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Database: UniProt
Entry: P19712
LinkDB: P19712
Original site: P19712 
ID   POLG_CSFVA              Reviewed;        3898 AA.
AC   P19712;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=N-terminal protease;
DE              Short=N-pro;
DE              EC=3.4.22.-;
DE     AltName: Full=Autoprotease p20;
DE   Contains:
DE     RecName: Full=Capsid protein C;
DE     AltName: Full=Core protein;
DE   Contains:
DE     RecName: Full=E(rns) glycoprotein;
DE     AltName: Full=gp44/48;
DE   Contains:
DE     RecName: Full=Envelope glycoprotein E1;
DE     AltName: Full=gp33;
DE   Contains:
DE     RecName: Full=Envelope glycoprotein E2;
DE     AltName: Full=gp55;
DE   Contains:
DE     RecName: Full=Viroporin p7 {ECO:0000303|PubMed:22496228};
DE   Contains:
DE     RecName: Full=Non-structural protein 2-3;
DE              Short=NS2-3;
DE   Contains:
DE     RecName: Full=Cysteine protease NS2;
DE              EC=3.4.22.-;
DE     AltName: Full=Non-structural protein 2;
DE   Contains:
DE     RecName: Full=Serine protease NS3;
DE              EC=3.4.21.113;
DE              EC=3.6.1.15;
DE              EC=3.6.4.13;
DE     AltName: Full=Non-structural protein 3;
DE   Contains:
DE     RecName: Full=Non-structural protein 4A;
DE              Short=NS4A;
DE   Contains:
DE     RecName: Full=Non-structural protein 4B;
DE              Short=NS4B;
DE   Contains:
DE     RecName: Full=Non-structural protein 5A;
DE              Short=NS5A;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48;
DE     AltName: Full=NS5B;
OS   Classical swine fever virus (strain Alfort) (CSFV) (Hog cholera virus).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Pestivirus; Pestivirus suis.
OX   NCBI_TaxID=11097;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2763466; DOI=10.1016/0042-6822(89)90625-9;
RA   Meyers G., Ruemenapf T., Thiel H.-J.;
RT   "Molecular cloning and nucleotide sequence of the genome of hog cholera
RT   virus.";
RL   Virology 171:555-567(1989).
RN   [2]
RP   SEQUENCE REVISION TO 2731.
RA   Meyers G.;
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 169-178; 268-291; 495-518 AND 690-713, AND PROTEOLYTIC
RP   PROCESSING OF POLYPROTEIN (GENOME POLYPROTEIN).
RX   PubMed=8388499; DOI=10.1128/jvi.67.6.3288-3294.1993;
RA   Ruemenapf T., Unger G., Strauss J.H., Thiel H.-J.;
RT   "Processing of the envelope glycoproteins of pestiviruses.";
RL   J. Virol. 67:3288-3294(1993).
RN   [4]
RP   SUBUNIT (ENVELOPE GLYCOPROTEIN E1), AND SUBUNIT (ENVELOPE GLYCOPROTEIN E2).
RX   PubMed=2370675; DOI=10.1128/jvi.64.8.3563-3569.1990;
RA   Weiland E., Stark R., Haas B., Ruemenapf T., Meyers G., Thiel H.J.;
RT   "Pestivirus glycoprotein which induces neutralizing antibodies forms part
RT   of a disulfide-linked heterodimer.";
RL   J. Virol. 64:3563-3569(1990).
RN   [5]
RP   SUBUNIT (E(RNS) GLYCOPROTEIN), AND GLYCOSYLATION (E(RNS) GLYCOPROTEIN).
RX   PubMed=1870198; DOI=10.1128/jvi.65.9.4705-4712.1991;
RA   Thiel H.-J., Stark R., Weiland E., Ruemenapf T., Meyers G.;
RT   "Hog cholera virus: molecular composition of virions from a pestivirus.";
RL   J. Virol. 65:4705-4712(1991).
RN   [6]
RP   PROTEOLYTIC PROCESSING (GENOME POLYPROTEIN).
RX   PubMed=8230432; DOI=10.1128/jvi.67.12.7088-7095.1993;
RA   Stark R., Meyers G., Ruemenapf T., Thiel H.-J.;
RT   "Processing of pestivirus polyprotein: cleavage site between autoprotease
RT   and nucleocapsid protein of classical swine fever virus.";
RL   J. Virol. 67:7088-7095(1993).
RN   [7]
RP   FUNCTION (E(RNS) GLYCOPROTEIN).
RX   PubMed=8356450; DOI=10.1126/science.8356450;
RA   Schneider R., Unger G., Stark R., Schneider-Scherzer E., Thiel H.J.;
RT   "Identification of a structural glycoprotein of an RNA virus as a
RT   ribonuclease.";
RL   Science 261:1169-1171(1993).
RN   [8]
RP   ACTIVE SITE (N-TERMINAL PROTEASE), AND MUTAGENESIS OF GLU-22; HIS-40;
RP   HIS-49; CYS-69; HIS-99; CYS-112; HIS-130; CYS-134; CYS-138 AND CYS-161.
RX   PubMed=9499122; DOI=10.1128/jvi.72.3.2544-2547.1998;
RA   Ruemenapf T., Stark R., Heimann M., Thiel H.-J.;
RT   "N-terminal protease of pestiviruses: identification of putative catalytic
RT   residues by site-directed mutagenesis.";
RL   J. Virol. 72:2544-2547(1998).
RN   [9]
RP   INDUCTION.
RX   PubMed=9573242; DOI=10.1128/jvi.72.6.4775-4782.1998;
RA   Sizova D.V., Kolupaeva V.G., Pestova T.V., Shatsky I.N., Hellen C.U.;
RT   "Specific interaction of eukaryotic translation initiation factor 3 with
RT   the 5' nontranslated regions of hepatitis C virus and classical swine fever
RT   virus RNAs.";
RL   J. Virol. 72:4775-4782(1998).
RN   [10]
RP   FUNCTION (CAPSID PROTEIN C).
RX   PubMed=9617770; DOI=10.1016/s0168-1702(97)00132-9;
RA   Liu J.J., Wong M.L., Chang T.J.;
RT   "The recombinant nucleocapsid protein of classical swine fever virus can
RT   act as a transcriptional regulator.";
RL   Virus Res. 53:75-80(1998).
