Sainz I., Lu Z., Brocchi E., Baxt B.,
Piccone M.E., Rodriguez L., Borca M.V.;
"Foot-and-mouth disease virus nonstructural protein 2C interacts with
Beclin1, modulating virus replication.";
J. Virol. 86:12080-12090(2012).
[20]
FUNCTION (PROTEIN 2C), AND INTERACTION WITH HOST VIM (PROTEIN 2C).
PubMed=23576498; DOI=10.1128/JVI.00448-13;
Gladue D.P., O'Donnell V., Baker-Branstetter R., Holinka L.G.,
Pacheco J.M., Fernandez Sainz I., Lu Z., Ambroggio X., Rodriguez L.,
Borca M.V.;
"Foot-and-mouth disease virus modulates cellular vimentin for virus
survival.";
J. Virol. 87:6794-6803(2013).
[21]
SUBCELLULAR LOCATION (RNA-DIRECTED RNA POLYMERASE 3D-POL), AND NUCLEAR
LOCALIZATIION SIGNAL (RNA-DIRECTED RNA POLYMERASE 3D-POL).
PubMed=23886493; DOI=10.1016/j.virol.2013.06.011;
Sanchez-Aparicio M.T., Rosas M.F., Sobrino F.;
"Characterization of a nuclear localization signal in the foot-and-
mouth disease virus polymerase.";
Virology 444:203-210(2013).
[22]
TOPOLOGY (PROTEIN 3A), AND SUBCELLULAR LOCATION (PROTEIN 3A).
PubMed=25275544; DOI=10.1371/journal.pone.0106685;
Gonzalez-Magaldi M., Martin-Acebes M.A., Kremer L., Sobrino F.;
"Membrane topology and cellular dynamics of foot-and-mouth disease
virus 3A protein.";
PLoS ONE 9:E106685-E106685(2014).
[23]
FUNCTION (PROTEIN 3A), INTERACTION WITH HOST DCTN3 (PROTEIN 3A), AND
SUBCELLULAR LOCATION (PROTEIN 3A).
PubMed=24352458; DOI=10.1128/JVI.03059-13;
Gladue D.P., O'Donnell V., Baker-Bransetter R., Pacheco J.M.,
Holinka L.G., Arzt J., Pauszek S., Fernandez-Sainz I., Fletcher P.,
Brocchi E., Lu Z., Rodriguez L.L., Borca M.V.;
"Interaction of foot-and-mouth disease virus nonstructural protein 3A
with host protein DCTN3 is important for viral virulence in cattle.";
J. Virol. 88:2737-2747(2014).
[24]
FUNCTION (PROTEIN 2B), SUBUNIT (PROTEIN 2B), SUBCELLULAR LOCATION
(PROTEIN 2B), AND TOPOLOGY (PROTEIN 2B).
PubMed=25946195; DOI=10.1371/journal.pone.0125828;
Ao D., Guo H.C., Sun S.Q., Sun D.H., Fung T.S., Wei Y.Q., Han S.C.,
Yao X.P., Cao S.Z., Liu D.X., Liu X.T.;
"Viroporin Activity of the Foot-and-Mouth Disease Virus Non-Structural
2B Protein.";
PLoS ONE 10:E0125828-E0125828(2015).
[25]
FUNCTION (CAPSID PROTEIN VP1), AND INTERACTION WITH HOST ITGAV/ITGB6
(CAPSID PROTEIN VP1).
PubMed=28534487; DOI=10.1038/ncomms15408;
Kotecha A., Wang Q., Dong X., Ilca S.L., Ondiviela M., Zihe R.,
Seago J., Charleston B., Fry E.E., Abrescia N.G.A., Springer T.A.,
Huiskonen J.T., Stuart D.I.;
"Rules of engagement between alphavbeta6 integrin and foot-and-mouth
disease virus.";
Nat. Commun. 8:15408-15408(2017).
[26]
FUNCTION (LEADER PROTEASE), AND INTERACTION WITH HOST ISG15 (LEADER
PROTEASE).
PubMed=29463763; DOI=10.1073/pnas.1710617115;
Swatek K.N., Aumayr M., Pruneda J.N., Visser L.J., Berryman S.,
Kueck A.F., Geurink P.P., Ovaa H., van Kuppeveld F.J.M., Tuthill T.J.,
Skern T., Komander D.;
"Irreversible inactivation of ISG15 by a viral leader protease enables
alternative infection detection strategies.";
Proc. Natl. Acad. Sci. U.S.A. 115:2371-2376(2018).
[27]
FUNCTION (PROTEIN 3A), AND SUBCELLULAR LOCATION (PROTEIN 3A).
