GenomeNet

Database: UniProt
Entry: POLG_DEN1W
LinkDB: POLG_DEN1W
Original site: POLG_DEN1W 
ID   POLG_DEN1W              Reviewed;        3392 AA.
AC   P17763; P27910; P89313; P89314;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   11-DEC-2019, entry version 174.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Capsid protein C;
DE     AltName: Full=Capsid protein;
DE     AltName: Full=Core protein;
DE   Contains:
DE     RecName: Full=Protein prM;
DE     AltName: Full=Precursor membrane protein;
DE   Contains:
DE     RecName: Full=Peptide pr;
DE     AltName: Full=Peptide precursor;
DE   Contains:
DE     RecName: Full=Small envelope protein M;
DE     AltName: Full=Matrix protein;
DE   Contains:
DE     RecName: Full=Envelope protein E;
DE   Contains:
DE     RecName: Full=Non-structural protein 1;
DE              Short=NS1;
DE   Contains:
DE     RecName: Full=Non-structural protein 2A;
DE              Short=NS2A;
DE   Contains:
DE     RecName: Full=Serine protease subunit NS2B;
DE     AltName: Full=Flavivirin protease NS2B regulatory subunit;
DE     AltName: Full=Non-structural protein 2B;
DE   Contains:
DE     RecName: Full=Serine protease NS3;
DE              EC=3.4.21.91;
DE              EC=3.6.1.15 {ECO:0000250|UniProtKB:Q9Q6P4};
DE              EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9Q6P4};
DE     AltName: Full=Flavivirin protease NS3 catalytic subunit;
DE     AltName: Full=Non-structural protein 3;
DE   Contains:
DE     RecName: Full=Non-structural protein 4A;
DE              Short=NS4A;
DE   Contains:
DE     RecName: Full=Peptide 2k;
DE   Contains:
DE     RecName: Full=Non-structural protein 4B;
DE              Short=NS4B;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase NS5;
DE              EC=2.1.1.56 {ECO:0000255|PROSITE-ProRule:PRU00924};
DE              EC=2.1.1.57 {ECO:0000255|PROSITE-ProRule:PRU00924};
DE              EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE     AltName: Full=Non-structural protein 5;
OS   Dengue virus type 1 (strain Nauru/West Pac/1974) (DENV-1).
OC   Viruses; Riboviria; Flaviviridae; Flavivirus.
OX   NCBI_TaxID=11059;
OH   NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OH   NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate 45AZ5, and Isolate WestPac;
RX   PubMed=9292016; DOI=10.1099/0022-1317-78-9-2287;
RA   Puri B., Nelson W.M., Henchal E.A., Hoke C.H., Eckels K.H., Dubois D.R.,
RA   Porter K.R., Hayes C.G.;
RT   "Molecular analysis of dengue virus attenuation after serial passage in
RT   primary dog kidney cells.";
RL   J. Gen. Virol. 78:2287-2291(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-1226.
RX   PubMed=3672932; DOI=10.1016/0042-6822(87)90196-6;
RA   Mason P.W., McAda P.C., Mason T.L., Fournier M.J.;
RT   "Sequence of the dengue-1 virus genome in the region encoding the three
RT   structural proteins and the major nonstructural protein NS1.";
RL   Virology 161:262-267(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-792.
RC   STRAIN=Isolate Philippines/836-1/1984;
RX   PubMed=2738579; DOI=10.1099/0022-1317-70-7-1701;
RA   Chu M.C., O'Rourke E.J., Trent D.W.;
RT   "Genetic relatedness among structural protein genes of dengue 1 virus
RT   strains.";
RL   J. Gen. Virol. 70:1701-1712(1989).
RN   [4]
RP   SUBUNIT (NON-STRUCTURAL PROTEIN 1).
RX   PubMed=2827377; DOI=10.1016/0042-6822(88)90408-4;
RA   Winkler G., Randolph V.B., Cleaves G.R., Ryan T.E., Stollar V.;
RT   "Evidence that the mature form of the flavivirus nonstructural protein NS1
RT   is a dimer.";
RL   Virology 162:187-196(1988).
RN   [5]
RP   PROTEOLYTIC CLEAVAGE (PROTEIN PRM).
RX   PubMed=2154882; DOI=10.1016/0042-6822(90)90099-d;
RA   Randolph V.B., Winkler G., Stollar V.;
RT   "Acidotropic amines inhibit proteolytic processing of flavivirus prM
RT   protein.";
RL   Virology 174:450-458(1990).
RN   [6]
RP   GLYCOSYLATION (NON-STRUCTURAL PROTEIN 1).
RX   PubMed=8176380; DOI=10.1099/0022-1317-75-5-1183;
RA   Pryor M.J., Wright P.J.;
RT   "Glycosylation mutants of dengue virus NS1 protein.";
RL   J. Gen. Virol. 75:1183-1187(1994).
RN   [7]
RP   SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 1), SUBUNIT (NON-STRUCTURAL
RP   PROTEIN 1), AND GLYCOSYLATION (NON-STRUCTURAL PROTEIN 1).
RX   PubMed=10364366;
RA   Flamand M., Megret F., Mathieu M., Lepault J., Rey F.A., Deubel V.;
RT   "Dengue virus type 1 nonstructural glycoprotein NS1 is secreted from
RT   mammalian cells as a soluble hexamer in a glycosylation-dependent
RT   fashion.";
RL   J. Virol. 73:6104-6110(1999).
RN   [8]
RP   PHOSPHORYLATION (RNA-DIRECTED RNA POLYMERASE NS5).
RX   PubMed=7642575; DOI=10.1074/jbc.270.32.19100;
RA   Kapoor M., Zhang L., Ramachandra M., Kusukawa J., Ebner K.E.,
RA   Padmanabhan R.;
RT   "Association between NS3 and NS5 proteins of dengue virus type 2 in the
RT   putative RNA replicase is linked to differential phosphorylation of NS5.";
RL   J. Biol. Chem. 270:19100-19106(1995).
RN   [9]
RP   FUNCTION (PROTEIN PRM), INTERACTION WITH ENVELOPE PROTEIN E (PROTEIN PRM),
RP   AND INTERACTION WITH PROTEIN PRM (ENVELOPE PROTEIN E).
RX   PubMed=9971841;
RA   Wang S., He R., Anderson R.;
RT   "PrM- and cell-binding domains of the dengue virus E protein.";
RL   J. Virol. 73:2547-2551(1999).
RN   [10]
RP   FUNCTION (SMALL ENVELOPE PROTEIN M).
RX   PubMed=13679613; DOI=10.1099/vir.0.19163-0;
RA   Catteau A., Kalinina O., Wagner M.C., Deubel V., Courageot M.P.,
RA   Despres P.;
RT   "Dengue virus M protein contains a proapoptotic sequence referred to as
RT   ApoptoM.";
RL   J. Gen. Virol. 84:2781-2793(2003).
RN   [11]
RP   CHARACTERIZATION OF METHYLTRANSFERASE ACTIVITY, AND FUNCTION (RNA-DIRECTED
RP   RNA POLYMERASE NS5).
RX   PubMed=17267492; DOI=10.1128/jvi.02704-06;
RA   Zhou Y., Ray D., Zhao Y., Dong H., Ren S., Li Z., Guo Y., Bernard K.A.,
RA   Shi P.-Y., Li H.;
RT   "Structure and function of flavivirus NS5 methyltransferase.";
RL   J. Virol. 81:3891-3903(2007).
RN   [12]
RP   FUNCTION (CAPSID PROTEIN C), FUNCTION (ENVELOPE PROTEIN E), AND SUBUNIT
RP   (ENVELOPE PROTEIN E).
