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Genome polyprotein [Cleaved into: N-terminal protease (N-pro) (EC 3.4.22.-) (Autoprotease p20); Capsid protein C; E(rns) glycoprotein (gp44/48); Envelope glycoprotein E1 (gp33); Envelope glycoprotein E2 (gp55); p7; Non-structural protein 2-3 (NS2-3); Cysteine protease NS2 (EC 3.4.22.-) (Non-structural protein 2); Serine protease NS3 (EC 3.4.21.113) (EC 3.6.1.15) (EC 3.6.4.13) (Non-structural protein 3); Non-structural protein 4A (NS4A); Non-structural protein 4B (NS4B); Non-structural protein 5A (NS5A); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B)]

 POLG_CSFVA              Reviewed;        3898 AA.
P19712;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
11-JUL-2001, sequence version 2.
12-SEP-2018, entry version 155.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=N-terminal protease;
Short=N-pro;
EC=3.4.22.-;
AltName: Full=Autoprotease p20;
Contains:
RecName: Full=Capsid protein C;
AltName: Full=Core protein;
Contains:
RecName: Full=E(rns) glycoprotein;
AltName: Full=gp44/48;
Contains:
RecName: Full=Envelope glycoprotein E1;
AltName: Full=gp33;
Contains:
RecName: Full=Envelope glycoprotein E2;
AltName: Full=gp55;
Contains:
RecName: Full=p7;
Contains:
RecName: Full=Non-structural protein 2-3;
Short=NS2-3;
Contains:
RecName: Full=Cysteine protease NS2;
EC=3.4.22.-;
AltName: Full=Non-structural protein 2;
Contains:
RecName: Full=Serine protease NS3;
EC=3.4.21.113;
EC=3.6.1.15;
EC=3.6.4.13;
AltName: Full=Non-structural protein 3;
Contains:
RecName: Full=Non-structural protein 4A;
Short=NS4A;
Contains:
RecName: Full=Non-structural protein 4B;
Short=NS4B;
Contains:
RecName: Full=Non-structural protein 5A;
Short=NS5A;
Contains:
RecName: Full=RNA-directed RNA polymerase;
EC=2.7.7.48;
AltName: Full=NS5B;
Classical swine fever virus (strain Alfort) (CSFV) (Hog cholera
virus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Pestivirus.
NCBI_TaxID=11097;
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2763466; DOI=10.1016/0042-6822(89)90625-9;
Meyers G., Ruemenapf T., Thiel H.-J.;
"Molecular cloning and nucleotide sequence of the genome of hog
cholera virus.";
Virology 171:555-567(1989).
[2]
SEQUENCE REVISION TO 2731.
Meyers G.;
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[3]
HOMODIMERIZATION (E(RNS) GLYCOPROTEIN), AND GLYCOSYLATION (E(RNS)
GLYCOPROTEIN).
PubMed=1870198;
Thiel H.-J., Stark R., Weiland E., Ruemenapf T., Meyers G.;
"Hog cholera virus: molecular composition of virions from a
pestivirus.";
J. Virol. 65:4705-4712(1991).
[4]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND PROTEIN SEQUENCE OF
169-178.
PubMed=8388499;
Ruemenapf T., Unger G., Strauss J.H., Thiel H.-J.;
"Processing of the envelope glycoproteins of pestiviruses.";
J. Virol. 67:3288-3294(1993).
[5]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=8230432;
Stark R., Meyers G., Ruemenapf T., Thiel H.-J.;
"Processing of pestivirus polyprotein: cleavage site between
autoprotease and nucleocapsid protein of classical swine fever
virus.";
J. Virol. 67:7088-7095(1993).
[6]
FUNCTION (E(RNS) GLYCOPROTEIN).
PubMed=8356450;
Schneider R., Unger G., Stark R., Schneider-Scherzer E., Thiel H.J.;
"Identification of a structural glycoprotein of an RNA virus as a
ribonuclease.";
Science 261:1169-1171(1993).
[7]
ACTIVE SITE (N-TERMINAL PROTEASE), AND MUTAGENESIS OF GLU-22; HIS-40;
HIS-49; CYS-69; HIS-99; CYS-112; HIS-130; CYS-134; CYS-138 AND
CYS-161.
PubMed=9499122;
Ruemenapf T., Stark R., Heimann M., Thiel H.-J.;
"N-terminal protease of pestiviruses: identification of putative
catalytic residues by site-directed mutagenesis.";
J. Virol. 72:2544-2547(1998).
[8]
INDUCTION.
PubMed=9573242;
Sizova D.V., Kolupaeva V.G., Pestova T.V., Shatsky I.N., Hellen C.U.;
"Specific interaction of eukaryotic translation initiation factor 3
with the 5' nontranslated regions of hepatitis C virus and classical
swine fever virus RNAs.";
J. Virol. 72:4775-4782(1998).
[9]
FUNCTION (CAPSID PROTEIN C).
PubMed=9617770;
Liu J.J., Wong M.L., Chang T.J.;
"The recombinant nucleocapsid protein of classical swine fever virus
can act as a transcriptional regulator.";
Virus Res. 53:75-80(1998).
[10]
SUBCELLULAR LOCATION (E(RNS) GLYCOPROTEIN), AND SUBCELLULAR LOCATION
(ENVELOPE GLYCOPROTEIN E2).
PubMed=10355762;
Weiland F., Weiland E., Unger G., Saalmuller A., Thiel H.-J.;
"Localization of pestiviral envelope proteins E(rns) and E2 at the
cell surface and on isolated particles.";
J. Gen. Virol. 80:1157-1165(1999).
[11]
FUNCTION (ENVELOPE GLYCOPROTEIN E2).
PubMed=10438869;
Moser C., Stettler P., Tratschin J.D., Hofmann M.A.;
"Cytopathogenic and noncytopathogenic RNA replicons of classical swine
fever virus.";
J. Virol. 73:7787-7794(1999).
[12]
FUNCTION (ENVELOPE GLYCOPROTEIN E1), AND FUNCTION (ENVELOPE
GLYCOPROTEIN E2).