RN   [11]
RP   SUBCELLULAR LOCATION (E(RNS) GLYCOPROTEIN), AND SUBCELLULAR LOCATION
RP   (ENVELOPE GLYCOPROTEIN E2).
RX   PubMed=10355762; DOI=10.1099/0022-1317-80-5-1157;
RA   Weiland F., Weiland E., Unger G., Saalmuller A., Thiel H.-J.;
RT   "Localization of pestiviral envelope proteins E(rns) and E2 at the cell
RT   surface and on isolated particles.";
RL   J. Gen. Virol. 80:1157-1165(1999).
RN   [12]
RP   FUNCTION (ENVELOPE GLYCOPROTEIN E2).
RX   PubMed=10438869; DOI=10.1128/jvi.73.9.7787-7794.1999;
RA   Moser C., Stettler P., Tratschin J.D., Hofmann M.A.;
RT   "Cytopathogenic and noncytopathogenic RNA replicons of classical swine
RT   fever virus.";
RL   J. Virol. 73:7787-7794(1999).
RN   [13]
RP   FUNCTION (ENVELOPE GLYCOPROTEIN E1), AND FUNCTION (ENVELOPE GLYCOPROTEIN
RP   E2).
RX   PubMed=15527858; DOI=10.1016/j.virol.2004.09.023;
RA   Wang Z., Nie Y., Wang P., Ding M., Deng H.;
RT   "Characterization of classical swine fever virus entry by using pseudotyped
RT   viruses: E1 and E2 are sufficient to mediate viral entry.";
RL   Virology 330:332-341(2004).
RN   [14]
RP   BIOPHYSICOCHEMICAL PROPERTIES (E(RNS) GLYCOPROTEIN), AND FUNCTION (E(RNS)
RP   GLYCOPROTEIN).
RX   PubMed=15113930; DOI=10.1128/jvi.78.10.5507-5512.2004;
RA   Hausmann Y., Roman-Sosa G., Thiel H.J., Ruemenapf T.;
RT   "Classical swine fever virus glycoprotein E rns is an endoribonuclease with
RT   an unusual base specificity.";
RL   J. Virol. 78:5507-5512(2004).
RN   [15]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 2-3), AND FUNCTION (NON-STRUCTURAL PROTEIN
RP   4A).
RX   PubMed=17482232; DOI=10.1016/j.virol.2007.03.056;
RA   Moulin H.R., Seuberlich T., Bauhofer O., Bennett L.C., Tratschin J.D.,
RA   Hofmann M.A., Ruggli N.;
RT   "Nonstructural proteins NS2-3 and NS4A of classical swine fever virus:
RT   essential features for infectious particle formation.";
RL   Virology 365:376-389(2007).
RN   [16]
RP   FUNCTION (N-TERMINAL PROTEASE), INTERACTION WITH HOST IRF3 (N-TERMINAL
RP   PROTEASE), AND SUBCELLULAR LOCATION (N-TERMINAL PROTEASE).
RX   PubMed=17215286; DOI=10.1128/jvi.02032-06;
RA   Bauhofer O., Summerfield A., Sakoda Y., Tratschin J.D., Hofmann M.A.,
RA   Ruggli N.;
RT   "Classical swine fever virus Npro interacts with interferon regulatory
RT   factor 3 and induces its proteasomal degradation.";
RL   J. Virol. 81:3087-3096(2007).
RN   [17]
RP   FUNCTION (E(RNS) GLYCOPROTEIN), MUTAGENESIS OF CYS-438, AND DISULFIDE BOND.
RX   PubMed=19264773; DOI=10.1128/jvi.01710-08;
RA   Tews B.A., Schuermann E.M., Meyers G.;
RT   "Mutation of cysteine 171 of pestivirus E rns RNase prevents homodimer
RT   formation and leads to attenuation of classical swine fever virus.";
RL   J. Virol. 83:4823-4834(2009).
RN   [18]
RP   FUNCTION (E(RNS) GLYCOPROTEIN).
RX   PubMed=19767841; DOI=10.1139/w09-013;
RA   Luo X., Ling D., Li T., Wan C., Zhang C., Pan Z.;
RT   "Classical swine fever virus Erns glycoprotein antagonizes induction of
RT   interferon-beta by double-stranded RNA.";
RL   Can. J. Microbiol. 55:698-704(2009).
RN   [19]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 3), INTERACTION WITH RNA-DIRECTED RNA
RP   POLYMERASE (NON-STRUCTURAL PROTEIN 3), AND INTERACTION WITH NON-STRUCTURAL
RP   PROTEIN 3 (RNA-DIRECTED RNA POLYMERASE).
RX   PubMed=19185595; DOI=10.1016/j.virusres.2008.12.014;
RA   Wen G., Xue J., Shen Y., Zhang C., Pan Z.;
RT   "Characterization of classical swine fever virus (CSFV) nonstructural
RT   protein 3 (NS3) helicase activity and its modulation by CSFV RNA-dependent
RT   RNA polymerase.";
RL   Virus Res. 141:63-70(2009).
RN   [20]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 5A).
RX   PubMed=22261205; DOI=10.1016/j.virusres.2012.01.004;
RA   Sheng C., Chen Y., Xiao J., Xiao J., Wang J., Li G., Chen J., Xiao M.;
RT   "Classical swine fever virus NS5A protein interacts with 3'-untranslated
RT   region and regulates viral RNA synthesis.";
RL   Virus Res. 163:636-643(2012).
RN   [21]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 5A), INTERACTION WITH RNA-DIRECTED RNA
RP   POLYMERASE (NON-STRUCTURAL PROTEIN 5A), AND INTERACTION WITH NON-STRUCTURAL
RP   PROTEIN 5A (RNA-DIRECTED RNA POLYMERASE).
RX   PubMed=22795973; DOI=10.1016/j.virol.2012.04.014;
RA   Chen Y., Xiao J., Xiao J., Sheng C., Wang J., Jia L., Zhi Y., Li G.,
RA   Chen J., Xiao M.;
RT   "Classical swine fever virus NS5A regulates viral RNA replication through
RT   binding to NS5B and 3'UTR.";
RL   Virology 432:376-388(2012).