RX   PubMed=11893341; DOI=10.1016/s0092-8674(02)00660-8;
RA   Kuhn R.J., Zhang W., Rossmann M.G., Pletnev S.V., Corver J., Lenches E.,
RA   Jones C.T., Mukhopadhyay S., Chipman P.R., Strauss E.G., Baker T.S.,
RA   Strauss J.H.;
RT   "Structure of dengue virus: implications for flavivirus organization,
RT   maturation, and fusion.";
RL   Cell 108:717-725(2002).
RN   [13]
RP   DISULFIDE BOND (NON-STRUCTURAL PROTEIN 1).
RC   STRAIN=DENV-2 strain Puerto Rico/PR159-S1/1969;
RX   PubMed=14981082; DOI=10.1074/jbc.m312907200;
RA   Wallis T.P., Huang C.Y., Nimkar S.B., Young P.R., Gorman J.J.;
RT   "Determination of the disulfide bond arrangement of dengue virus NS1
RT   protein.";
RL   J. Biol. Chem. 279:20729-20741(2004).
RN   [14]
RP   DISULFIDE BOND (ENVELOPE PROTEIN E).
RC   STRAIN=DENV-2 strain Thailand/16681/1984;
RX   PubMed=14963174; DOI=10.1128/jvi.78.5.2648-2652.2004;
RA   Roehrig J.T., Volpe K.E., Squires J., Hunt A.R., Davis B.S., Chang G.J.;
RT   "Contribution of disulfide bridging to epitope expression of the dengue
RT   type 2 virus envelope glycoprotein.";
RL   J. Virol. 78:2648-2652(2004).
RN   [15]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 4B).
RX   PubMed=15956546; DOI=10.1128/jvi.79.13.8004-8013.2005;
RA   Munoz-Jordan J.L., Laurent-Rolle M., Ashour J., Martinez-Sobrido L.,
RA   Ashok M., Lipkin W.I., Garcia-Sastre A.;
RT   "Inhibition of alpha/beta interferon signaling by the NS4B protein of
RT   flaviviruses.";
RL   J. Virol. 79:8004-8013(2005).
RN   [16]
RP   FUNCTION (SMALL ENVELOPE PROTEIN M).
RX   PubMed=16007501; DOI=10.1007/s00232-005-0744-9;
RA   Premkumar A., Horan C.R., Gage P.W.;
RT   "Dengue virus M protein C-terminal peptide (DVM-C) forms ion channels.";
RL   J. Membr. Biol. 204:33-38(2005).
RN   [17]
RP   INTERACTION WITH SERINE PROTEASE NS3 (RNA-DIRECTED RNA POLYMERASE NS5),
RP   INTERACTION WITH RNA-DIRECTED RNA POLYMERASE NS5 (SERINE PROTEASE NS3), AND
RP   CATALYTIC ACTIVITY (SERINE PROTEASE NS3).
RC   STRAIN=Thailand/NGS-C/1944;
RX   PubMed=15917225; DOI=10.1074/jbc.m501393200;
RA   Yon C., Teramoto T., Mueller N., Phelan J., Ganesh V.K., Murthy K.H.,
RA   Padmanabhan R.;
RT   "Modulation of the nucleoside triphosphatase/RNA helicase and 5'-RNA
RT   triphosphatase activities of Dengue virus type 2 nonstructural protein 3
RT   (NS3) by interaction with NS5, the RNA-dependent RNA polymerase.";
RL   J. Biol. Chem. 280:27412-27419(2005).
RN   [18]
RP   INTERACTION WITH NON-STRUCTURAL PROTEIN 4B (NON-STRUCTURAL PROTEIN 3), AND
RP   INTERACTION WITH NON-STRUCTURAL PROTEIN 3 (NON-STRUCTURAL PROTEIN 4B).
RX   PubMed=16894199; DOI=10.1099/vir.0.81844-0;
RA   Umareddy I., Chao A., Sampath A., Gu F., Vasudevan S.G.;
RT   "Dengue virus NS4B interacts with NS3 and dissociates it from single-
RT   stranded RNA.";
RL   J. Gen. Virol. 87:2605-2614(2006).
RN   [19]
RP   SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 4B), AND TOPOLOGY
RP   (NON-STRUCTURAL PROTEIN 4B).
RX   PubMed=16436383; DOI=10.1074/jbc.m512697200;
RA   Miller S., Sparacio S., Bartenschlager R.;
RT   "Subcellular localization and membrane topology of the Dengue virus type 2
RT   Non-structural protein 4B.";
RL   J. Biol. Chem. 281:8854-8863(2006).
RN   [20]
RP   SUBCELLULAR LOCATION (RNA-DIRECTED RNA POLYMERASE NS5).
RX   PubMed=16699025; DOI=10.1128/jvi.01982-05;
RA   Uchil P.D., Kumar A.V., Satchidanandam V.;
RT   "Nuclear localization of flavivirus RNA synthesis in infected cells.";
RL   J. Virol. 80:5451-5464(2006).
RN   [21]
RP   SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 4A), AND TOPOLOGY (PEPTIDE
RP   2K).
RX   PubMed=17276984; DOI=10.1074/jbc.m609919200;
RA   Miller S., Kastner S., Krijnse-Locker J., Buhler S., Bartenschlager R.;
RT   "The non-structural protein 4A of dengue virus is an integral membrane
RT   protein inducing membrane alterations in a 2K-regulated manner.";
RL   J. Biol. Chem. 282:8873-8882(2007).
RN   [22]
RP   GLYCOSYLATION AT ASN-347 (ENVELOPE PROTEIN E).
RX   PubMed=17459925; DOI=10.1128/jvi.00116-07;
RA   Mondotte J.A., Lozach P.Y., Amara A., Gamarnik A.V.;
RT   "Essential role of dengue virus envelope protein N glycosylation at
RT   asparagine-67 during viral propagation.";
RL   J. Virol. 81:7136-7148(2007).
RN   [23]
RP   REVIEW.
RX   PubMed=18644250; DOI=10.1016/j.mib.2008.06.004;
RA   Perera R., Kuhn R.J.;
RT   "Structural proteomics of dengue virus.";
RL   Curr. Opin. Microbiol. 11:369-377(2008).
RN   [24]
RP   SUBCELLULAR LOCATION (CAPSID PROTEIN C), AND FUNCTION (CAPSID PROTEIN C).
RX   PubMed=18420804; DOI=10.1099/vir.0.83264-0;
RA   Sangiambut S., Keelapang P., Aaskov J., Puttikhunt C., Kasinrerk W.,
RA   Malasit P., Sittisombut N.;
RT   "Multiple regions in dengue virus capsid protein contribute to nuclear
RT   localization during virus infection.";
RL   J. Gen. Virol. 89:1254-1264(2008).
RN   [25]
RP   FUNCTION (ENVELOPE PROTEIN E), FUNCTION (PROTEIN PRM), AND FUNCTION
RP   (PEPTIDE PR).
RX   PubMed=18369148; DOI=10.1126/science.1153264;
RA   Yu I.M., Zhang W., Holdaway H.A., Li L., Kostyuchenko V.A., Chipman P.R.,
RA   Kuhn R.J., Rossmann M.G., Chen J.;
RT   "Structure of the immature dengue virus at low pH primes proteolytic
RT   maturation.";
RL   Science 319:1834-1837(2008).
RN   [26]
RP   FUNCTION (PROTEIN PR), AND SUBCELLULAR LOCATION (PROTEIN PR).
RX   PubMed=19759134; DOI=10.1128/jvi.01637-09;
RA   Yu I.M., Holdaway H.A., Chipman P.R., Kuhn R.J., Rossmann M.G., Chen J.;
RT   "Association of the pr peptides with dengue virus at acidic pH blocks
RT   membrane fusion.";
RL   J. Virol. 83:12101-12107(2009).