PubMed=15527858; DOI=10.1016/j.virol.2004.09.023;
Wang Z., Nie Y., Wang P., Ding M., Deng H.;
"Characterization of classical swine fever virus entry by using
pseudotyped viruses: E1 and E2 are sufficient to mediate viral
entry.";
Virology 330:332-341(2004).
[13]
FUNCTION (NON-STRUCTURAL PROTEIN 2-3), AND FUNCTION (NON-STRUCTURAL
PROTEIN 4A).
PubMed=17482232; DOI=10.1016/j.virol.2007.03.056;
Moulin H.R., Seuberlich T., Bauhofer O., Bennett L.C., Tratschin J.D.,
Hofmann M.A., Ruggli N.;
"Nonstructural proteins NS2-3 and NS4A of classical swine fever virus:
essential features for infectious particle formation.";
Virology 365:376-389(2007).
[14]
FUNCTION (N-TERMINAL PROTEASE), INTERACTION WITH HOST IRF3 (N-TERMINAL
PROTEASE), AND SUBCELLULAR LOCATION (N-TERMINAL PROTEASE).
PubMed=17215286; DOI=10.1128/JVI.02032-06;
Bauhofer O., Summerfield A., Sakoda Y., Tratschin J.D., Hofmann M.A.,
Ruggli N.;
"Classical swine fever virus Npro interacts with interferon regulatory
factor 3 and induces its proteasomal degradation.";
J. Virol. 81:3087-3096(2007).
[15]
FUNCTION (E(RNS) GLYCOPROTEIN).
PubMed=19264773; DOI=10.1128/JVI.01710-08;
Tews B.A., Schuermann E.M., Meyers G.;
"Mutation of cysteine 171 of pestivirus E rns RNase prevents homodimer
formation and leads to attenuation of classical swine fever virus.";
J. Virol. 83:4823-4834(2009).
[16]
FUNCTION (E(RNS) GLYCOPROTEIN).
PubMed=19767841; DOI=10.1139/w09-013;
Luo X., Ling D., Li T., Wan C., Zhang C., Pan Z.;
"Classical swine fever virus Erns glycoprotein antagonizes induction
of interferon-beta by double-stranded RNA.";
Can. J. Microbiol. 55:698-704(2009).
[17]
FUNCTION (NON-STRUCTURAL PROTEIN 3), INTERACTION WITH RNA-DIRECTED RNA
POLYMERASE (NON-STRUCTURAL PROTEIN 3), AND INTERACTION WITH
NON-STRUCTURAL PROTEIN 3 (RNA-DIRECTED RNA POLYMERASE).
PubMed=19185595; DOI=10.1016/j.virusres.2008.12.014;
Wen G., Xue J., Shen Y., Zhang C., Pan Z.;
"Characterization of classical swine fever virus (CSFV) nonstructural
protein 3 (NS3) helicase activity and its modulation by CSFV RNA-
dependent RNA polymerase.";
Virus Res. 141:63-70(2009).
[18]
FUNCTION (P7).
PubMed=22496228; DOI=10.1128/JVI.00560-12;
Gladue D.P., Holinka L.G., Largo E., Fernandez Sainz I., Carrillo C.,
O'Donnell V., Baker-Branstetter R., Lu Z., Ambroggio X., Risatti G.R.,
Nieva J.L., Borca M.V.;
"Classical swine fever virus p7 protein is a viroporin involved in
virulence in swine.";
J. Virol. 86:6778-6791(2012).
[19]
ACTIVE SITE (N-TERMINAL PROTEASE), AND FUNCTION (N-TERMINAL PROTEASE).
PubMed=24606708; DOI=10.1016/j.virol.2014.01.026;
Gottipati K., Acholi S., Ruggli N., Choi K.H.;
"Autocatalytic activity and substrate specificity of the pestivirus N-
terminal protease Npro.";
Virology 452:303-309(2014).
[20]
INTERACTION WITH HOST OS9 (CAPSID PROTEIN C).
PubMed=25010283; DOI=10.1016/j.virol.2014.05.008;
Gladue D.P., O'Donnell V., Fernandez-Sainz I.J., Fletcher P.,
Baker-Branstetter R., Holinka L.G., Sanford B., Carlson J., Lu Z.,
Borca M.V.;
"Interaction of structural core protein of classical swine fever virus
with endoplasmic reticulum-associated degradation pathway protein
OS9.";
Virology 460:173-179(2014).
[21]
FUNCTION (P7).
PubMed=24189547; DOI=10.1016/j.antiviral.2013.10.015;
Largo E., Gladue D.P., Huarte N., Borca M.V., Nieva J.L.;
"Pore-forming activity of pestivirus p7 in a minimal model system
supports genus-specific viroporin function.";
Antiviral Res. 101:30-36(2014).
[22]
INTERACTION WITH HOST TRX2 (ENVELOPE GLYCOPROTEIN E2).
PubMed=26041303; DOI=10.1128/JVI.00429-15;
Li S., Wang J., He W.R., Feng S., Li Y., Wang X., Liao Y., Qin H.Y.,
Li L.F., Dong H., Sun Y., Luo Y., Qiu H.J.;
"Thioredoxin 2 Is a Novel E2-Interacting Protein That Inhibits the
Replication of Classical Swine Fever Virus.";
J. Virol. 89:8510-8524(2015).
[23]
INTERACTION WITH HOST RPSA (E(RNS) GLYCOPROTEIN), AND FUNCTION (E(RNS)
GLYCOPROTEIN).
PubMed=25694590; DOI=10.1128/JVI.00019-15;
Chen J., He W.R., Shen L., Dong H., Yu J., Wang X., Yu S., Li Y.,
Li S., Luo Y., Sun Y., Qiu H.J.;
"The laminin receptor is a cellular attachment receptor for classical
Swine Fever virus.";
J. Virol. 89:4894-4906(2015).
[24]
FUNCTION (N-TERMINAL PROTEASE), AND INTERACTION WITH HOST IRF3
(N-TERMINAL PROTEASE).
PubMed=27334592; DOI=10.1128/JVI.00318-16;
Gottipati K., Holthauzen L.M., Ruggli N., Choi K.H.;
"Pestivirus Npro Directly Interacts with Interferon Regulatory Factor
3 Monomer and Dimer.";
J. Virol. 90:7740-7747(2016).
[25]
FUNCTION (CAPSID PROTEIN C), AND SUBCELLULAR LOCATION (CAPSID PROTEIN
C).