RN   [22]
RP   FUNCTION (VIROPORIN P7).
RX   PubMed=22496228; DOI=10.1128/jvi.00560-12;
RA   Gladue D.P., Holinka L.G., Largo E., Fernandez Sainz I., Carrillo C.,
RA   O'Donnell V., Baker-Branstetter R., Lu Z., Ambroggio X., Risatti G.R.,
RA   Nieva J.L., Borca M.V.;
RT   "Classical swine fever virus p7 protein is a viroporin involved in
RT   virulence in swine.";
RL   J. Virol. 86:6778-6791(2012).
RN   [23]
RP   ACTIVE SITE (N-TERMINAL PROTEASE), AND FUNCTION (N-TERMINAL PROTEASE).
RX   PubMed=24606708; DOI=10.1016/j.virol.2014.01.026;
RA   Gottipati K., Acholi S., Ruggli N., Choi K.H.;
RT   "Autocatalytic activity and substrate specificity of the pestivirus N-
RT   terminal protease Npro.";
RL   Virology 452:303-309(2014).
RN   [24]
RP   INTERACTION WITH HOST OS9 (CAPSID PROTEIN C).
RX   PubMed=25010283; DOI=10.1016/j.virol.2014.05.008;
RA   Gladue D.P., O'Donnell V., Fernandez-Sainz I.J., Fletcher P.,
RA   Baker-Branstetter R., Holinka L.G., Sanford B., Carlson J., Lu Z.,
RA   Borca M.V.;
RT   "Interaction of structural core protein of classical swine fever virus with
RT   endoplasmic reticulum-associated degradation pathway protein OS9.";
RL   Virology 460:173-179(2014).
RN   [25]
RP   FUNCTION (VIROPORIN P7).
RX   PubMed=24189547; DOI=10.1016/j.antiviral.2013.10.015;
RA   Largo E., Gladue D.P., Huarte N., Borca M.V., Nieva J.L.;
RT   "Pore-forming activity of pestivirus p7 in a minimal model system supports
RT   genus-specific viroporin function.";
RL   Antiviral Res. 101:30-36(2014).
RN   [26]
RP   INTERACTION WITH HOST TRX2 (ENVELOPE GLYCOPROTEIN E2).
RX   PubMed=26041303; DOI=10.1128/jvi.00429-15;
RA   Li S., Wang J., He W.R., Feng S., Li Y., Wang X., Liao Y., Qin H.Y.,
RA   Li L.F., Dong H., Sun Y., Luo Y., Qiu H.J.;
RT   "Thioredoxin 2 Is a Novel E2-Interacting Protein That Inhibits the
RT   Replication of Classical Swine Fever Virus.";
RL   J. Virol. 89:8510-8524(2015).
RN   [27]
RP   INTERACTION WITH HOST RPSA (E(RNS) GLYCOPROTEIN), AND FUNCTION (E(RNS)
RP   GLYCOPROTEIN).
RX   PubMed=25694590; DOI=10.1128/jvi.00019-15;
RA   Chen J., He W.R., Shen L., Dong H., Yu J., Wang X., Yu S., Li Y., Li S.,
RA   Luo Y., Sun Y., Qiu H.J.;
RT   "The laminin receptor is a cellular attachment receptor for classical Swine
RT   Fever virus.";
RL   J. Virol. 89:4894-4906(2015).
RN   [28]
RP   FUNCTION (N-TERMINAL PROTEASE), AND INTERACTION WITH HOST IRF3 (N-TERMINAL
RP   PROTEASE).
RX   PubMed=27334592; DOI=10.1128/jvi.00318-16;
RA   Gottipati K., Holthauzen L.M., Ruggli N., Choi K.H.;
RT   "Pestivirus Npro Directly Interacts with Interferon Regulatory Factor 3
RT   Monomer and Dimer.";
RL   J. Virol. 90:7740-7747(2016).
RN   [29]
RP   FUNCTION (CAPSID PROTEIN C), AND SUBCELLULAR LOCATION (CAPSID PROTEIN C).
RX   PubMed=28290554; DOI=10.1038/srep44459;
RA   Riedel C., Lamp B., Hagen B., Indik S., Ruemenapf T.;
RT   "The core protein of a pestivirus protects the incoming virus against IFN-
RT   induced effectors.";
RL   Sci. Rep. 7:44459-44459(2017).
RN   [30]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 3), AND INTERACTION WITH HOST TRAF6
RP   (NON-STRUCTURAL PROTEIN 3).
RC   STRAIN=Shimen;
RX   PubMed=28751780; DOI=10.1038/s41598-017-06934-1;
RA   Lv H., Dong W., Cao Z., Li X., Wang J., Qian G., Lv Q., Wang C., Guo K.,
RA   Zhang Y.;
RT   "TRAF6 is a novel NS3-interacting protein that inhibits classical swine
RT   fever virus replication.";
RL   Sci. Rep. 7:6737-6737(2017).
RN   [31]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 4B), INTERACTION WITH HOST RAB5
RP   (NON-STRUCTURAL PROTEIN 4B), SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN
RP   4B), SUBCELLULAR LOCATION (SERINE PROTEASE NS3), AND SUBCELLULAR LOCATION
RP   (NON-STRUCTURAL PROTEIN 5A).
RX   PubMed=28848503; DOI=10.3389/fmicb.2017.01468;
RA   Lin J., Wang C., Zhang L., Wang T., Zhang J., Liang W., Li C., Qian G.,
RA   Ouyang Y., Guo K., Zhang Y.;
RT   "Rab5 Enhances Classical Swine Fever Virus Proliferation and Interacts with
RT   Viral NS4B Protein to Facilitate Formation of NS4B Related Complex.";
RL   Front. Microbiol. 8:1468-1468(2017).
RN   [32]
RP   FUNCTION (E(RNS) GLYCOPROTEIN), AND SUBUNIT (E(RNS) GLYCOPROTEIN).