RN   [27]
RP   FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), AND INTERACTION WITH HUMAN
RP   STAT2 (RNA-DIRECTED RNA POLYMERASE NS5).
RX   PubMed=19279106; DOI=10.1128/jvi.02188-08;
RA   Ashour J., Laurent-Rolle M., Shi P.Y., Garcia-Sastre A.;
RT   "NS5 of dengue virus mediates STAT2 binding and degradation.";
RL   J. Virol. 83:5408-5418(2009).
RN   [28]
RP   FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), AND INTERACTION WITH
RP   RNA-DIRECTED RNA POLYMERASE NS5 (SERINE PROTEASE NS3).
RC   STRAIN=Thailand/16681/1984;
RX   PubMed=19850911; DOI=10.1261/rna.1609709;
RA   Issur M., Geiss B.J., Bougie I., Picard-Jean F., Despins S., Mayette J.,
RA   Hobdey S.E., Bisaillon M.;
RT   "The flavivirus NS5 protein is a true RNA guanylyltransferase that
RT   catalyzes a two-step reaction to form the RNA cap structure.";
RL   RNA 15:2340-2350(2009).
RN   [29]
RP   DOMAIN (ENVELOPE PROTEIN E).
RX   PubMed=20181718; DOI=10.1128/jvi.01963-09;
RA   Hsieh S.C., Tsai W.Y., Wang W.K.;
RT   "The length of and nonhydrophobic residues in the transmembrane domain of
RT   dengue virus envelope protein are critical for its retention and assembly
RT   in the endoplasmic reticulum.";
RL   J. Virol. 84:4782-4797(2010).
RN   [30]
RP   INTERACTION WITH HUMAN EXOC1 (CAPSID PROTEIN C), AND SUBCELLULAR LOCATION
RP   (CAPSID PROTEIN C).
RC   STRAIN=DENV-2;
RX   PubMed=19889084; DOI=10.1111/j.1462-5822.2009.01407.x;
RA   Bhuvanakantham R., Li J., Tan T.T., Ng M.L.;
RT   "Human Sec3 protein is a novel transcriptional and translational repressor
RT   of flavivirus.";
RL   Cell. Microbiol. 12:453-472(2010).
RN   [31]
RP   INTERACTION WITH HUMAN EXOC1 (CAPSID PROTEIN C), AND FUNCTION (CAPSID
RP   PROTEIN C).
RC   STRAIN=DENV-2;
RX   PubMed=23522008; DOI=10.1111/cmi.12143;
RA   Bhuvanakantham R., Ng M.L.;
RT   "West Nile virus and dengue virus capsid protein negates the antiviral
RT   activity of human Sec3 protein through the proteasome pathway.";
RL   Cell. Microbiol. 15:1688-1706(2013).
RN   [32]
RP   REVIEW.
RX   PubMed=20372965; DOI=10.1007/s00018-010-0357-z;
RA   Rodenhuis-Zybert I.A., Wilschut J., Smit J.M.;
RT   "Dengue virus life cycle: viral and host factors modulating infectivity.";
RL   Cell. Mol. Life Sci. 67:2773-2786(2010).
RN   [33]
RP   FUNCTION (CAPSID PROTEIN C).
RX   PubMed=21909430; DOI=10.1371/journal.pone.0024365;
RA   Colpitts T.M., Barthel S., Wang P., Fikrig E.;
RT   "Dengue virus capsid protein binds core histones and inhibits nucleosome
RT   formation in human liver cells.";
RL   PLoS ONE 6:E24365-E24365(2011).
RN   [34]
RP   REVIEW (PROTEIN PRM).
RX   PubMed=21388812; DOI=10.1016/j.tim.2011.02.002;
RA   Rodenhuis-Zybert I.A., Wilschut J., Smit J.M.;
RT   "Partial maturation: an immune-evasion strategy of dengue virus?";
RL   Trends Microbiol. 19:248-254(2011).
RN   [35]
RP   SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 2A), AND TOPOLOGY
RP   (NON-STRUCTURAL PROTEIN 2A).
RC   STRAIN=DENV-2 strain NGC;
RX   PubMed=23408612; DOI=10.1128/jvi.02424-12;
RA   Xie X., Gayen S., Kang C., Yuan Z., Shi P.Y.;
RT   "Membrane topology and function of dengue virus NS2A protein.";
RL   J. Virol. 87:4609-4622(2013).
RN   [36]
RP   FUNCTION (SMALL ENVELOPE PROTEIN M), AND FUNCTION (PROTEIN PRM).
RC   STRAIN=DENV-1 strain Hawaii;
RX   PubMed=25326389; DOI=10.1074/jbc.m114.610428;
RA   Hsieh S.C., Wu Y.C., Zou G., Nerurkar V.R., Shi P.Y., Wang W.K.;
RT   "Highly conserved residues in the helical domain of dengue virus type 1
RT   precursor membrane protein are involved in assembly, precursor membrane
RT   (prM) protein cleavage, and entry.";
RL   J. Biol. Chem. 289:33149-33160(2014).
RN   [37]
RP   INTERACTION WITH ENVELOPE PROTEIN E (NON-STRUCTURAL PROTEIN 1), INTERACTION
RP   WITH PRM (NON-STRUCTURAL PROTEIN 1), INTERACTION WITH NON-STRUCTURAL
RP   PROTEIN 1 (PROTEIN PRM), AND INTERACTION WITH NON-STRUCTURAL PROTEIN 1
RP   (ENVELOPE PROTEIN E).
RC   STRAIN=DENV-2 strain 16681;
RX   PubMed=26562291; DOI=10.1371/journal.ppat.1005277;
RA   Scaturro P., Cortese M., Chatel-Chaix L., Fischl W., Bartenschlager R.;
RT   "Dengue virus non-structural protein 1 modulates infectious particle
RT   production via interaction with the structural proteins.";
RL   PLoS Pathog. 11:E1005277-E1005277(2015).
RN   [38]
RP   SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 1).
RX   PubMed=26655246; DOI=10.1016/j.virol.2015.11.020;
RA   Alcala A.C., Medina F., Gonzalez-Robles A., Salazar-Villatoro L.,
RA   Fragoso-Soriano R.J., Vasquez C., Cervantes-Salazar M., Del Angel R.M.,
RA   Ludert J.E.;
RT   "The dengue virus non-structural protein 1 (NS1) is secreted efficiently
RT   from infected mosquito cells.";
RL   Virology 488:278-287(2015).
RN   [39]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 2A), AND MUTAGENESIS OF GLY-1138;
RP   GLU-1147; GLU-1227; ASP-1252; GLN-1314; LYS-1315 AND GLY-1327.
RX   PubMed=25392211; DOI=10.1128/jvi.02882-14;
RA   Xie X., Zou J., Puttikhunt C., Yuan Z., Shi P.Y.;
RT   "Two distinct sets of NS2A molecules are responsible for dengue virus RNA
RT   synthesis and virion assembly.";
RL   J. Virol. 89:1298-1313(2015).
RN   [40]
RP   SUBCELLULAR LOCATION (SERINE PROTEASE SUBUNIT NS2B), AND TOPOLOGY (SERINE
RP   PROTEASE SUBUNIT NS2B).
RC   STRAIN=DENV-4;
RX   PubMed=26072288; DOI=10.1016/j.bbamem.2015.06.010;
RA   Li Y., Li Q., Wong Y.L., Liew L.S., Kang C.;
RT   "Membrane topology of NS2B of dengue virus revealed by NMR spectroscopy.";
RL   Biochim. Biophys. Acta 1848:2244-2252(2015).