PubMed=28290554; DOI=10.1038/srep44459;
Riedel C., Lamp B., Hagen B., Indik S., Ruemenapf T.;
"The core protein of a pestivirus protects the incoming virus against
IFN-induced effectors.";
Sci. Rep. 7:44459-44459(2017).
[26]
FUNCTION (NON-STRUCTURAL PROTEIN 3), AND INTERACTION WITH HOST TRAF6
(NON-STRUCTURAL PROTEIN 3).
PubMed=28751780; DOI=10.1038/s41598-017-06934-1;
Lv H., Dong W., Cao Z., Li X., Wang J., Qian G., Lv Q., Wang C.,
Guo K., Zhang Y.;
"TRAF6 is a novel NS3-interacting protein that inhibits classical
swine fever virus replication.";
Sci. Rep. 7:6737-6737(2017).
[27]
FUNCTION (NON-STRUCTURAL PROTEIN 4B), INTERACTION WITH HOST RAB5
(NON-STRUCTURAL PROTEIN 4B), SUBCELLULAR LOCATION (NON-STRUCTURAL
PROTEIN 4B), SUBCELLULAR LOCATION (SERINE PROTEASE NS3), AND
SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 5A).
PubMed=28848503; DOI=10.3389/fmicb.2017.01468;
Lin J., Wang C., Zhang L., Wang T., Zhang J., Liang W., Li C.,
Qian G., Ouyang Y., Guo K., Zhang Y.;
"Rab5 Enhances Classical Swine Fever Virus Proliferation and Interacts
with Viral NS4B Protein to Facilitate Formation of NS4B Related
Complex.";
Front. Microbiol. 8:1468-1468(2017).
[28]
FUNCTION (E(RNS) GLYCOPROTEIN), AND SUBUNIT (E(RNS) GLYCOPROTEIN).
PubMed=29235980; DOI=10.1099/jgv.0.000990;
Tucakov A.K., Yavuz S., Schuermann E.M., Mischler M., Klingebeil A.,
Meyers G.;
"dimerization via pseudoreversion partially restores virulence of
classical swine fever virus.";
J. Gen. Virol. 99:86-96(2018).
[29]
FUNCTION (NON-STRUCTURAL PROTEIN 4B), INTERACTION WITH HOST FTH1
(NON-STRUCTURAL PROTEIN 4B), AND SUBCELLULAR LOCATION (NON-STRUCTURAL
PROTEIN 4B).
PubMed=29844394; DOI=10.1038/s41598-018-26777-8;
Qian G., Lv H., Lin J., Li X., Lv Q., Wang T., Zhang J., Dong W.,
Guo K., Zhang Y.;
"FHC, an NS4B-interacting Protein, Enhances Classical Swine Fever
Virus Propagation and Acts Positively in Viral Anti-apoptosis.";
Sci. Rep. 8:8318-8318(2018).
[30]
X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 1782-2280.
PubMed=25653438; DOI=10.1128/JVI.03165-14;
Tortorici M.A., Duquerroy S., Kwok J., Vonrhein C., Perez J., Lamp B.,
Bricogne G., Ruemenapf T., Vachette P., Rey F.A.;
"X-ray structure of the pestivirus NS3 helicase and its conformation
in solution.";
J. Virol. 89:4356-4371(2015).
[31]
X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 1590-2280, AND INTERACTION
WITH NS4A (SERINE PROTEASE NS3).
PubMed=28151973; DOI=10.1371/journal.ppat.1006134;
Dubrau D., Tortorici M.A., Rey F.A., Tautz N.;
"A positive-strand RNA virus uses alternative protein-protein
interactions within a viral protease/cofactor complex to switch
between RNA replication and virion morphogenesis.";
PLoS Pathog. 13:E1006134-E1006134(2017).
-!- FUNCTION: N-terminal protease: Leader cysteine autoprotease that
cleaves itself from the nascent polyprotein during translation of
the viral mRNA. Once released, plays a role in the inhibition of
host innate immune response by interacting with host IRF3 and
inducing its proteasomal degradation.
{ECO:0000269|PubMed:17215286, ECO:0000269|PubMed:24606708,
ECO:0000269|PubMed:27334592}.
-!- FUNCTION: Capsid protein C: Packages viral RNA to form a viral
nucleocapsid and thereby protects viral RNA. Plays also a role in
transcription regulation. Protects the incoming virus against IFN-
induced effectors. {ECO:0000269|PubMed:28290554,
ECO:0000269|PubMed:9617770}.
-!- FUNCTION: E(rns) glycoprotein: Plays a role in viral entry.
Interacts with host RPSA that acts as a cellular attachment
receptor for the virus. Possesses also intrinsic ribonuclease
(RNase) activity that can inhibit the production of type I
interferon and assist in the development of persistent infections.
{ECO:0000269|PubMed:19264773, ECO:0000269|PubMed:19767841,
ECO:0000269|PubMed:25694590, ECO:0000269|PubMed:29235980,
ECO:0000269|PubMed:8356450}.
-!- FUNCTION: Envelope glycoprotein E1: Plays a role in cell
attachment and subsequent fusion of viral and cellular membranes.
Therefore, mediates together with envelope glycoprotein E2 the
viral entry. {ECO:0000269|PubMed:15527858}.
-!- FUNCTION: Envelope glycoprotein E2: Plays a role in cell
attachment and subsequent fusion of viral and cellular membranes.
Therefore, mediates together with envelope glycoprotein E1 the
viral entry. {ECO:0000269|PubMed:15527858}.
-!- FUNCTION: P7: Plays an essential role in the virus replication
cycle by acting as a viroporin. Forms ion conductive pores, which
alters the cell permeability allowing the transport of ions and
other small molecules. {ECO:0000269|PubMed:22496228,
ECO:0000269|PubMed:24189547}.
-!- FUNCTION: Non-structural protein 2-3: Autoprotease that associates
with the host chaperone JIV and cleaves the NS2-3 protein between
NS2 and NS3. Plays also a role in the formation of infectious
particles. {ECO:0000269|PubMed:17482232}.