RX   PubMed=29235980; DOI=10.1099/jgv.0.000990;
RA   Tucakov A.K., Yavuz S., Schuermann E.M., Mischler M., Klingebeil A.,
RA   Meyers G.;
RT   "dimerization via pseudoreversion partially restores virulence of classical
RT   swine fever virus.";
RL   J. Gen. Virol. 99:86-96(2018).
RN   [33]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 4B), INTERACTION WITH HOST FTH1
RP   (NON-STRUCTURAL PROTEIN 4B), AND SUBCELLULAR LOCATION (NON-STRUCTURAL
RP   PROTEIN 4B).
RX   PubMed=29844394; DOI=10.1038/s41598-018-26777-8;
RA   Qian G., Lv H., Lin J., Li X., Lv Q., Wang T., Zhang J., Dong W., Guo K.,
RA   Zhang Y.;
RT   "FHC, an NS4B-interacting Protein, Enhances Classical Swine Fever Virus
RT   Propagation and Acts Positively in Viral Anti-apoptosis.";
RL   Sci. Rep. 8:8318-8318(2018).
RN   [34]
RP   INTERACTION WITH HOST RSAD2 (NON-STRUCTURAL PROTEIN 5A).
RX   PubMed=31517388; DOI=10.1002/jmv.25595;
RA   Xu C., Feng L., Chen P., Li A., Guo S., Jiao X., Zhang C., Zhao Y., Jin X.,
RA   Zhong K., Guo Y., Zhu H., Han L., Yang G., Li H., Wang Y.;
RT   "Viperin inhibits classical swine fever virus replication by interacting
RT   with viral nonstructural 5A protein.";
RL   J. Med. Virol. 92:149-160(2020).
RN   [35]
RP   FUNCTION (ENVELOPE GLYCOPROTEIN E2), AND INTERACTION WITH HOST ADAM17
RP   (ENVELOPE GLYCOPROTEIN E2).
RX   PubMed=33684175; DOI=10.1371/journal.ppat.1009393;
RA   Yuan F., Li D., Li C., Zhang Y., Song H., Li S., Deng H., Gao G.F.,
RA   Zheng A.;
RT   "ADAM17 is an essential attachment factor for classical swine fever
RT   virus.";
RL   PLoS Pathog. 17:e1009393-e1009393(2021).
RN   [36]
RP   X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 1782-2280.
RX   PubMed=25653438; DOI=10.1128/jvi.03165-14;
RA   Tortorici M.A., Duquerroy S., Kwok J., Vonrhein C., Perez J., Lamp B.,
RA   Bricogne G., Ruemenapf T., Vachette P., Rey F.A.;
RT   "X-ray structure of the pestivirus NS3 helicase and its conformation in
RT   solution.";
RL   J. Virol. 89:4356-4371(2015).
RN   [37]
RP   X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 1590-2280, AND INTERACTION WITH
RP   NS4A (SERINE PROTEASE NS3).
RX   PubMed=28151973; DOI=10.1371/journal.ppat.1006134;
RA   Dubrau D., Tortorici M.A., Rey F.A., Tautz N.;
RT   "A positive-strand RNA virus uses alternative protein-protein interactions
RT   within a viral protease/cofactor complex to switch between RNA replication
RT   and virion morphogenesis.";
RL   PLoS Pathog. 13:E1006134-E1006134(2017).
CC   -!- FUNCTION: [N-terminal protease]: Leader cysteine autoprotease that
CC       cleaves itself from the nascent polyprotein during translation of the
CC       viral mRNA. Once released, plays a role in the inhibition of host
CC       innate immune response by interacting with host IRF3 and inducing its
CC       proteasomal degradation. {ECO:0000269|PubMed:17215286,
CC       ECO:0000269|PubMed:24606708, ECO:0000269|PubMed:27334592}.
CC   -!- FUNCTION: [Capsid protein C]: Packages viral RNA to form a viral
CC       nucleocapsid and thereby protects viral RNA. Also plays a role in
CC       transcription regulation. Protects the incoming virus against IFN-
CC       induced effectors. {ECO:0000269|PubMed:28290554,
CC       ECO:0000269|PubMed:9617770}.
CC   -!- FUNCTION: [E(rns) glycoprotein]: Plays a role in viral entry. Interacts
CC       with host RPSA that acts as a cellular attachment receptor for the
CC       virus. Possesses also intrinsic ribonuclease (RNase) activity that can
CC       inhibit the production of type I interferon and assist in the
CC       development of persistent infections. Cleaves preferentially NpU bonds
CC       (PubMed:15113930). {ECO:0000269|PubMed:15113930,
CC       ECO:0000269|PubMed:19264773, ECO:0000269|PubMed:19767841,
CC       ECO:0000269|PubMed:25694590, ECO:0000269|PubMed:29235980,
CC       ECO:0000269|PubMed:8356450}.
CC   -!- FUNCTION: [Envelope glycoprotein E1]: Plays a role in cell attachment
CC       and subsequent fusion of viral and cellular membranes. Therefore,
CC       mediates together with envelope glycoprotein E2 the viral entry.
CC       {ECO:0000269|PubMed:15527858}.
CC   -!- FUNCTION: [Envelope glycoprotein E2]: Plays a role in cell attachment
CC       and subsequent fusion of viral and cellular membranes
CC       (PubMed:15527858). Therefore, mediates together with envelope
CC       glycoprotein E1 the viral entry (PubMed:15527858). Binds to host ADAM17
CC       receptor for entry (PubMed:33684175). {ECO:0000269|PubMed:15527858,
CC       ECO:0000269|PubMed:33684175}.
CC   -!- FUNCTION: [Viroporin p7]: Plays an essential role in the virus
CC       replication cycle by acting as a viroporin. Forms ion conductive pores,
CC       which alters the cell permeability allowing the transport of ions and
CC       other small molecules. {ECO:0000269|PubMed:22496228,
CC       ECO:0000269|PubMed:24189547}.
CC   -!- FUNCTION: [Non-structural protein 2-3]: Autoprotease that associates
CC       with the host chaperone JIV and cleaves the NS2-3 protein between NS2
CC       and NS3. Also plays a role in the formation of infectious particles.
CC       {ECO:0000269|PubMed:17482232}.
CC   -!- FUNCTION: [Cysteine protease NS2]: Plays a role in the regulation of
CC       viral RNA replication. {ECO:0000269|PubMed:10438869}.