RN   [41]
RP   FUNCTION (SERINE PROTEASE SUBUNIT NS2B), AND SUBUNIT (SERINE PROTEASE
RP   SUBUNIT NS2B).
RC   STRAIN=DENV-2 New Guinea strain AF0136;
RX   PubMed=26728778; DOI=10.1186/s12985-015-0456-4;
RA   Leon-Juarez M., Martinez-Castillo M., Shrivastava G., Garcia-Cordero J.,
RA   Villegas-Sepulveda N., Mondragon-Castelan M., Mondragon-Flores R.,
RA   Cedillo-Barron L.;
RT   "Recombinant Dengue virus protein NS2B alters membrane permeability in
RT   different membrane models.";
RL   Virol. J. 13:1-1(2016).
RN   [42]
RP   SUBUNIT (RNA-DIRECTED RNA POLYMERASE NS5).
RC   STRAIN=DENV-3;
RX   PubMed=26895240; DOI=10.1371/journal.ppat.1005451;
RA   Klema V.J., Ye M., Hindupur A., Teramoto T., Gottipati K., Padmanabhan R.,
RA   Choi K.H.;
RT   "Dengue virus nonstructural protein 5 (NS5) assembles into a dimer with a
RT   unique methyltransferase and polymerase interface.";
RL   PLoS Pathog. 12:E1005451-E1005451(2016).
RN   [43]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 1).
RX   PubMed=27416066; DOI=10.1371/journal.ppat.1005738;
RA   Puerta-Guardo H., Glasner D.R., Harris E.;
RT   "Dengue virus NS1 disrupts the endothelial glycocalyx, leading to
RT   hyperpermeability.";
RL   PLoS Pathog. 12:E1005738-E1005738(2016).
RN   [44]
RP   REVIEW (NON-STRUCTURAL PROTEIN 1).
RX   PubMed=27473856; DOI=10.1186/s12985-016-0590-7;
RA   Rastogi M., Sharma N., Singh S.K.;
RT   "Flavivirus NS1: a multifaceted enigmatic viral protein.";
RL   Virol. J. 13:131-131(2016).
RN   [45]
RP   FUNCTION, INTERACTION WITH HOST MAVS, AND SUBCELLULAR LOCATION.
RX   PubMed=27252539; DOI=10.1128/jvi.00221-16;
RA   He Z., Zhu X., Wen W., Yuan J., Hu Y., Chen J., An S., Dong X., Lin C.,
RA   Yu J., Wu J., Yang Y., Cai J., Li J., Li M.;
RT   "Dengue virus subverts host innate immunity by targeting adaptor protein
RT   MAVS.";
RL   J. Virol. 90:7219-7230(2016).
RN   [46]
RP   INTERACTION WITH HOST SHFL (SERINE PROTEASE NS3 AND NON-STRUCTURAL PROTEIN
RP   4A).
RC   STRAIN=Tonga/74 type 2;
RX   PubMed=27974568; DOI=10.1128/jvi.01606-16;
RA   Balinsky C.A., Schmeisser H., Wells A.I., Ganesan S., Jin T., Singh K.,
RA   Zoon K.C.;
RT   "IRAV (FLJ11286), an Interferon-Stimulated Gene with Antiviral Activity
RT   against Dengue Virus, Interacts with MOV10.";
RL   J. Virol. 91:0-0(2017).
RN   [47]
RP   REVIEW (RNA-DIRECTED RNA POLYMERASE NS5).
RX   PubMed=28441781; DOI=10.3390/v9040091;
RA   El Sahili A., Lescar J.;
RT   "Dengue virus non-structural protein 5.";
RL   Viruses 9:0-0(2017).
RN   [48]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1394-1661, INTERACTION WITH SERINE
RP   PROTEASE NS3 (SERINE PROTEASE SUBUNIT NS2B), AND INTERACTION WITH SERINE
RP   PROTEASE SUBUNIT NS2B (SERINE PROTEASE NS3).
RX   PubMed=20042502; DOI=10.1128/jvi.02044-09;
RA   Chandramouli S., Joseph J.S., Daudenarde S., Gatchalian J.,
RA   Cornillez-Ty C., Kuhn P.;
RT   "Serotype-specific structural differences in the protease-cofactor
RT   complexes of the dengue virus family.";
RL   J. Virol. 84:3059-3067(2010).
CC   -!- FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding
CC       to the cell membrane and gathering the viral RNA into a nucleocapsid
CC       that forms the core of a mature virus particle (PubMed:11893341).
CC       During virus entry, may induce genome penetration into the host
CC       cytoplasm after hemifusion induced by the surface proteins. Can migrate
CC       to the cell nucleus where it modulates host functions (PubMed:18420804,
CC       PubMed:21909430). Overcomes the anti-viral effects of host EXOC1 by
CC       sequestering and degrading the latter through the proteasome
CC       degradation pathway (PubMed:23522008). {ECO:0000269|PubMed:11893341,
CC       ECO:0000269|PubMed:18420804, ECO:0000269|PubMed:21909430,
CC       ECO:0000269|PubMed:23522008}.
CC   -!- FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering
CC       with host Dicer. {ECO:0000250|UniProtKB:P03314}.
CC   -!- FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope
CC       proteins in trans-Golgi by binding to envelope protein E at pH6.0.
CC       After virion release in extracellular space, gets dissociated from E
CC       dimers. {ECO:0000269|PubMed:18369148, ECO:0000269|PubMed:19759134}.
CC   -!- FUNCTION: [Protein prM]: Acts as a chaperone for envelope protein E
CC       during intracellular virion assembly by masking and inactivating
CC       envelope protein E fusion peptide. prM is the only viral peptide
CC       matured by host furin in the trans-Golgi network probably to avoid
CC       catastrophic activation of the viral fusion activity in acidic Golgi
CC       compartment prior to virion release (PubMed:9971841). prM-E cleavage is
CC       inefficient, and many virions are only partially matured. These
CC       uncleaved prM would play a role in immune evasion (PubMed:21388812).
CC       {ECO:0000269|PubMed:18369148, ECO:0000269|PubMed:25326389,
CC       ECO:0000269|PubMed:9971841, ECO:0000303|PubMed:21388812}.
CC   -!- FUNCTION: [Small envelope protein M]: May play a role in virus budding
CC       (PubMed:25326389). Exerts cytotoxic effects by activating a
CC       mitochondrial apoptotic pathway through M extodomain (PubMed:13679613).
CC       May display a viroporin activity (PubMed:16007501).
CC       {ECO:0000269|PubMed:13679613, ECO:0000269|PubMed:16007501,
CC       ECO:0000269|PubMed:25326389}.
CC   -!- FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and
CC       mediates fusion between viral and cellular membranes. Envelope protein
CC       is synthesized in the endoplasmic reticulum in the form of heterodimer
CC       with protein prM. They play a role in virion budding in the ER, and the
CC       newly formed immature particle is covered with 60 spikes composed of
CC       heterodimer between precursor prM and envelope protein E. The virion is
CC       transported to the Golgi apparatus where the low pH causes dissociation
CC       of PrM-E heterodimers and formation of E homodimers (PubMed:18369148).
CC       prM-E cleavage is ineficient, and many virions are only partially
CC       matured. These uncleaved prM would play a role in immune evasion
CC       (PubMed:11893341). {ECO:0000269|PubMed:11893341,
CC       ECO:0000269|PubMed:18369148}.
CC   -!- FUNCTION: [Non-structural protein 1]: Involved in immune evasion,
CC       pathogenesis and viral replication. Once cleaved off the polyprotein,
CC       is targeted to three destinations: the viral replication cycle, the
CC       plasma membrane and the extracellular compartment. Essential for viral
CC       replication. Required for formation of the replication complex and
CC       recruitment of other non-structural proteins to the ER-derived membrane
CC       structures. Excreted as a hexameric lipoparticle that plays a role
CC       against host immune response. Antagonizing the complement function.