-!- FUNCTION: Cysteine protease NS2: Plays a roile in the regulation
of viral RNA replication. {ECO:0000269|PubMed:10438869}.
-!- FUNCTION: Serine protease NS3: Multifunctional protein that
contains an N-terminal protease and a C-terminal helicase, playing
essential roles in viral polyprotein processing and viral genome
replication. The chymotrypsin-like serine protease activity
utilizes NS4A as an essential cofactor and catalyzes the cleavage
of the polyprotein leading to the release of NS4A, NS4B, NS5A, and
NS5B. Plays a role in the inhibition of host NF-kappa-B activation
by interacting with and inhibiting host TRAF6. Interacts with NS5B
to enhance RNA-dependent RNA polymerase activity.
{ECO:0000269|PubMed:19185595, ECO:0000269|PubMed:28751780}.
-!- FUNCTION: Non-structural protein 4A: Acts as a cofactor for the
NS3 protease activity. {ECO:0000269|PubMed:17482232}.
-!- FUNCTION: Non-structural protein 4B: Induces a specific membrane
alteration that serves as a scaffold for the virus replication
complex. {ECO:0000250|UniProtKB:P27958}.
-!- FUNCTION: RNA-directed RNA polymerase: Replicates the viral (+)
and (-) genome. {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: Leu is conserved at position P1 for all four
cleavage sites. Alanine is found at position P1' of the NS4A-NS4B
cleavage site, whereas serine is found at position P1' of the NS3-
NS4A, NS4B-NS5A and NS5A-NS5B cleavage sites.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: N-terminal protease: Interacts with host IRF3
(PubMed:17215286, PubMed:27334592). Capsid protein C: Interacts
with host OS9 (PubMed:25010283). E(rns) glycoprotein: Homodimer
(PubMed:29235980); disulfide-linked. Interacts with host RPSA.
Envelope glycoprotein E2: Interacts with host TRX2. Forms
disulfide-linked homodimers as well as heterodimers with E1.
Serine protease NS3: Interacts with host TRAF6; this interaction
inhibits host NF-kappa-B pathway. Interacts with NS5B; this
interaction enhances RNA-dependent RNA polymerase activity.
Interacts with protein NS4A. Non-structural protein 4B: Interacts
with host RAB5, this interaction facilitates the formation of
NS4B-related complex (PubMed:28848503). Interacts with host FTH1;
this interaction plays a positive role in viral anti-apoptosis
(PubMed:29844394). {ECO:0000269|PubMed:17215286,
ECO:0000269|PubMed:19185595, ECO:0000269|PubMed:25010283,
ECO:0000269|PubMed:25694590, ECO:0000269|PubMed:28751780,
ECO:0000269|PubMed:28848503, ECO:0000269|PubMed:29235980,
ECO:0000269|PubMed:29844394}.
-!- SUBCELLULAR LOCATION: N-terminal protease: Host cytoplasm
{ECO:0000269|PubMed:17215286}.
-!- SUBCELLULAR LOCATION: Capsid protein C: Virion
{ECO:0000269|PubMed:28290554}.
-!- SUBCELLULAR LOCATION: E(rns) glycoprotein: Host cell membrane
{ECO:0000269|PubMed:28290554}; Peripheral membrane protein. Virion
membrane {ECO:0000269|PubMed:28290554}; Peripheral membrane
protein {ECO:0000305}. Note=The C-terminus membrane anchor of Erns
represents an amphipathic helix embedded in plane into the
membrane.
-!- SUBCELLULAR LOCATION: Envelope glycoprotein E2: Host cell surface
{ECO:0000269|PubMed:28290554}. Virion membrane
{ECO:0000269|PubMed:28290554}.
-!- SUBCELLULAR LOCATION: Cysteine protease NS2: Host membrane
{ECO:0000255|PROSITE-ProRule:PRU01029}; Multi-pass membrane
protein {ECO:0000255|PROSITE-ProRule:PRU01029}.
-!- SUBCELLULAR LOCATION: Serine protease NS3: Host cytoplasm
{ECO:0000269|PubMed:28848503}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host cytoplasm
{ECO:0000269|PubMed:28848503, ECO:0000269|PubMed:29844394}.
-!- SUBCELLULAR LOCATION: Non-structural protein 5A: Host cytoplasm
{ECO:0000269|PubMed:28848503}.
-!- INDUCTION: Translated cap independently from an internal ribosome
entry site (IRES). {ECO:0000269|PubMed:9573242}.
-!- PTM: The E(rns) glycoprotein is heavily glycosylated.
{ECO:0000269|PubMed:1870198}.
-!- PTM: The viral RNA of pestiviruses is expressed as a single
polyprotein which undergoes post-translational proteolytic
processing resulting in the production of at least eleven
individual proteins. The N-terminal protease cleaves itself from
the nascent polyprotein autocatalytically and thereby generates
the N-terminus of the adjacent viral capsid protein C.
{ECO:0000269|PubMed:8230432, ECO:0000269|PubMed:8388499}.
-!- PTM: Cleavage between E2 and p7 is partial. {ECO:0000250}.
-!- SIMILARITY: Belongs to the pestivirus polyprotein family.
{ECO:0000305}.
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EMBL; J04358; AAA43844.2; -; Genomic_RNA.
PDB; 4CBG; X-ray; 2.82 A; A/B/C/D=1782-2280.
PDB; 4CBH; X-ray; 2.51 A; A/B/C/D=1782-2280.
PDB; 4CBI; X-ray; 3.00 A; A/B/C/D=1782-2280.
PDB; 4CBL; X-ray; 3.05 A; A/B/C/D=1792-2280.
PDB; 4CBM; X-ray; 3.27 A; A/B/C/D=1782-2280.
PDB; 5MZ4; X-ray; 3.05 A; A/B=1590-2280.
PDBsum; 4CBG; -.
PDBsum; 4CBH; -.
PDBsum; 4CBI; -.
PDBsum; 4CBL; -.
PDBsum; 4CBM; -.
PDBsum; 5MZ4; -.
ProteinModelPortal; P19712; -.
SMR; P19712; -.