CC   -!- FUNCTION: [Serine protease NS3]: Multifunctional protein that contains
CC       an N-terminal protease and a C-terminal helicase, playing essential
CC       roles in viral polyprotein processing and viral genome replication. The
CC       chymotrypsin-like serine protease activity utilizes NS4A as an
CC       essential cofactor and catalyzes the cleavage of the polyprotein
CC       leading to the release of NS4A, NS4B, NS5A, and NS5B. Plays a role in
CC       the inhibition of host NF-kappa-B activation by interacting with and
CC       inhibiting host TRAF6. Interacts with NS5B to enhance RNA-dependent RNA
CC       polymerase activity. {ECO:0000269|PubMed:19185595,
CC       ECO:0000269|PubMed:28751780}.
CC   -!- FUNCTION: [Non-structural protein 4A]: Acts as a cofactor for the NS3
CC       protease activity. {ECO:0000269|PubMed:17482232}.
CC   -!- FUNCTION: [Non-structural protein 4B]: Induces a specific membrane
CC       alteration that serves as a scaffold for the virus replication complex
CC       (By similarity). Antagonizes host cell apoptosis by interacting with
CC       host ferritin heavy chain. The ORF4 protein physically binds host
CC       FTH1/FHC, resulting in the reduction of FTH1 protein levels in host
CC       cells. Reduction of FTH1 concentration further inhibits the
CC       accumulation of reactive oxygen in host cells, leading to reduced
CC       apoptosis (PubMed:29844394) (By similarity).
CC       {ECO:0000250|UniProtKB:O56125, ECO:0000250|UniProtKB:Q9Q6P4,
CC       ECO:0000269|PubMed:29844394}.
CC   -!- FUNCTION: [Non-structural protein 5A]: Regulates viral RNA replication
CC       by interacting with the 3'-untranslated region of viral RNA in a dose-
CC       dependent manner. At small concentrations promotes viral synthesis by
CC       interacting with the polymerase NS5B while at large concentrations,
CC       inhibits replication. {ECO:0000269|PubMed:22261205,
CC       ECO:0000269|PubMed:22795973}.
CC   -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral (+) and
CC       (-) genome. {ECO:0000255|PROSITE-ProRule:PRU00539}.
CC   -!- CATALYTIC ACTIVITY: [Serine protease NS3]:
CC       Reaction=Leu is conserved at position P1 for all four cleavage sites.
CC         Alanine is found at position P1' of the NS4A-NS4B cleavage site,
CC         whereas serine is found at position P1' of the NS3-NS4A, NS4B-NS5A
CC         and NS5A-NS5B cleavage sites.; EC=3.4.21.113;
CC   -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY: [Serine protease NS3]:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC   -!- CATALYTIC ACTIVITY: [Serine protease NS3]:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=84 uM for Sub-UpU {ECO:0000269|PubMed:15113930};
CC         KM=103 uM for Sub-GpU {ECO:0000269|PubMed:15113930};
CC         KM=220 uM for Sub-CpU {ECO:0000269|PubMed:15113930};
CC         KM=259 uM for Sub-ApU {ECO:0000269|PubMed:15113930};
CC   -!- SUBUNIT: [N-terminal protease]: Interacts with host IRF3.
CC       {ECO:0000269|PubMed:17215286, ECO:0000269|PubMed:27334592}.
CC   -!- SUBUNIT: [Capsid protein C]: Interacts with host OS9 (PubMed:25010283).
CC       {ECO:0000269|PubMed:25010283}.
CC   -!- SUBUNIT: [E(rns) glycoprotein]: Homodimer; disulfide-linked
CC       (PubMed:29235980, PubMed:1870198). Interacts with host RPSA
CC       (PubMed:25694590). {ECO:0000269|PubMed:1870198,
CC       ECO:0000269|PubMed:25694590, ECO:0000269|PubMed:29235980}.
CC   -!- SUBUNIT: [Envelope glycoprotein E1]: Homodimer; disulfide-linked
CC       (PubMed:2370675). Heterodimer with E1; disulfide-linked
CC       (PubMed:2370675). {ECO:0000269|PubMed:2370675}.
CC   -!- SUBUNIT: [Envelope glycoprotein E2]: Homodimer; disulfide-linked
CC       (PubMed:2370675). Heterodimer with E1; disulfide-linked
CC       (PubMed:2370675). Interacts with host TRX2 (PubMed:26041303). Interacts
CC       with host receptor ADAM17 (via metalloproteinase domain); this
CC       interaction allows binding and probably entry of the virus into the
CC       host cell (PubMed:33684175). {ECO:0000269|PubMed:2370675,
CC       ECO:0000269|PubMed:26041303, ECO:0000269|PubMed:33684175}.
CC   -!- SUBUNIT: [Serine protease NS3]: Interacts with host TRAF6; this
CC       interaction inhibits host NF-kappa-B pathway. Interacts with NS5B; this
CC       interaction enhances RNA-dependent RNA polymerase activity. Interacts
CC       with protein NS4A. {ECO:0000305}.
CC   -!- SUBUNIT: [Non-structural protein 4B]: Interacts with host RAB5, this
CC       interaction facilitates the formation of NS4B-related complex
CC       (PubMed:28848503). Interacts with host FTH1; this interaction plays a
CC       positive role in viral anti-apoptosis (PubMed:29844394).
CC       {ECO:0000269|PubMed:28848503, ECO:0000269|PubMed:29844394}.
CC   -!- SUBUNIT: [Non-structural protein 5A]: Interacts with RNA-directed RNA
CC       polymerase (PubMed:22795973). Interacts with host RSAD2; this
CC       interaction inhibits viral replication (PubMed:31517388).
CC       {ECO:0000269|PubMed:22795973, ECO:0000269|PubMed:31517388}.
CC   -!- SUBUNIT: [RNA-directed RNA polymerase]: Interacts with NS5A; this
CC       interaction promotes viral replication. {ECO:0000269|PubMed:22795973,
CC       ECO:0000269|PubMed:31517388}.