PubMed=29536193; DOI=10.1007/s00705-018-3795-9;
Lotufo C.M., Wilda M., Giraldez A.N., Grigera P.R., Mattion N.M.;
"Relevance of the N-terminal and major hydrophobic domains of non-
structural protein 3A in the replicative process of a DNA-launched
foot-and-mouth disease virus replicon.";
Arch. Virol. 163:1769-1778(2018).
[28]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), FUNCTION (CAPSID PROTEIN VP2),
FUNCTION (CAPSID PROTEIN VP3), FUNCTION (CAPSID PROTEIN VP1),
SUBCELLULAR LOCATION (CAPSID PROTEIN VP2), SUBCELLULAR LOCATION
(CAPSID PROTEIN VP3), AND SUBCELLULAR LOCATION (CAPSID PROTEIN VP1).
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).
[29]
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).
[30]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 202-286; 287-504 AND
505-724.
PubMed=9927414; DOI=10.1093/emboj/18.3.543;
Fry E.E., Lea S.M., Jackson T., Newman J.W., Ellard F.M.,
Blakemore W.E., Abu-Ghazaleh R., Samuel A., King A.M., Stuart D.I.;
"The structure and function of a foot-and-mouth disease virus-
oligosaccharide receptor complex.";
EMBO J. 18:543-554(1999).
[31]
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).
[32]
STRUCTURE BY NMR OF 29-195.
PubMed=17897674; DOI=10.1016/j.jmb.2007.08.061;
Cencic R., Mayer C., Juliano M.A., Juliano L., Konrat R., Kontaxis G.,
Skern T.;
"Investigating the substrate specificity and oligomerisation of the
leader protease of foot and mouth disease virus using NMR.";
J. Mol. Biol. 373:1071-1087(2007).
[33]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 29-195, FUNCTION (LEADER
PROTEASE), AND ACTIVE SITE (LEADER PROTEASE).
PubMed=25240326; DOI=10.1016/j.virol.2014.08.023;
Steinberger J., Grishkovskaya I., Cencic R., Juliano L., Juliano M.A.,
Skern T.;
"Foot-and-mouth disease virus leader proteinase: structural insights
into the mechanism of intermolecular cleavage.";
Virology 468:397-408(2014).
-!- FUNCTION: Leader protease: Autocatalytically cleaves itself from
the polyprotein at the L/VP0 junction. Cleaves also the host
translation initiation factors EIF4G1 and EIF4G3, in order to
shutoff the capped cellular mRNA transcription. Plays a role in
counteracting host innate antiviral response using diverse
mechanisms. Possesses a deubiquitinase activity acting on both
'Lys'-48 and 'Lys'-63-linked polyubiquitin chains. In turn,
inhibits the ubiquitination and subsequent activation of key
signaling molecules of type I IFN response such as host DDX58,
TBK1, TRAF3 and TRAF6. Inhibits host NF-kappa-B activity by
inducing a decrease in RELA mRNA levels. Cleaves a peptide bond in
the C-terminus of host ISG15, resulting in the damaging of this
mofidier that can no longer be attached to target proteins.
{ECO:0000269|PubMed:11034318, ECO:0000269|PubMed:15016848,
ECO:0000269|PubMed:17881445, ECO:0000269|PubMed:21307201,
ECO:0000269|PubMed:29463763, ECO:0000269|PubMed:8386879}.
-!- FUNCTION: Capsid protein VP4: Lies on the inner surface of the
capsid shell. After binding to the host receptor, the capsid
undergoes conformational changes. Capsid protein VP4 is released,
capsid protein VP1 N-terminus is externalized, and together, they
shape a pore in the host membrane through which the viral genome
is translocated into the host cell cytoplasm. After genome has
been released, the channel shrinks.
{ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: Capsid protein VP2: Forms an icosahedral capsid of
pseudo T=3 symmetry with capsid proteins VP1 and VP3. The capsid
is composed of 60 copies of each capsid protein organized in the
form of twelve pentamers and encloses the viral positive strand
RNA genome. {ECO:0000269|PubMed:2537470}.
-!- FUNCTION: Capsid protein V1: Forms an icosahedral capsid of pseudo
T=3 symmetry with capsid proteins VP2 and VP3. The capsid is
composed of 60 copies of each capsid protein organized in the form
of twelve pentamers and encloses the viral positive strand RNA
genome. Mediates cell entry by attachment to an integrin receptor,
usually host ITGAV/ITGB6, via a conserved arginine-glycine-
aspartic acid (R-G-D) motif. {ECO:0000269|PubMed:18045932,
ECO:0000269|PubMed:2537470, ECO:0000269|PubMed:2543752,
ECO:0000269|PubMed:28534487}.
-!- FUNCTION: Capsid protein V3: Forms an icosahedral capsid of pseudo
T=3 symmetry with capsid proteins VP0 and VP3. The capsid is
composed of 60 copies of each capsid protein organized in the form
of twelve pentamers and encloses the viral positive strand RNA
genome. {ECO:0000269|PubMed:2537470}.