IntAct; P19712; 96.
MEROPS; C53.001; -.
PRIDE; P19712; -.
OrthoDB; VOG09000032; -.
PMAP-CutDB; P19712; -.
Proteomes; UP000008568; Genome.
GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
GO; GO:0044165; C:host cell endoplasmic reticulum; IDA:AgBase.
GO; GO:0042025; C:host cell nucleus; IDA:AgBase.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0019013; C:viral nucleocapsid; IDA:UniProtKB.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0004540; F:ribonuclease activity; IDA:UniProtKB.
GO; GO:0033897; F:ribonuclease T2 activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:1990214; P:negative regulation by symbiont of host protein levels; IDA:AgBase.
GO; GO:0032688; P:negative regulation of interferon-beta production; IDA:AgBase.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IDA:UniProtKB.
GO; GO:1990219; P:positive regulation by symbiont of host protein levels; IMP:AgBase.
GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IDA:AgBase.
GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
GO; GO:1903608; P:protein localization to cytoplasmic stress granule; IMP:AgBase.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IDA:UniProtKB.
GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IDA:UniProtKB.
GO; GO:0039548; P:suppression by virus of host IRF3 activity; IDA:UniProtKB.
GO; GO:0039644; P:suppression by virus of host NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0039547; P:suppression by virus of host TRAF activity; IDA:UniProtKB.
GO; GO:0039501; P:suppression by virus of host type I interferon production; IDA:AgBase.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IDA:UniProtKB.
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; cd00079; HELICc; 1.
Gene3D; 3.90.730.10; -; 1.
InterPro; IPR021824; Capsid-C_pestivirus.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR022120; NS2.
InterPro; IPR030399; NS2_C74.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008751; Peptidase_C53.
InterPro; IPR032521; Pestivirus_E2.
InterPro; IPR000280; Pestivirus_NS3_S31.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002166; RNA_pol_HCV.
InterPro; IPR036430; RNase_T2-like_sf.
InterPro; IPR033130; RNase_T2_His_AS_2.
Pfam; PF11889; DUF3409; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF05550; Peptidase_C53; 1.
Pfam; PF12387; Peptidase_C74; 1.
Pfam; PF05578; Peptidase_S31; 1.
Pfam; PF16329; Pestivirus_E2; 1.
Pfam; PF00998; RdRP_3; 1.
PRINTS; PR00729; CDVENDOPTASE.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF55895; SSF55895; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51692; PESTIVIRUS_NS2_PRO; 1.
PROSITE; PS51535; PESTIVIRUS_NS3PRO; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS00531; RNASE_T2_2; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus; ATP-binding;
Complete proteome; Direct protein sequencing; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
Host cell membrane; Host cytoplasm; Host membrane;
Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host IRF3 by virus;
Inhibition of host RLR pathway by virus; Ion channel; Ion transport;
Membrane; Nucleotide-binding; Nucleotidyltransferase; Protease;
RNA-directed RNA polymerase; Serine protease; Thiol protease;
Transferase; Transmembrane; Transmembrane helix; Transport;
Viral attachment to host cell; Viral immunoevasion; Viral ion channel;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus entry into host cell.
CHAIN 1 168 N-terminal protease.
/FTId=PRO_0000038050.
CHAIN 169 267 Capsid protein C.
/FTId=PRO_0000038051.
CHAIN 268 494 E(rns) glycoprotein.
/FTId=PRO_0000038052.
CHAIN 495 656 Envelope glycoprotein E1.
/FTId=PRO_0000038053.
CHAIN 657 1062 Envelope glycoprotein E2.
/FTId=PRO_0000038054.
CHAIN 1063 1132 p7. {ECO:0000250}.
/FTId=PRO_0000038055.
CHAIN 1133 2272 Non-structural protein 2-3.
{ECO:0000250}.
/FTId=PRO_0000038056.
CHAIN 1133 1589 Cysteine protease NS2.
{ECO:0000255|PROSITE-ProRule:PRU01029}.
/FTId=PRO_0000349361.
CHAIN 1590 2272 Serine protease NS3. {ECO:0000250}.
/FTId=PRO_0000038057.
CHAIN 2273 2336 Non-structural protein 4A. {ECO:0000250}.
/FTId=PRO_0000038058.
CHAIN 2337 2683 Non-structural protein 4B. {ECO:0000250}.
/FTId=PRO_0000038059.
CHAIN 2684 3180 Non-structural protein 5A. {ECO:0000250}.
/FTId=PRO_0000038060.
CHAIN 3181 3898 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000038061.
TRANSMEM 1140 1164 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1189 1209 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1217 1237 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1247 1267 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1281 1301 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1360 1380 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
TRANSMEM 1568 1588 Helical. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
DOMAIN 1 168 Peptidase C53.
DOMAIN 1441 1589 Peptidase C74. {ECO:0000255|PROSITE-
ProRule:PRU01029}.
DOMAIN 1590 1763 Peptidase S31. {ECO:0000255|PROSITE-
ProRule:PRU00868}.
DOMAIN 1802 1960 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1978 2179 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 3519 3642 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
ACT_SITE 22 22 For N-terminal protease activity.
{ECO:0000255|PROSITE-ProRule:PRU10046,
ECO:0000269|PubMed:9499122}.
ACT_SITE 49 49 For N-terminal protease activity.
{ECO:0000255|PROSITE-ProRule:PRU10046,
ECO:0000269|PubMed:9499122}.
ACT_SITE 69 69 For N-terminal protease activity.
{ECO:0000255|PROSITE-ProRule:PRU10046,
ECO:0000269|PubMed:24606708,
ECO:0000269|PubMed:9499122}.
ACT_SITE 1447 1447 For cysteine protease NS2 activity.
{ECO:0000255|PROSITE-ProRule:PRU01029}.
ACT_SITE 1461 1461 For cysteine protease NS2 activity.
{ECO:0000255|PROSITE-ProRule:PRU01029}.
ACT_SITE 1512 1512 For cysteine protease NS2 activity.
{ECO:0000255|PROSITE-ProRule:PRU01029}.
ACT_SITE 1658 1658 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00868}.
ACT_SITE 1695 1695 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00868}.
ACT_SITE 1752 1752 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00868}.