CC       Binds to the host macrophages and dendritic cells. Inhibits signal
CC       transduction originating from Toll-like receptor 3 (TLR3).
CC       {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- FUNCTION: [Non-structural protein 1]: Disrupts the host endothelial
CC       glycocalyx layer of host pulmonary microvascular endothelial cells,
CC       inducing degradation of sialic acid and shedding of heparan sulfate
CC       proteoglycans. NS1 induces expression of sialidases, heparanase, and
CC       activates cathepsin L, which activates heparanase via enzymatic
CC       cleavage. These effects are probably linked to the endothelial
CC       hyperpermeability observed in severe dengue disease.
CC       {ECO:0000269|PubMed:27416066}.
CC   -!- FUNCTION: [Non-structural protein 2A]: Component of the viral RNA
CC       replication complex that functions in virion assembly and antagonizes
CC       the host immune response. {ECO:0000269|PubMed:25392211}.
CC   -!- FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the
CC       serine protease function of NS3. May have membrane-destabilizing
CC       activity and form viroporins (PubMed:26728778). {ECO:0000255|PROSITE-
CC       ProRule:PRU00859, ECO:0000269|PubMed:26728778}.
CC   -!- FUNCTION: [Serine protease NS3]: Displays three enzymatic activities:
CC       serine protease, NTPase and RNA helicase. NS3 serine protease, in
CC       association with NS2B, performs its autocleavage and cleaves the
CC       polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-
CC       NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and
CC       unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}.
CC   -!- FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of
CC       the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy
CC       during unwinding. Plays a role in the inhibition of the host innate
CC       immune response. Interacts with host MAVS and thereby prevents the
CC       interaction between DDX58 and MAVS. In turn, IFN-beta production is
CC       impaired. {ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27252539}.
CC   -!- FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is
CC       required for the interferon antagonism activity of the latter.
CC       {ECO:0000269|PubMed:17276984}.
CC   -!- FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-
CC       derived membrane vesicles where the viral replication takes place (By
CC       similarity). Inhibits interferon (IFN)-induced host STAT1
CC       phosphorylation and nuclear translocation, thereby preventing the
CC       establishment of a cellular antiviral state by blocking the IFN-
CC       alpha/beta pathway (PubMed:15956546). {ECO:0000250|UniProtKB:Q9Q6P4,
CC       ECO:0000269|PubMed:15956546}.
CC   -!- FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+)
CC       and (-) RNA genome, and performs the capping of genomes in the
CC       cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O
CC       positions. Besides its role in RNA genome replication, also prevents
CC       the establishment of cellular antiviral state by blocking the
CC       interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host
CC       TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-
CC       STAT signaling pathway. {ECO:0000269|PubMed:17267492,
CC       ECO:0000269|PubMed:19279106, ECO:0000269|PubMed:19850911}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of
CC         the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.;
CC         EC=3.4.21.91; Evidence={ECO:0000269|PubMed:15917225};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
CC         EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY:
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:
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-guanosine in mRNA + S-
CC         adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-guanosine in mRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:60856, Rhea:RHEA-COMP:15681, Rhea:RHEA-COMP:15683,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143971,
CC         ChEBI:CHEBI:143975; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00924};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-adenosine in mRNA + S-
CC         adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-adenosine in mRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:60852, Rhea:RHEA-COMP:15680, Rhea:RHEA-COMP:15682,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143973,
CC         ChEBI:CHEBI:143974; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00924};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-guanosine in
CC         mRNA + S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-
CC         triphosphoguanosine)-(2'-O-methyl-guanosine) in mRNA + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:60864, Rhea:RHEA-COMP:15683,
CC         Rhea:RHEA-COMP:15685, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:143975, ChEBI:CHEBI:143977;
CC         EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-adenosine in
CC         mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-(2'-O-methyl-adenosine) in mRNA + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:60860, Rhea:RHEA-COMP:15682,
CC         Rhea:RHEA-COMP:15684, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:143974, ChEBI:CHEBI:143976;
CC         EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
CC   -!- SUBUNIT: Capsid protein C: Homodimer. Interacts (via N-terminus) with
CC       host EXOC1 (via C-terminus) (PubMed:19889084, PubMed:23522008); this
CC       interaction results in EXOC1 degradation through the proteasome
CC       degradation pathway (PubMed:23522008). Protein prM: Forms heterodimers
CC       with envelope protein E in the endoplasmic reticulum and Golgi
CC       (PubMed:9971841). Envelope protein E: Homodimer; in the endoplasmic
CC       reticulum and Golgi (PubMed:11893341). Interacts with protein prM
CC       (PubMed:9971841). Interacts with non-structural protein 1
CC       (PubMed:26562291). Non-structural protein 1: Homodimer; Homohexamer
CC       when secreted (PubMed:2827377, PubMed:10364366). Interacts with
CC       envelope protein E (PubMed:26562291). Non-structural protein 2A:
CC       Interacts (via N-terminus) with serine protease NS3. Non-structural
CC       protein 2B: Forms a heterodimer with serine protease NS3
CC       (PubMed:20042502). May form homooligomers (PubMed:26728778). Serine
CC       protease NS3: Forms a heterodimer with NS2B (PubMed:20042502).
CC       Interacts with NS4B (PubMed:16894199). Interacts with unphosphorylated
CC       RNA-directed RNA polymerase NS5; this interaction stimulates RNA-
CC       directed RNA polymerase NS5 guanylyltransferase activity
CC       (PubMed:19850911, PubMed:15917225). Interacts with host SHFL
CC       (PubMed:27974568). Non-structural protein 4A: Interacts with host MAVS;
CC       this interaction inhibits the synthesis of IFN-beta (PubMed:27252539).
CC       Interacts with host SHFL (PubMed:27974568). Non-structural protein 4B:
CC       Interacts with serine protease NS3 (PubMed:16894199). RNA-directed RNA
CC       polymerase NS5: Homodimer (PubMed:26895240). Interacts with host STAT2;
CC       this interaction inhibits the phosphorylation of the latter, and, when
CC       all viral proteins are present (polyprotein), targets STAT2 for
CC       degradation (PubMed:19279106). Interacts with serine protease NS3
CC       (PubMed:15917225, PubMed:19850911). {ECO:0000269|PubMed:10364366,
CC       ECO:0000269|PubMed:11893341, ECO:0000269|PubMed:15917225,
CC       ECO:0000269|PubMed:16894199, ECO:0000269|PubMed:19279106,
CC       ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:19889084,
CC       ECO:0000269|PubMed:20042502, ECO:0000269|PubMed:23522008,
CC       ECO:0000269|PubMed:26562291, ECO:0000269|PubMed:26728778,
CC       ECO:0000269|PubMed:26895240, ECO:0000269|PubMed:27252539,
CC       ECO:0000269|PubMed:27974568, ECO:0000269|PubMed:2827377,
CC       ECO:0000269|PubMed:9971841}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein C]: Virion. Host nucleus
CC       {ECO:0000269|PubMed:18420804}. Host cytoplasm
CC       {ECO:0000269|PubMed:19889084}. Host cytoplasm, host perinuclear region
CC       {ECO:0000269|PubMed:19889084}.
CC   -!- SUBCELLULAR LOCATION: [Peptide pr]: Secreted
CC       {ECO:0000269|PubMed:19759134}.