CC   -!- INTERACTION:
CC       PRO_0000038050; Q08211: DHX9; Xeno; NbExp=6; IntAct=EBI-10901281, EBI-352022;
CC       PRO_0000038050; Q764M6: IRF3; Xeno; NbExp=4; IntAct=EBI-10901281, EBI-12512266;
CC       PRO_0000038050; P67809: YBX1; Xeno; NbExp=4; IntAct=EBI-10901281, EBI-354065;
CC       PRO_0000038060; A0A8D1U8F1; Xeno; NbExp=4; IntAct=EBI-12513719, EBI-12512146;
CC   -!- SUBCELLULAR LOCATION: [N-terminal protease]: Host cytoplasm
CC       {ECO:0000269|PubMed:17215286}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein C]: Virion
CC       {ECO:0000269|PubMed:28290554}.
CC   -!- SUBCELLULAR LOCATION: [E(rns) glycoprotein]: Host cell membrane
CC       {ECO:0000269|PubMed:28290554}; Peripheral membrane protein. Virion
CC       membrane {ECO:0000269|PubMed:28290554}; Peripheral membrane protein
CC       {ECO:0000305}. Note=The C-terminus membrane anchor of Erns represents
CC       an amphipathic helix embedded in plane into the membrane.
CC   -!- SUBCELLULAR LOCATION: [Envelope glycoprotein E2]: Host cell surface
CC       {ECO:0000269|PubMed:28290554}. Virion membrane
CC       {ECO:0000269|PubMed:28290554}.
CC   -!- SUBCELLULAR LOCATION: [Cysteine protease NS2]: Host membrane
CC       {ECO:0000255|PROSITE-ProRule:PRU01029}; Multi-pass membrane protein
CC       {ECO:0000255|PROSITE-ProRule:PRU01029}.
CC   -!- SUBCELLULAR LOCATION: [Serine protease NS3]: Host cytoplasm
CC       {ECO:0000269|PubMed:28848503}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host cytoplasm
CC       {ECO:0000269|PubMed:28848503, ECO:0000269|PubMed:29844394}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 5A]: Host cytoplasm
CC       {ECO:0000269|PubMed:28848503}.
CC   -!- INDUCTION: Translated cap independently from an internal ribosome entry
CC       site (IRES). {ECO:0000269|PubMed:9573242}.
CC   -!- PTM: [E(rns) glycoprotein]: Heavily glycosylated.
CC       {ECO:0000269|PubMed:1870198}.
CC   -!- PTM: The viral RNA of pestiviruses is expressed as a single polyprotein
CC       which undergoes post-translational proteolytic processing resulting in
CC       the production of at least eleven individual proteins. The N-terminal
CC       protease cleaves itself from the nascent polyprotein autocatalytically
CC       and thereby generates the N-terminus of the adjacent viral capsid
CC       protein C. {ECO:0000269|PubMed:8230432, ECO:0000269|PubMed:8388499}.
CC   -!- PTM: [Genome polyprotein]: Cleavage between E2 and p7 is partial.
CC   -!- SIMILARITY: Belongs to the pestivirus polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; J04358; AAA43844.2; -; Genomic_RNA.
DR   PDB; 4CBG; X-ray; 2.82 A; A/B/C/D=1782-2280.
DR   PDB; 4CBH; X-ray; 2.51 A; A/B/C/D=1782-2280.
DR   PDB; 4CBI; X-ray; 3.00 A; A/B/C/D=1782-2280.
DR   PDB; 4CBL; X-ray; 3.05 A; A/B/C/D=1792-2280.
DR   PDB; 4CBM; X-ray; 3.27 A; A/B/C/D=1782-2280.
DR   PDB; 5MZ4; X-ray; 3.05 A; A/B=1590-2280.
DR   PDBsum; 4CBG; -.
DR   PDBsum; 4CBH; -.
DR   PDBsum; 4CBI; -.
DR   PDBsum; 4CBL; -.
DR   PDBsum; 4CBM; -.
DR   PDBsum; 5MZ4; -.
DR   SMR; P19712; -.
DR   IntAct; P19712; 96.
DR   MEROPS; C53.001; -.
DR   MEROPS; S31.001; -.
DR   BRENDA; 3.4.21.113; 1439.
DR   Proteomes; UP000008568; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0033897; F:ribonuclease T2 activity; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR   GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0039707; P:virus-mediated pore formation in host cell membrane; IEA:UniProtKB-KW.
DR   CDD; cd17931; DEXHc_viral_Ns3; 1.
DR   CDD; cd23201; Pestivirus_RdRp; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 2.60.40.4200; Pestivirus envelope glycoprotein E2, C-terminal domain; 1.
DR   Gene3D; 2.60.320.20; Pestivirus envelope glycoprotein E2, domain A; 1.
DR   Gene3D; 2.60.40.3000; Pestivirus envelope glycoprotein E2, domain B; 1.
DR   Gene3D; 2.30.140.40; Pestivirus Npro endopeptidase C53, interaction domain; 1.
DR   Gene3D; 3.90.730.10; Ribonuclease T2-like; 1.
DR   InterPro; IPR021824; Capsid-C_pestivirus.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR011492; Flavi_DEAD.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR022120; NS2.
DR   InterPro; IPR030399; NS2_C74.
DR   InterPro; IPR049486; NS3-hel_C_flaviviridae.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008751; Peptidase_C53.
DR   InterPro; IPR042542; Peptidase_C53_interaction.
DR   InterPro; IPR032521; Pestivirus_E2.
DR   InterPro; IPR042309; Pestivirus_E2_A.
DR   InterPro; IPR042310; Pestivirus_E2_B.
DR   InterPro; IPR042311; Pestivirus_E2_D.
DR   InterPro; IPR000280; Pestivirus_NS3_S31.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR002166; RNA_pol_HCV.
DR   InterPro; IPR036430; RNase_T2-like_sf.
DR   InterPro; IPR033130; RNase_T2_His_AS_2.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF234; ATP-DEPENDENT RNA HELICASE DHX40-RELATED; 1.
DR   Pfam; PF11889; Capsid_pestivir; 1.
DR   Pfam; PF20907; Flav_NS3-hel_C; 1.
DR   Pfam; PF07652; Flavi_DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF05550; Peptidase_C53; 1.