SITE 168 169 Cleavage; by autolysis.
SITE 267 268 Cleavage; by host signal peptidase.
SITE 494 495 Cleavage.
SITE 656 657 Cleavage; by host signal peptidase.
SITE 1062 1063 Cleavage; by host signal peptidase;
partial. {ECO:0000250}.
SITE 1132 1133 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 1589 1590 Cleavage; partial; cysteine protease NS2.
{ECO:0000255|PROSITE-ProRule:PRU01029}.
SITE 2272 2273 Cleavage; by serine protease NS3.
{ECO:0000250}.
SITE 2336 2337 Cleavage; by serine protease NS3.
{ECO:0000250}.
SITE 2683 2684 Cleavage; by serine protease NS3.
{ECO:0000250}.
SITE 3180 3181 Cleavage; by serine protease NS3.
{ECO:0000250}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 269 269 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 274 274 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 278 278 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 293 293 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 332 332 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 362 362 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 367 367 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 410 410 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 425 425 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 500 500 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 594 594 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 805 805 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 810 810 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 874 874 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 918 918 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 949 949 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 986 986 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 1713 1713 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2134 2134 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2217 2217 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2494 2494 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2787 2787 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2815 2815 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2891 2891 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 3211 3211 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 3316 3316 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 3689 3689 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 3698 3698 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 3794 3794 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
VARIANT 387 387 T -> A.
VARIANT 3542 3542 R -> S.
MUTAGEN 22 22 E->V: Almost complete loss of cleavage
between N-pro and C.
{ECO:0000269|PubMed:9499122}.
MUTAGEN 40 40 H->L: No effect.
{ECO:0000269|PubMed:9499122}.
MUTAGEN 49 49 H->L: Complete loss of cleavage between
N-pro and C.
{ECO:0000269|PubMed:9499122}.
MUTAGEN 69 69 C->A: Complete loss of cleavage between
N-pro and C.
{ECO:0000269|PubMed:9499122}.
MUTAGEN 69 69 C->S: Complete loss of cleavage between
N-pro and C.
{ECO:0000269|PubMed:9499122}.
MUTAGEN 99 99 H->L: No effect.
{ECO:0000269|PubMed:9499122}.
MUTAGEN 112 112 C->A: No effect.
{ECO:0000269|PubMed:9499122}.
MUTAGEN 112 112 C->S: No effect.
{ECO:0000269|PubMed:9499122}.
MUTAGEN 130 130 H->L: No effect.
{ECO:0000269|PubMed:9499122}.
MUTAGEN 134 134 C->A: No effect.
{ECO:0000269|PubMed:9499122}.
MUTAGEN 134 134 C->S: No effect.
{ECO:0000269|PubMed:9499122}.
MUTAGEN 138 138 C->A: No effect.
{ECO:0000269|PubMed:9499122}.
MUTAGEN 138 138 C->S: No effect.
{ECO:0000269|PubMed:9499122}.
MUTAGEN 161 161 C->A: No effect.
{ECO:0000269|PubMed:9499122}.
MUTAGEN 161 161 C->S: No effect.
{ECO:0000269|PubMed:9499122}.
STRAND 1598 1600 {ECO:0000244|PDB:5MZ4}.
HELIX 1610 1614 {ECO:0000244|PDB:5MZ4}.
STRAND 1632 1639 {ECO:0000244|PDB:5MZ4}.
STRAND 1642 1649 {ECO:0000244|PDB:5MZ4}.
STRAND 1652 1655 {ECO:0000244|PDB:5MZ4}.
HELIX 1657 1660 {ECO:0000244|PDB:5MZ4}.
STRAND 1665 1669 {ECO:0000244|PDB:5MZ4}.
STRAND 1672 1676 {ECO:0000244|PDB:5MZ4}.
STRAND 1680 1682 {ECO:0000244|PDB:5MZ4}.
TURN 1683 1686 {ECO:0000244|PDB:5MZ4}.
STRAND 1687 1691 {ECO:0000244|PDB:5MZ4}.
STRAND 1703 1712 {ECO:0000244|PDB:5MZ4}.
STRAND 1718 1727 {ECO:0000244|PDB:5MZ4}.
STRAND 1730 1734 {ECO:0000244|PDB:5MZ4}.
HELIX 1745 1748 {ECO:0000244|PDB:5MZ4}.
STRAND 1755 1758 {ECO:0000244|PDB:5MZ4}.
TURN 1759 1761 {ECO:0000244|PDB:5MZ4}.
STRAND 1764 1767 {ECO:0000244|PDB:5MZ4}.
STRAND 1770 1777 {ECO:0000244|PDB:5MZ4}.
STRAND 1780 1782 {ECO:0000244|PDB:5MZ4}.
HELIX 1792 1803 {ECO:0000244|PDB:4CBH}.
STRAND 1810 1814 {ECO:0000244|PDB:4CBH}.
STRAND 1817 1819 {ECO:0000244|PDB:4CBH}.
STRAND 1821 1823 {ECO:0000244|PDB:4CBH}.
HELIX 1824 1833 {ECO:0000244|PDB:4CBH}.
STRAND 1839 1845 {ECO:0000244|PDB:4CBH}.
HELIX 1846 1859 {ECO:0000244|PDB:4CBH}.
STRAND 1865 1871 {ECO:0000244|PDB:4CBH}.
STRAND 1880 1885 {ECO:0000244|PDB:4CBH}.
HELIX 1886 1889 {ECO:0000244|PDB:4CBH}.
HELIX 1894 1901 {ECO:0000244|PDB:4CBH}.
STRAND 1905 1910 {ECO:0000244|PDB:4CBH}.
HELIX 1912 1914 {ECO:0000244|PDB:4CBH}.
HELIX 1917 1927 {ECO:0000244|PDB:4CBH}.
HELIX 1928 1932 {ECO:0000244|PDB:4CBH}.
STRAND 1935 1939 {ECO:0000244|PDB:4CBH}.
STRAND 1956 1958 {ECO:0000244|PDB:4CBH}.
TURN 1970 1972 {ECO:0000244|PDB:4CBL}.
STRAND 1973 1976 {ECO:0000244|PDB:4CBG}.