CC   -!- SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane
CC       {ECO:0000269|PubMed:9971841}; Multi-pass membrane protein
CC       {ECO:0000255}. Host endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:9971841}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane
CC       {ECO:0000269|PubMed:20181718}; Multi-pass membrane protein
CC       {ECO:0000255}. Host endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:20181718}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted
CC       {ECO:0000269|PubMed:10364366, ECO:0000269|PubMed:26655246}. Host
CC       endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal
CC       side {ECO:0000305}. Note=Located in RE-derived vesicles hosting the
CC       replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic
CC       reticulum membrane {ECO:0000269|PubMed:23408612}; Multi-pass membrane
CC       protein {ECO:0000269|PubMed:23408612}.
CC   -!- SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic
CC       reticulum membrane; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:26072288}.
CC   -!- SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum
CC       membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane
CC       protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side
CC       {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently
CC       associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic
CC       reticulum membrane {ECO:0000269|PubMed:17276984}; Multi-pass membrane
CC       protein {ECO:0000269|PubMed:17276984}. Host mitochondrion
CC       {ECO:0000269|PubMed:27252539}. Note=Located in RE-associated vesicles
CC       hosting the replication complex. Interacts with host MAVS in the
CC       mitochondrion-associated endoplasmic reticulum membranes.
CC       {ECO:0000269|PubMed:17276984, ECO:0000269|PubMed:27252539}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic
CC       reticulum membrane {ECO:0000269|PubMed:16436383}; Multi-pass membrane
CC       protein {ECO:0000269|PubMed:16436383}. Note=Located in RE-derived
CC       vesicles hosting the replication complex.
CC       {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host
CC       endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Host nucleus
CC       {ECO:0000269|PubMed:16699025}. Note=Located in RE-associated vesicles
CC       hosting the replication complex. NS5 protein is mainly localized in the
CC       nucleus rather than in ER vesicles, especially in the DENV 2, 3, 4
CC       serotypes. {ECO:0000303|PubMed:28441781}.
CC   -!- DOMAIN: The transmembrane domains of the small envelope protein M and
CC       envelope protein E contain an endoplasmic reticulum retention signal.
CC       {ECO:0000269|PubMed:20181718}.
CC   -!- PTM: [RNA-directed RNA polymerase NS5]: Sumoylation of RNA-directed RNA
CC       polymerase NS5 increases NS5 protein stability allowing proper viral
CC       RNA replication. {ECO:0000250|UniProtKB:P29990}.
CC   -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield
CC       mature proteins. Cleavages in the lumen of endoplasmic reticulum are
CC       performed by host signal peptidase, whereas cleavages in the
CC       cytoplasmic side are performed by the Serine protease NS3. Signal
CC       cleavage at the 2K-4B site requires a prior NS3 protease-mediated
CC       cleavage at the 4A-2K site.
CC   -!- PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin,
CC       releasing the mature small envelope protein M, and peptide pr. This
CC       cleavage is incomplete as up to 30% of viral particles still carry
CC       uncleaved prM. {ECO:0000269|PubMed:21388812,
CC       ECO:0000269|PubMed:2154882}.
CC   -!- PTM: [Non-structural protein 1]: N-glycosylated (PubMed:8176380,
CC       PubMed:10364366). The excreted form is glycosylated and this is
CC       required for efficient secretion of the protein from infected cells.
CC       {ECO:0000269|PubMed:10364366, ECO:0000269|PubMed:8176380}.
CC   -!- PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines
CC       residues. This phosphorylation may trigger NS5 nuclear localization.
CC       {ECO:0000269|PubMed:7642575}.
CC   -!- PTM: [Envelope protein E]: N-glycosylated.
CC       {ECO:0000269|PubMed:17459925}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the class I-like SAM-
CC       binding methyltransferase superfamily. mRNA cap 0-1 NS5-type
CC       methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}.
CC   -!- WEB RESOURCE: Name=Virus Pathogen Resource;
CC       URL="http://www.viprbrc.org/brc/home.do?decorator=flavi_dengue";
DR   EMBL; U88535; AAB70694.1; -; Genomic_RNA.
DR   EMBL; U88536; AAB70695.1; -; Genomic_RNA.
DR   EMBL; M23027; AAA42940.1; -; Genomic_RNA.
DR   EMBL; D00503; BAA00395.1; -; Genomic_RNA.
DR   PIR; A27032; GNWVWP.
DR   RefSeq; NP_059433.1; NC_001477.1.
DR   PDB; 3J8D; EM; 26.00 A; B/F=579-675.
DR   PDB; 3L6P; X-ray; 2.20 A; A=1476-1648.
DR   PDB; 3LKW; X-ray; 2.00 A; A=1476-1657.
DR   PDB; 4AL8; X-ray; 1.66 A; C=575-675.
DR   PDB; 4GSX; X-ray; 1.90 A; A/B=281-691.
DR   PDB; 4GT0; X-ray; 2.57 A; A/B=281-701.
DR   PDB; 4LCY; X-ray; 1.60 A; C/J=1741-1749.
DR   PDB; 4OIG; X-ray; 2.69 A; A/B/D/E=947-1127.
DR   PDB; 5VIC; X-ray; 3.00 A; E=578-676.
DR   PDB; 5WJL; X-ray; 3.15 A; C/F/I=1608-1617.
DR   PDB; 5WKF; X-ray; 2.95 A; C/H=1608-1617.
DR   PDBsum; 3J8D; -.
DR   PDBsum; 3L6P; -.
DR   PDBsum; 3LKW; -.
DR   PDBsum; 4AL8; -.
DR   PDBsum; 4GSX; -.
DR   PDBsum; 4GT0; -.
DR   PDBsum; 4LCY; -.
DR   PDBsum; 4OIG; -.
DR   PDBsum; 5VIC; -.
DR   PDBsum; 5WJL; -.
DR   PDBsum; 5WKF; -.
DR   SMR; P17763; -.
DR   IntAct; P17763; 1.
DR   PRIDE; P17763; -.
DR   ABCD; P17763; -.
DR   GeneID; 5075725; -.
DR   KEGG; vg:5075725; -.
DR   EvolutionaryTrace; P17763; -.
DR   PRO; PR:P17763; -.
DR   Proteomes; UP000002500; Genome.
DR   GO; GO:0039714; C:cytoplasmic viral factory; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; 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:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by 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:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR   GO; GO:0039545; P:suppression by virus of host MAVS activity; IEA:UniProtKB-KW.
DR   GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039574; P:suppression by virus of host TYK2 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0046762; P:viral budding from ER membrane; IDA:UniProtKB.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   CDD; cd12149; Flavi_E_C; 1.
DR   DisProt; DP01929; -.
DR   Gene3D; 1.10.10.930; -; 1.
DR   Gene3D; 1.10.8.970; -; 1.
DR   Gene3D; 1.20.1280.260; -; 1.
DR   Gene3D; 2.60.260.50; -; 1.
DR   Gene3D; 2.60.40.350; -; 1.
DR   Gene3D; 2.60.98.10; -; 1.
DR   Gene3D; 3.30.387.10; -; 1.
DR   Gene3D; 3.30.67.10; -; 1.
DR   InterPro; IPR011492; DEAD_Flavivir.
DR   InterPro; IPR000069; Env_glycoprot_M_flavivir.
DR   InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
DR   InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
DR   InterPro; IPR001122; Flavi_capsidC.
DR   InterPro; IPR037172; Flavi_capsidC_sf.
DR   InterPro; IPR027287; Flavi_E_Ig-like.
DR   InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
DR   InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
DR   InterPro; IPR001157; Flavi_NS1.
DR   InterPro; IPR000752; Flavi_NS2A.
DR   InterPro; IPR000487; Flavi_NS2B.
DR   InterPro; IPR000404; Flavi_NS4A.
DR   InterPro; IPR001528; Flavi_NS4B.
DR   InterPro; IPR002535; Flavi_propep.