-!- FUNCTION: Protein 2A: Mediates self-processing of the polyprotein
by a translational effect termed "ribosome skipping".
Mechanistically, 2A-mediated cleavage occurs between the C-
terminal glycine and the proline of the downstream protein 2B. In
the case of foot-and-mouth disease virus, the 2A oligopeptide is
post-translationally 'trimmed' from the C-terminus of the upstream
protein 1D by 3C proteinase. {ECO:0000269|PubMed:1658199}.
-!- FUNCTION: Protein 2B: Plays an essential role in the virus
replication cycle by acting as a viroporin. Creates a pore in the
host reticulum endoplasmic and as a consequence releases Ca2+ in
the cytoplasm of infected cell. In turn, high levels of
cytoplasmic calcium may trigger membrane trafficking and transport
of viral ER-associated proteins to viroplasms, sites of viral
genome replication. {ECO:0000269|PubMed:25946195}.
-!- FUNCTION: Protein 2C: Associates with and induces structural
rearrangements of intracellular membranes. Triggers host autophagy
by interacting with host BECN1 and thereby promotes viral
replication. Participates in viral replication and interacts with
host DHX9. Displays RNA-binding, nucleotide binding and NTPase
activities. May play a role in virion morphogenesis and viral RNA
encapsidation by interacting with the capsid protein VP3.
{ECO:0000269|PubMed:20507978, ECO:0000269|PubMed:21307201,
ECO:0000269|PubMed:22933281, ECO:0000269|PubMed:23576498}.
-!- FUNCTION: Protein 3A: Plays important roles in virus replication,
virulence and host range. {ECO:0000269|PubMed:24352458,
ECO:0000269|PubMed:29536193}.
-!- FUNCTION: Protein 3B-1: Covalently linked to the 5'-end of both
the positive-strand and negative-strand genomic RNAs. Acts as a
genome-linked replication primer. {ECO:0000269|PubMed:15919922}.
-!- FUNCTION: Protein 3B-2: Covalently linked to the 5'-end of both
the positive-strand and negative-strand genomic RNAs. Acts as a
genome-linked replication primer. {ECO:0000269|PubMed:15919922}.
-!- FUNCTION: Protein 3B-3: Covalently linked to the 5'-end of both
the positive-strand and negative-strand genomic RNAs. Acts as a
genome-linked replication primer. {ECO:0000269|PubMed:15919922}.
-!- FUNCTION: Protease 3C: Cysteine protease that generates mature
viral proteins from the precursor polyprotein. In addition to its
proteolytic activity, binds to viral RNA and thus influences viral
genome replication. RNA and substrate bind cooperatively to the
protease. {ECO:0000269|PubMed:3041041}.
-!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic
and antigenomic RNA by recognizing replications specific signals.
Covalently attaches UMP to a tyrosine of VPg, which is used to
prime RNA synthesis. The positive stranded RNA genome is first
replicated at virus induced membranous vesicles, creating a dsRNA
genomic replication form. This dsRNA is then used as template to
synthesize positive stranded RNA genomes. ss(+)RNA genomes are
either translated, replicated or encapsidated.
{ECO:0000255|PROSITE-ProRule:PRU00539,
ECO:0000269|PubMed:15919922}.
-!- 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: Leader protease: Interacts with host ISG15
(PubMed:29463763). Capsid protein VP1: Interacts (via R-G-D motif)
with host ITGAV/ITGB6 (PubMed:28534487). Protein 2B: Forms
homooligomers. Protein 2C: Interacts with host VIM
(PubMed:23576498). Interacts with host BECN1 (PubMed:22933281).
Protein 3A: Interacts with host DCTN3 (PubMed:24352458).
{ECO:0000269|PubMed:22933281, ECO:0000269|PubMed:23576498,
ECO:0000269|PubMed:24352458, ECO:0000269|PubMed:25946195,
ECO:0000269|PubMed:28534487, ECO:0000269|PubMed:29463763}.
-!- SUBCELLULAR LOCATION: Leader protease: Host nucleus
{ECO:0000269|PubMed:17881445}. Host cytoplasm
{ECO:0000269|PubMed:17881445}.
-!- SUBCELLULAR LOCATION: Capsid protein VP2: Virion
{ECO:0000269|PubMed:2537470}. Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein VP3: Virion
{ECO:0000269|PubMed:2537470}. Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein VP1: Virion
{ECO:0000269|PubMed:2537470}. Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 2B: Host endoplasmic reticulum
membrane {ECO:0000269|PubMed:25946195}.
-!- 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 cytoplasm
{ECO:0000269|PubMed:24352458, ECO:0000269|PubMed:29536193}. Host
endoplasmic reticulum membrane {ECO:0000269|PubMed:25275544}.