DR   Pfam; PF12387; Peptidase_C74; 1.
DR   Pfam; PF05578; Peptidase_S31; 1.
DR   Pfam; PF16329; Pestivirus_E2; 1.
DR   Pfam; PF00998; RdRP_3; 1.
DR   PRINTS; PR00729; CDVENDOPTASE.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF55895; Ribonuclease Rh-like; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51692; PESTIVIRUS_NS2_PRO; 1.
DR   PROSITE; PS51535; PESTIVIRUS_NS3PRO; 1.
DR   PROSITE; PS51876; PV_NPRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS00531; RNASE_T2_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activation of host autophagy by virus; ATP-binding;
KW   Direct protein sequencing; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein; GTP-binding;
KW   Helicase; Host cell membrane; Host cytoplasm; Host membrane;
KW   Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host IRF3 by virus; Inhibition of host RLR pathway by virus;
KW   Ion channel; Ion transport; Membrane; Nuclease; Nucleotide-binding;
KW   Nucleotidyltransferase; Protease; RNA-directed RNA polymerase;
KW   Serine protease; Thiol protease; Transferase; Transmembrane;
KW   Transmembrane helix; Transport; Viral attachment to host cell;
KW   Viral attachment to host entry receptor; Viral immunoevasion;
KW   Viral ion channel; Viral penetration into host cytoplasm;
KW   Viral RNA replication; Virion; Virus entry into host cell.
FT   CHAIN           1..3898
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000450893"
FT   CHAIN           1..168
FT                   /note="N-terminal protease"
FT                   /id="PRO_0000038050"
FT   CHAIN           169..267
FT                   /note="Capsid protein C"
FT                   /id="PRO_0000038051"
FT   CHAIN           268..494
FT                   /note="E(rns) glycoprotein"
FT                   /id="PRO_0000038052"
FT   CHAIN           495..689
FT                   /note="Envelope glycoprotein E1"
FT                   /id="PRO_0000038053"
FT   CHAIN           690..1062
FT                   /note="Envelope glycoprotein E2"
FT                   /id="PRO_0000038054"
FT   CHAIN           1063..1132
FT                   /note="Viroporin p7"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038055"
FT   CHAIN           1133..2272
FT                   /note="Non-structural protein 2-3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038056"
FT   CHAIN           1133..1589
FT                   /note="Cysteine protease NS2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT                   /id="PRO_0000349361"
FT   CHAIN           1590..2272
FT                   /note="Serine protease NS3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038057"
FT   CHAIN           2273..2336
FT                   /note="Non-structural protein 4A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038058"
FT   CHAIN           2337..2683
FT                   /note="Non-structural protein 4B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038059"
FT   CHAIN           2684..3180
FT                   /note="Non-structural protein 5A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038060"
FT   CHAIN           3181..3898
FT                   /note="RNA-directed RNA polymerase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038061"
FT   TRANSMEM        1031..1051
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1070..1090
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1104..1124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1140..1164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT   TRANSMEM        1189..1209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT   TRANSMEM        1217..1237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT   TRANSMEM        1247..1267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT   TRANSMEM        1281..1301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT   TRANSMEM        1360..1380
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT   TRANSMEM        1568..1588
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT   DOMAIN          1..168
FT                   /note="Peptidase C53"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01224"
FT   DOMAIN          1441..1589
FT                   /note="Peptidase C74"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT   DOMAIN          1590..1763
FT                   /note="Peptidase S31"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT   DOMAIN          1802..1960
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1978..2179
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          3519..3642
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          32..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1910..1913
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   COMPBIAS        173..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        49
FT                   /note="For N-terminal protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01224,
FT                   ECO:0000269|PubMed:9499122"
FT   ACT_SITE        69
FT                   /note="For N-terminal protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01224,
FT                   ECO:0000269|PubMed:24606708, ECO:0000269|PubMed:9499122"
FT   ACT_SITE        1447
FT                   /note="For cysteine protease NS2 activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT   ACT_SITE        1461
FT                   /note="For cysteine protease NS2 activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT   ACT_SITE        1512
FT                   /note="For cysteine protease NS2 activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT   ACT_SITE        1658
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT   ACT_SITE        1695
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT   ACT_SITE        1752
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT   BINDING         1815..1822
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         3500
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P19711"
FT   BINDING         3502
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P19711"
FT   BINDING         3697
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P19711"
FT   BINDING         3705
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P19711"
FT   SITE            168..169
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01224"
FT   SITE            267..268
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000269|PubMed:8388499"
FT   SITE            297
FT                   /note="Hydrogen donor to release the cleavage products of
FT                   E(rns) glycoprotein RNase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q96662"
FT   SITE            494..495
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000269|PubMed:8388499"
FT   SITE            689..690
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000269|PubMed:8388499"
FT   SITE            759
FT                   /note="Serves as pH sensor to control fusion"
FT                   /evidence="ECO:0000250|UniProtKB:P19711"
FT   SITE            1062..1063
FT                   /note="Cleavage; by host signal peptidase; partial"
FT                   /evidence="ECO:0000250"
FT   SITE            1132..1133
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250"
FT   SITE            1589..1590
FT                   /note="Cleavage; partial; cysteine protease NS2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT   SITE            2272..2273
FT                   /note="Cleavage; by serine protease NS3"
FT                   /evidence="ECO:0000250"
FT   SITE            2336..2337
FT                   /note="Cleavage; by serine protease NS3"
FT                   /evidence="ECO:0000250"
FT   SITE            2683..2684
FT                   /note="Cleavage; by serine protease NS3"
FT                   /evidence="ECO:0000250"
FT   SITE            3180..3181
FT                   /note="Cleavage; by serine protease NS3"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        157
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        278
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        367
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        410
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        425
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        500
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        594
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        805
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        810
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        874
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        918
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        949
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        986
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1713
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2134
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2217
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2494
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2787
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2815
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2891
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3211
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3316
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3689
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3698
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3794
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        305..349
FT                   /evidence="ECO:0000250|UniProtKB:Q96662"
FT   DISULFID        335..336
FT                   /evidence="ECO:0000250|UniProtKB:Q96662"
FT   DISULFID        377..422
FT                   /evidence="ECO:0000250|UniProtKB:Q96662"
FT   DISULFID        381..405
FT                   /evidence="ECO:0000250|UniProtKB:Q96662"
FT   DISULFID        438
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305|PubMed:19264773"
FT   DISULFID        693..737
FT                   /evidence="ECO:0000250|UniProtKB:P19711"
FT   DISULFID        983
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P19711"
FT   VARIANT         387
FT                   /note="T -> A"
FT   VARIANT         3542
FT                   /note="R -> S"
FT   MUTAGEN         22
FT                   /note="E->V: Almost complete loss of cleavage between N-pro
FT                   and C."