STRAND 1979 1982 {ECO:0000244|PDB:4CBG}.
HELIX 1983 1987 {ECO:0000244|PDB:4CBG}.
STRAND 1990 1993 {ECO:0000244|PDB:4CBG}.
HELIX 1997 2009 {ECO:0000244|PDB:4CBG}.
STRAND 2014 2017 {ECO:0000244|PDB:4CBG}.
HELIX 2024 2030 {ECO:0000244|PDB:4CBG}.
STRAND 2032 2034 {ECO:0000244|PDB:4CBG}.
STRAND 2036 2041 {ECO:0000244|PDB:4CBG}.
HELIX 2042 2045 {ECO:0000244|PDB:4CBI}.
STRAND 2054 2057 {ECO:0000244|PDB:4CBG}.
STRAND 2061 2068 {ECO:0000244|PDB:4CBH}.
STRAND 2070 2073 {ECO:0000244|PDB:4CBH}.
STRAND 2075 2082 {ECO:0000244|PDB:4CBH}.
HELIX 2086 2093 {ECO:0000244|PDB:4CBH}.
STRAND 2096 2100 {ECO:0000244|PDB:4CBH}.
STRAND 2103 2105 {ECO:0000244|PDB:4CBH}.
STRAND 2112 2114 {ECO:0000244|PDB:4CBG}.
HELIX 2118 2124 {ECO:0000244|PDB:4CBH}.
HELIX 2125 2128 {ECO:0000244|PDB:4CBH}.
TURN 2129 2132 {ECO:0000244|PDB:4CBH}.
HELIX 2135 2146 {ECO:0000244|PDB:4CBH}.
HELIX 2153 2166 {ECO:0000244|PDB:4CBH}.
HELIX 2173 2181 {ECO:0000244|PDB:4CBH}.
HELIX 2188 2193 {ECO:0000244|PDB:4CBH}.
TURN 2194 2196 {ECO:0000244|PDB:4CBH}.
STRAND 2204 2207 {ECO:0000244|PDB:4CBH}.
STRAND 2210 2215 {ECO:0000244|PDB:4CBH}.
STRAND 2234 2237 {ECO:0000244|PDB:4CBH}.
HELIX 2238 2246 {ECO:0000244|PDB:4CBH}.
HELIX 2257 2270 {ECO:0000244|PDB:4CBH}.
HELIX 2272 2275 {ECO:0000244|PDB:4CBH}.
STRAND 2276 2279 {ECO:0000244|PDB:5MZ4}.
STRAND 2298 2312 {ECO:0000244|PDB:5MZ4}.
HELIX 2315 2317 {ECO:0000244|PDB:5MZ4}.
STRAND 2336 2343 {ECO:0000244|PDB:5MZ4}.
SEQUENCE 3898 AA; 438578 MW; 2C1F17B8A359D0F6 CRC64;
MELNHFELLY KTSKQKPVGV EEPVYDTAGR PLFGNPSEVH PQSTLKLPHD RGRGDIRTTL
RDLPRKGDCR SGNHLGPVSG IYIKPGPVYY QDYTGPVYHR APLEFFDEAQ FCEVTKRIGR
VTGSDGKLYH IYVCVDGCIL LKLAKRGTPR TLKWIRNFTN CPLWVTSCSD DGASGSKDKK
PDRMNKGKLK IAPREHEKDS KTKPPDATIV VEGVKYQIKK KGKVKGKNTQ DGLYHNKNKP
PESRKKLEKA LLAWAVITIL LYQPVAAENI TQWNLSDNGT NGIQRAMYLR GVNRSLHGIW
PEKICKGVPT HLATDTELKE IRGMMDASER TNYTCCRLQR HEWNKHGWCN WYNIDPWIQL
MNRTQTNLTE GPPDKECAVT CRYDKNTDVN VVTQARNRPT TLTGCKKGKN FSFAGTVIEG
PCNFNVSVED ILYGDHECGS LLQDTALYLL DGMTNTIENA RQGAARVTSW LGRQLSTAGK
KLERRSKTWF GAYALSPYCN VTRKIGYIWY TNNCTPACLP KNTKIIGPGK FDTNAEDGKI
LHEMGGHLSE FLLLSLVILS DFAPETASTL YLILHYAIPQ SHEEPEGCDT NQLNLTVKLR
TEDVVPSSVW NIGKYVCVRP DWWPYETKVA LLFEEAGQVI KLVLRALRDL TRVWNSASTT
AFLICLIKVL RGQVVQGIIW LLLVTGAQGR LACKEDYRYA ISSTNEIGLL GAEGLTTTWK
EYSHGLQLDD GTVKAVCTAG SFKVTALNVV SRRYLASLHK RALPTSVTFE LLFDGTNPAI
EEMDDDFGFG LCPFDTSPVI KGKYNTTLLN GSAFYLVCPI GWTGVVECTA VSPTTLRTEV
VKTFRRDKPF PHRVDCVTTI VEKEDLFHCK LGGNWTCVKG DPVTYKGGQV KQCRWCGFEF
KEPYGLPHYP IGKCILTNET GYRVVDSTDC NRDGVVISTE GEHECLIGNT TVKVHALDER
LGPMPCRPKE IVSSEGPVRK TSCTFNYTKT LRNKYYEPRD SYFQQYMLKG EYQYWFNLDV
TDHHTDYFAE FVVLVVVALL GGRYVLWLIV TYIILTEQLA AGLQLGQGEV VLIGNLITHT
DNEVVVYFLL LYLVIRDEPI KKWILLLFHA MTNNPVKTIT VALLMISGVA KGGKIDGGWQ
RQPVTSFDIQ LALAVVVVVV MLLAKRDPTT FPLVITVATL RTAKITNGFS TDLVIATVSA
ALLTWTYISD YYKYKTWLQY LVSTVTGIFL IRVLKGIGEL DLHAPTLPSH RPLFYILVYL
ISTAVVTRWN LDVAGLLLQC VPTLLMVFTM WADILTLILI LPTYELTKLY YLKEVKIGAE