Note=Interacts with host endoplasmic reticulum membranes through
its hydrophobic stretch, while its N- and C-terminus face the
cytosol being accessible to other viral proteins for viral
replication. {ECO:0000269|PubMed:25275544}.
-!- 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: Protease 3C: Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Host
cytoplasm {ECO:0000269|PubMed:23886493}. Host nucleus
{ECO:0000269|PubMed:23886493}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Lab;
IsoId=P03305-1; Sequence=Displayed;
Name=Lb;
IsoId=P03305-2; Sequence=VSP_018982;
-!- PTM: Leader protease: Removes six residues from its own C-
terminus, generating sLb(pro). {ECO:0000269|PubMed:25240326}.
-!- PTM: Genome polyprotein: 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. {ECO:0000269|PubMed:11297676}.
-!- PTM: Capsid protein VP4: Myristoylation is required during RNA
encapsidation and formation of the mature virus particle.
{ECO:0000250}.
-!- PTM: Protein 3B-1: 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.
{ECO:0000269|PubMed:15919922}.
-!- PTM: Protein 3B-2: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.
{ECO:0000269|PubMed:15919922}.
-!- PTM: Protein 3B-3: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.
{ECO:0000269|PubMed:15919922}.
-!- MISCELLANEOUS: 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.
PDB; 6FFA; X-ray; 1.50 A; A=29-195.
PDBsum; 1QMY; -.
PDBsum; 1QOL; -.
PDBsum; 1QQP; -.
PDBsum; 2JQF; -.
PDBsum; 2JQG; -.
PDBsum; 4QBB; -.
PDBsum; 6FFA; -.
DisProt; DP00573; -.
ProteinModelPortal; P03305; -.
SMR; P03305; -.
ELM; P03305; -.
MEROPS; C03.008; -.
PRIDE; P03305; -.
KEGG; ag:CAA25416; -.
OrthoDB; VOG090000RV; -.
BRENDA; 3.4.22.46; 2315.
EvolutionaryTrace; P03305; -.
Proteomes; UP000008765; Genome.
GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
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:0019785; F:ISG15-specific protease activity; IDA:UniProtKB.
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:0039648; P:modulation by virus of host protein ubiquitination; IDA:UniProtKB.
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:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0039579; P:suppression by virus of host ISG15 activity; IDA:UniProtKB.
GO; GO:0039644; P:suppression by virus of host NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; IDA:UniProtKB.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; 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; 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;
Autocatalytic cleavage; 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 endoplasmic reticulum;
Host membrane; Host nucleus; 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 Capsid protein VP0. {ECO:0000255}.
/FTId=PRO_0000374076.
CHAIN 202 286 Capsid protein VP4. {ECO:0000255}.
/FTId=PRO_0000039876.
CHAIN 287 504 Capsid protein VP2. {ECO:0000255}.
/FTId=PRO_0000039877.
CHAIN 505 724 Capsid protein VP3. {ECO:0000255}.
/FTId=PRO_0000039878.
CHAIN 725 935 Capsid 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 Protease 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:0000269|PubMed:2543752}.
MOTIF 1879 1886 Nuclear localization signal.
{ECO:0000269|PubMed:23886493}.
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 33 {ECO:0000244|PDB:6FFA}.
STRAND 38 40 {ECO:0000244|PDB:6FFA}.
STRAND 47 49 {ECO:0000244|PDB:6FFA}.
HELIX 51 63 {ECO:0000244|PDB:6FFA}.
HELIX 66 68 {ECO:0000244|PDB:1QOL}.
HELIX 69 72 {ECO:0000244|PDB:6FFA}.
STRAND 73 76 {ECO:0000244|PDB:2JQG}.
HELIX 79 90 {ECO:0000244|PDB:6FFA}.
HELIX 100 107 {ECO:0000244|PDB:6FFA}.
HELIX 108 110 {ECO:0000244|PDB:6FFA}.
STRAND 111 113 {ECO:0000244|PDB:2JQF}.
STRAND 115 120 {ECO:0000244|PDB:6FFA}.
STRAND 123 126 {ECO:0000244|PDB:6FFA}.
STRAND 129 131 {ECO:0000244|PDB:2JQG}.
HELIX 134 136 {ECO:0000244|PDB:6FFA}.
STRAND 137 143 {ECO:0000244|PDB:6FFA}.
STRAND 145 147 {ECO:0000244|PDB:6FFA}.
STRAND 149 155 {ECO:0000244|PDB:6FFA}.
STRAND 158 163 {ECO:0000244|PDB:6FFA}.
STRAND 166 169 {ECO:0000244|PDB:6FFA}.
HELIX 174 176 {ECO:0000244|PDB:6FFA}.
STRAND 177 182 {ECO:0000244|PDB:6FFA}.
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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