DR   InterPro; IPR038688; Flavi_propep_sf.
DR   InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR   InterPro; IPR001850; Flavivirus_NS3_S7.
DR   InterPro; IPR014412; Gen_Poly_FLV.
DR   InterPro; IPR011998; Glycoprot_cen/dimer.
DR   InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR   InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR   InterPro; IPR013756; GlyE_cen_dom_subdom2.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR000208; RNA-dir_pol_flavivirus.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF01003; Flavi_capsid; 1.
DR   Pfam; PF07652; Flavi_DEAD; 1.
DR   Pfam; PF02832; Flavi_glycop_C; 1.
DR   Pfam; PF00869; Flavi_glycoprot; 1.
DR   Pfam; PF01004; Flavi_M; 1.
DR   Pfam; PF00948; Flavi_NS1; 1.
DR   Pfam; PF01005; Flavi_NS2A; 1.
DR   Pfam; PF01002; Flavi_NS2B; 1.
DR   Pfam; PF01350; Flavi_NS4A; 1.
DR   Pfam; PF01349; Flavi_NS4B; 1.
DR   Pfam; PF00972; Flavi_NS5; 1.
DR   Pfam; PF01570; Flavi_propep; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF00949; Peptidase_S7; 1.
DR   PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF101257; SSF101257; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF56983; SSF56983; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   TIGRFAMs; TIGR04240; flavi_E_stem; 1.
DR   PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
DR   PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activation of host autophagy by virus; ATP-binding;
KW   Capsid protein; Clathrin-mediated endocytosis of virus by host;
KW   Cleavage on pair of basic residues; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
KW   Host cytoplasm; Host endoplasmic reticulum; Host membrane;
KW   Host mitochondrion; Host nucleus; Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host MAVS by virus; Inhibition of host RLR pathway by virus;
KW   Inhibition of host STAT2 by virus; Inhibition of host TYK2 by virus;
KW   Ion channel; Ion transport; Membrane; Metal-binding; Methyltransferase;
KW   mRNA capping; mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW   Nucleotidyltransferase; Phosphoprotein; Protease; Reference proteome;
KW   RNA-binding; RNA-directed RNA polymerase; S-adenosyl-L-methionine;
KW   Secreted; Serine protease; Suppressor of RNA silencing; Transcription;
KW   Transcription regulation; Transferase; Transmembrane; Transmembrane helix;
KW   Transport; Ubl conjugation; Viral attachment to host cell;
KW   Viral envelope protein; Viral immunoevasion; Viral ion channel;
KW   Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW   Virus endocytosis by host; Virus entry into host cell; Zinc.
FT   CHAIN           1..3392
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000405207"
FT   CHAIN           1..100
FT                   /note="Capsid protein C"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000264658"
FT   PROPEP          101..114
FT                   /note="ER anchor for the capsid protein C, removed in
FT                   mature form by serine protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000264659"
FT   CHAIN           115..280
FT                   /note="Protein prM"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000264660"
FT   CHAIN           115..205
FT                   /note="Peptide pr"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000264661"
FT   CHAIN           206..280
FT                   /note="Small envelope protein M"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000264662"
FT   CHAIN           281..775
FT                   /note="Envelope protein E"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000264663"
FT   CHAIN           776..1127
FT                   /note="Non-structural protein 1"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000264664"
FT   CHAIN           1128..1345
FT                   /note="Non-structural protein 2A"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000264666"
FT   CHAIN           1346..1475
FT                   /note="Serine protease subunit NS2B"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000264667"
FT   CHAIN           1476..2094
FT                   /note="Serine protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000264668"
FT   CHAIN           2095..2221
FT                   /note="Non-structural protein 4A"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000264669"
FT   PEPTIDE         2222..2244
FT                   /note="Peptide 2k"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000264670"
FT   CHAIN           2245..2493
FT                   /note="Non-structural protein 4B"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000264671"
FT   CHAIN           2494..3392
FT                   /note="RNA-directed RNA polymerase NS5"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000264672"
FT   TOPO_DOM        1..101
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..242
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        281..725
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        726..746
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        747..752
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        753..773
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        774..1195
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1196..1220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
FT   TOPO_DOM        1221..1226
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
FT   TRANSMEM        1227..1245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
FT   TOPO_DOM        1246..1269
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
FT   TRANSMEM        1270..1290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
FT   TOPO_DOM        1291
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
FT   TRANSMEM        1292..1310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
FT   TOPO_DOM        1311..1315
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
FT   TRANSMEM        1316..1336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
FT   TOPO_DOM        1337..1351
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:23408612"
FT   TRANSMEM        1352..1370
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:26072288"
FT   TOPO_DOM        1371
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:26072288"
FT   TRANSMEM        1372..1391
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:26072288"
FT   TOPO_DOM        1392..1447
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:26072288"
FT   INTRAMEM        1448..1468
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:26072288"
FT   TOPO_DOM        1469..2148
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2149..2169
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:17276984"
FT   TOPO_DOM        2170..2171
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:17276984"
FT   INTRAMEM        2172..2192
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:17276984"
FT   TOPO_DOM        2193
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:17276984"
FT   TRANSMEM        2194..2214
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:17276984"
FT   TOPO_DOM        2215..2229
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:17276984"
FT   TRANSMEM        2230..2244
FT                   /note="Helical; Note=Signal for NS4B"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:17276984,
FT                   ECO:0000305|PubMed:16436383"
FT   TOPO_DOM        2245..2276
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:16436383"
FT   INTRAMEM        2277..2297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:16436383"
FT   TOPO_DOM        2298..2349
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:16436383"
FT   TRANSMEM        2350..2370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:16436383"
FT   TOPO_DOM        2371..2415
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:16436383"
FT   TRANSMEM        2416..2436
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:16436383"
FT   TOPO_DOM        2437..2461
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:16436383"
FT   TRANSMEM        2462..2482
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:16436383"
FT   TOPO_DOM        2483..3392
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:26072288"
FT   DOMAIN          1476..1653
FT                   /note="Peptidase S7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT   DOMAIN          1656..1812
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1822..1988
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          2495..2756
FT                   /note="mRNA cap 0-1 NS5-type MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   DOMAIN          3020..3169
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   NP_BIND         1669..1676
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   REGION          1..15
FT                   /note="Interaction with host EXOC1"
FT                   /evidence="ECO:0000269|PubMed:19889084"
FT   REGION          37..72
FT                   /note="Hydrophobic; homodimerization of capsid protein C"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   REGION          378..391
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000250|UniProtKB:P14336"
FT   REGION          1398..1437
FT                   /note="Interacts with and activates NS3 protease"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00859"
FT   REGION          1660..1663
FT                   /note="Important for RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P14340"
FT   MOTIF           1760..1763
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           2570..2573
FT                   /note="SUMO-interacting motif"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   ACT_SITE        1526
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT   ACT_SITE        1550
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT   ACT_SITE        1610
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT   ACT_SITE        2554
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   ACT_SITE        2639
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   ACT_SITE        2673
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   ACT_SITE        2709
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   METAL           2930
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   METAL           2934
FT                   /note="Zinc 1; via tele nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   METAL           2939
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   METAL           2942
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   METAL           3204
FT                   /note="Zinc 2; via tele nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   METAL           3220
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   METAL           3339
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   BINDING         2549
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2579
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2580
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2597
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2598