FT                   /evidence="ECO:0000269|PubMed:9499122"
FT   MUTAGEN         40
FT                   /note="H->L: No effect."
FT                   /evidence="ECO:0000269|PubMed:9499122"
FT   MUTAGEN         49
FT                   /note="H->L: Complete loss of cleavage between N-pro and
FT                   C."
FT                   /evidence="ECO:0000269|PubMed:9499122"
FT   MUTAGEN         69
FT                   /note="C->A: Complete loss of cleavage between N-pro and
FT                   C."
FT                   /evidence="ECO:0000269|PubMed:9499122"
FT   MUTAGEN         69
FT                   /note="C->S: Complete loss of cleavage between N-pro and
FT                   C."
FT                   /evidence="ECO:0000269|PubMed:9499122"
FT   MUTAGEN         99
FT                   /note="H->L: No effect."
FT                   /evidence="ECO:0000269|PubMed:9499122"
FT   MUTAGEN         112
FT                   /note="C->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:9499122"
FT   MUTAGEN         112
FT                   /note="C->S: No effect."
FT                   /evidence="ECO:0000269|PubMed:9499122"
FT   MUTAGEN         130
FT                   /note="H->L: No effect."
FT                   /evidence="ECO:0000269|PubMed:9499122"
FT   MUTAGEN         134
FT                   /note="C->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:9499122"
FT   MUTAGEN         134
FT                   /note="C->S: No effect."
FT                   /evidence="ECO:0000269|PubMed:9499122"
FT   MUTAGEN         138
FT                   /note="C->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:9499122"
FT   MUTAGEN         138
FT                   /note="C->S: No effect."
FT                   /evidence="ECO:0000269|PubMed:9499122"
FT   MUTAGEN         161
FT                   /note="C->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:9499122"
FT   MUTAGEN         161
FT                   /note="C->S: No effect."
FT                   /evidence="ECO:0000269|PubMed:9499122"
FT   MUTAGEN         438
FT                   /note="C->F,S: Complete loss of E(rns) glycoprotein
FT                   dimerization. Virus shows attenuated phenotype."
FT                   /evidence="ECO:0000269|PubMed:19264773"
FT   STRAND          1592..1602
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   HELIX           1607..1614
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   STRAND          1632..1639
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   STRAND          1642..1649
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   STRAND          1652..1655
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   HELIX           1657..1660
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   STRAND          1665..1669
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   STRAND          1672..1676
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   STRAND          1680..1682
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   TURN            1683..1686
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   STRAND          1687..1691
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   STRAND          1703..1712
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   STRAND          1718..1727
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   STRAND          1730..1734
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   HELIX           1745..1748
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   STRAND          1755..1758
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   TURN            1759..1761
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   STRAND          1764..1767
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   STRAND          1770..1777
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   STRAND          1780..1782
FT                   /evidence="ECO:0007829|PDB:5MZ4"
FT   HELIX           1792..1803
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   STRAND          1810..1814
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   STRAND          1817..1819
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   STRAND          1821..1823
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   HELIX           1824..1833
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   STRAND          1839..1845
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   HELIX           1846..1859
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   STRAND          1865..1871
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   STRAND          1880..1885
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   HELIX           1886..1889
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   HELIX           1894..1901
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   STRAND          1905..1910
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   HELIX           1912..1914
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   HELIX           1917..1927
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   HELIX           1928..1932
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   STRAND          1935..1939
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   STRAND          1956..1958
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   TURN            1970..1972
FT                   /evidence="ECO:0007829|PDB:4CBL"
FT   STRAND          1973..1976
FT                   /evidence="ECO:0007829|PDB:4CBG"
FT   STRAND          1979..1982
FT                   /evidence="ECO:0007829|PDB:4CBG"
FT   HELIX           1983..1987
FT                   /evidence="ECO:0007829|PDB:4CBG"
FT   STRAND          1990..1993
FT                   /evidence="ECO:0007829|PDB:4CBG"
FT   HELIX           1997..2009
FT                   /evidence="ECO:0007829|PDB:4CBG"
FT   STRAND          2014..2017
FT                   /evidence="ECO:0007829|PDB:4CBG"
FT   HELIX           2024..2030
FT                   /evidence="ECO:0007829|PDB:4CBG"
FT   STRAND          2032..2034
FT                   /evidence="ECO:0007829|PDB:4CBG"
FT   STRAND          2036..2041
FT                   /evidence="ECO:0007829|PDB:4CBG"
FT   HELIX           2042..2045
FT                   /evidence="ECO:0007829|PDB:4CBI"
FT   STRAND          2054..2057
FT                   /evidence="ECO:0007829|PDB:4CBG"
FT   STRAND          2061..2068
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   STRAND          2070..2073
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   STRAND          2075..2082
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   HELIX           2086..2093
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   STRAND          2096..2100
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   STRAND          2103..2105
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   STRAND          2112..2114
FT                   /evidence="ECO:0007829|PDB:4CBG"
FT   HELIX           2118..2124
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   HELIX           2125..2128
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   TURN            2129..2132
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   HELIX           2135..2146
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   HELIX           2153..2166
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   HELIX           2173..2181
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   HELIX           2188..2193
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   TURN            2194..2196
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   STRAND          2204..2207
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   STRAND          2210..2215
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   STRAND          2234..2237
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   HELIX           2238..2246
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   HELIX           2257..2270
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   HELIX           2272..2275
FT                   /evidence="ECO:0007829|PDB:4CBH"
FT   STRAND          2276..2279
FT                   /evidence="ECO:0007829|PDB:5MZ4"
SQ   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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