RGWLWKTNYK RVNDIYEVDQ TSEGVYLFPS KQRTSAITST MLPLIKAILI SCISNKWQLI
YLLYLIFEVS YYLHKKVIDE IAGGTNFVSR LVAALIEVNW AFDNEEVKGL KKFFLLSSRV
KELIIKHKVR NEVVVRWFGD EEIYGMPKLI GLVKAATLSR NKHCMLCTVC EDRDWRGETC
PKCGRFGPPV VCGMTLADFE EKHYKRIFIR EDQSGGPLRE EHAGYLQYKA RGQLFLRNLP
VLATKVKMLL VGNLGTEIGD LEHLGWVLRG PAVCKKVTEH ERCTTSIMDK LTAFFGVMPR
GTTPRAPVRF PTSLLKIRRG LETGWAYTHQ GGISSVDHVT CGKDLLVCDT MGRTRVVCQS
NNKMTDESEY GVKTDSGCPE GARCYVFNPE AVNISGTKGA MVHLQKTGGE FTCVTASGTP
AFFDLKNLKG WSGLPIFEAS SGRVVGRVKV GKNEDSKPTK LMSGIQTVSK SATDLTEMVK
KITTMNRGEF RQITLATGAG KTTELPRSVI EEIGRHKRVL VLIPLRAAAE SVYQYMRQKH
PSIAFNLRIG EMKEGDMATG ITYASYGYFC QMSQPKLRAA MVEYSFIFLD EYHCATPEQL
AIMGKIHRFS ENLRVVAMTA TPAGTVTTTG QKHPIEEFIA PEVMKGEDLG SEYLDIAGLK
IPVEEMKNNM LVFVPTRNMA VEAAKKLKAK GYNSGYYYSG EDPSNLRVVT SQSPYVVVAT
NAIESGVTLP DLDVVVDTGL KCEKRIRLSP KMPFIVTGLK RMAVTIGEQA QRRGRVGRVK
PGRYYRSQET PVGSKDYHYD LLQAQRYGIE DGINITKSFR EMNYDWSLYE EDSLMITQLE
ILNNLLISEE LPMAVKNIMA RTDHPEPIQL AYNSYETQVP VLFPKIRNGE VTDTYDNYTF
LNARKLGDDV PPYVYATEDE DLAVELLGLD WPDPGNQGTV EAGRALKQVV GLSTAENALL
VALFGYVGYQ ALSKRHIPVV TDIYSVEDHR LEDTTHLQYA PNAIKTEGKE TELKELAQGD
VQRCVEAVTN YAREGIQFMK SQALKVRETP TYKETMNTVA DYVKKFIEAL TDSKEDIIKY
GLWGAHTALY KSIGARLGHE TAFATLVVKW LAFGGESISD HIKQAATDLV VYYIINRPQF
PGDTETQQEG RKFVASLLVS ALATYTYKSW NYNNLSKIVE PALATLPYAA KALKLFAPTR
LESVVILSTA IYKTYLSIRR GKSDGLLGTG VSAAMEIMSQ NPVSVGIAVM LGVGAVAAHN
AIEASEQKRT LLMKVFVKNF LDQAATDELV KESPEKIIMA LFEAVQTVGN PLRLVYHLYG
VFYKGWEAKE LAQRTAGRNL FTLIMFEAVE LLGVDSEGKI RQLSSNYILE LLYKFRDNIK
SSVREIAISW APAPFSCDWT PTDDRIGLPH ENYLRVETKC PCGYRMKAVK NCAGELRLLE
EGGSFLCRNK FGRGSQNYRV TKYYDDNLSE IKPVIRMEGH VELYYKGATI KLDFNNSKTV
LATDKWEVDH STLVRALKRY TGAGYRGAYL GEKPNHKHLI QRDCATITKD KVCFIKMKRG
CAFTYDLSLH NLTRLIELVH KNNLEDREIP AVTVTTWLAY TFVNEDIGTI KPTFGEKVTP
EKQEEVVLQP AVVVDTTDVA VTVVGETSTM TTGETPTTFT SLGSDSKVRQ VLKLGVDDGQ
YPGPNQQRAS LLEAIQGVDE RPSVLILGSD KATSNRVKTA KNVKIYRSRD PLELREMMKR
GKILVVALSR VDTALLKFVD YKGTFLTRET LEALSLGKPK KRDITKAEAQ WLLRLEDQIE
ELPDWFAAKE PIFLEANIKR DKYHLVGDIA TIKEKAKQLG ATDSTKISKE VGAKVYSMKL
SNWVIQEENK QGSLAPLFEE LLQQCPPGGQ NKTTHMVSAY QLAQGNWVPV SCHVFMGTIP
ARRTKTHPYE AYVKLRELVD EHKMKALCGG SGLSKHNEWV IGKVKYQGNL RTKHMLNPGK
VAEQLHREGY RHNVYNKTIG SVMTATGIRL EKLPVVRAQT DTTNFHQAIR DKIDKEENLQ
TPGLHKKLME VFNALKRPEL EASYDAVDWE ELERGINRKG AAGFFERKNI GEVLDSEKNK
VEEVIDSLKK GRNIRYYETA IPKNEKRDVN DDWTAGDFVD EKKPRVIQYP EAKTRLAITK
VMYKWVKQKP VVIPGYEGKT PLFQIFDKVK KEWDQFQNPV AVSFDTKAWD TQVTTRDLEL
IRDIQKFYFK KKWHKFIDTL TKHMSEVPVI SADGEVYIRK GQRGSGQPDT SAGNSMLNVL
TMVYAFCEAT GVPYKSFDRV AKIHVCGDDG FLITERALGE KFASKGVQIL YEAGKPQKIT
EGDKMKVAYQ FDDIEFCSHT PVQVRWSDNT SSYMPGRNTT TILAKMATRL DSSGERGTIA
YEKAVAFSFL LMYSWNPLIR RICLLVLSTE LQVRPGKSTT YYYEGDPISA YKEVIGHNLF
DLKRTSFEKL AKLNLSMSTL GVWTRHTSKR LLQDCVNVGT KEGNWLVNAD RLVSSKTGNR
YIPGEGHTLQ GKHYEELILA RKPIGNFEGT DRYNLGPIVN VVLRRLKIMM MALIGRGV


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