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2624
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2625
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2640
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2711
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            100..101
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            114..115
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            205..206
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000250|UniProtKB:P29990, ECO:0000255"
FT   SITE            280..281
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            775..776
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            1127..1128
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            1345..1346
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            1475..1476
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            1933
FT                   /note="Involved in NS3 ATPase and RTPase activities"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   SITE            1936
FT                   /note="Involved in NS3 ATPase and RTPase activities"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   SITE            2094..2095
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            2221..2222
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            2244..2245
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            2493..2494
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            2507
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2510
FT                   /note="mRNA cap binding; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2511
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2513
FT                   /note="mRNA cap binding; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2518
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2522
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2554
FT                   /note="Essential for 2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2639
FT                   /note="Essential for 2'-O-methyltransferase and N-7
FT                   methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2643
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2673
FT                   /note="Essential for 2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2704
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2706
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2709
FT                   /note="Essential for 2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   MOD_RES         2549
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT   CARBOHYD        183
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        433
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        905
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        982
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1190
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2303
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2307
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2459
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        283..310
FT                   /evidence="ECO:0000269|PubMed:14963174"
FT   DISULFID        340..401
FT                   /evidence="ECO:0000269|PubMed:14963174"
FT   DISULFID        354..385
FT                   /evidence="ECO:0000269|PubMed:14963174"
FT   DISULFID        372..396
FT                   /evidence="ECO:0000269|PubMed:14963174"
FT   DISULFID        465..565
FT                   /evidence="ECO:0000269|PubMed:14963174"
FT   DISULFID        582..613
FT                   /evidence="ECO:0000269|PubMed:14963174"
FT   DISULFID        779..790
FT                   /evidence="ECO:0000269|PubMed:14981082"
FT   DISULFID        830..918
FT                   /evidence="ECO:0000269|PubMed:14981082"
FT   DISULFID        954..998
FT                   /evidence="ECO:0000269|PubMed:14981082"
FT   DISULFID        1055..1104
FT                   /evidence="ECO:0000269|PubMed:14981082"
FT   DISULFID        1066..1088
FT                   /evidence="ECO:0000269|PubMed:14981082"
FT   DISULFID        1087..1091
FT                   /evidence="ECO:0000269|PubMed:14981082"
FT   VARIANT         125..126
FT                   /note="HM -> TL (in strain: Isolate Philippines/836-1/
FT                   1984)"
FT   VARIANT         142
FT                   /note="S -> P (in strain: Isolate Philippines/836-1/1984)"
FT   VARIANT         171..173
FT                   /note="TET -> AEA (in strain: Isolate Philippines/836-1/
FT                   1984)"
FT   VARIANT         186
FT                   /note="E -> D (in strain: Isolate Philippines/836-1/1984)"
FT   VARIANT         210
FT                   /note="A -> D (in strain: Isolate Philippines/836-1/1984)"
FT   VARIANT         251
FT                   /note="A -> G (in strain: Isolate Philippines/836-1/1984)"
FT   VARIANT         441
FT                   /note="T -> I (in strain: Isolate Philippines/836-1/1984)"
FT   VARIANT         475
FT                   /note="E -> R (in strain: Isolate Philippines/836-1/1984)"
FT   VARIANT         482
FT                   /note="E -> K (in strain: Isolate 45AZ5)"
FT   VARIANT         573
FT                   /note="T -> I (in strain: Isolate 45AZ5)"
FT   VARIANT         677
FT                   /note="S -> T (in strain: Isolate Philippines/836-1/1984)"
FT   VARIANT         786
FT                   /note="R -> K (in strain: Isolate Philippines/836-1/1984)"
FT   VARIANT         1689..1692
FT                   /note="RRNV -> KRKL (in strain: Isolate 45AZ5)"
FT   VARIANT         2242
FT                   /note="A -> V (in strain: Isolate 45AZ5)"
FT   VARIANT         2357
FT                   /note="F -> L (in strain: Isolate 45AZ5)"
FT   VARIANT         2543
FT                   /note="P -> T (in strain: Isolate 45AZ5)"
FT   VARIANT         2779
FT                   /note="G -> E (in strain: Isolate 45AZ5)"
FT   VARIANT         3337
FT                   /note="R -> Q (in strain: Isolate 45AZ5)"
FT   MUTAGEN         1138
FT                   /note="G->A: Impaired virion assembly."
FT                   /evidence="ECO:0000269|PubMed:25392211"
FT   MUTAGEN         1147
FT                   /note="E->A: Impaired virion assembly."
FT                   /evidence="ECO:0000269|PubMed:25392211"
FT   MUTAGEN         1227
FT                   /note="E->A: Impaired virion assembly."
FT                   /evidence="ECO:0000269|PubMed:25392211"
FT   MUTAGEN         1252
FT                   /note="D->A: Complete loss of viral RNA synthesis."
FT                   /evidence="ECO:0000269|PubMed:25392211"
FT   MUTAGEN         1314
FT                   /note="Q->A: Impaired virion assembly."
FT                   /evidence="ECO:0000269|PubMed:25392211"
FT   MUTAGEN         1315
FT                   /note="K->A: Impaired virion assembly."
FT                   /evidence="ECO:0000269|PubMed:25392211"
FT   MUTAGEN         1327
FT                   /note="G->A: Complete loss of viral RNA synthesis."
FT                   /evidence="ECO:0000269|PubMed:25392211"
FT   HELIX           288..290
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          291..293
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          295..308
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          311..313
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          321..332
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          334..352
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   HELIX           363..366
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          370..379
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   HELIX           381..383
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          389..409
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   HELIX           412..414
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          415..423
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          440..444
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          450..455
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   TURN            456..458
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          459..467
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   TURN            473..475
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          476..481
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          484..489
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   HELIX           490..494
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          500..504
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   HELIX           514..516
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          518..520
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          530..532
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   HELIX           537..543
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   TURN            544..546
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          547..553
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          556..559
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          562..571
FT                   /evidence="ECO:0000244|PDB:4GSX"
FT   STRAND          586..590
FT                   /evidence="ECO:0000244|PDB:4AL8"
FT   STRAND          596..598
FT                   /evidence="ECO:0000244|PDB:4GT0"
FT   STRAND          600..606
FT                   /evidence="ECO:0000244|PDB:4AL8"
FT   STRAND          612..614
FT                   /evidence="ECO:0000244|PDB:4AL8"
FT   STRAND          617..620
FT                   /evidence="ECO:0000244|PDB:4AL8"
FT   STRAND          633..635
FT                   /evidence="ECO:0000244|PDB:4AL8"
FT   STRAND          637..639
FT                   /evidence="ECO:0000244|PDB:4AL8"
FT   STRAND          645..649
FT                   /evidence="ECO:0000244|PDB:4AL8"
FT   STRAND          653..663
FT                   /evidence="ECO:0000244|PDB:4AL8"
FT   STRAND          667..673
FT                   /evidence="ECO:0000244|PDB:4AL8"
FT   TURN            956..958
FT                   /evidence="ECO:0000244|PDB:4OIG"
FT   STRAND          960..964
FT                   /evidence="ECO:0000244|PDB:4OIG"
FT   STRAND          967..971
FT                   /evidence="ECO:0000244|PDB:4OIG"
FT   STRAND          973..994
FT                   /evidence="ECO:0000244|PDB:4OIG"
FT   HELIX           1002..1004
FT                   /evidence="ECO:0000244|PDB:4OIG"
FT   HELIX           1013..1015
FT                   /evidence="ECO:0000244|PDB:4OIG"
FT   HELIX           1020..1022
FT                   /evidence="ECO:0000244|PDB:4OIG"
FT   HELIX           1028..1030
FT                   /evidence="ECO:0000244|PDB:4OIG"
FT   HELIX           1043..1045
FT                   /evidence="ECO:0000244|PDB:4OIG"
FT   STRAND          1046..1053
FT                   /evidence="ECO:0000244|PDB:4OIG"
FT   STRAND          1059..1062
FT                   /evidence="ECO:0000244|PDB:4OIG"
FT   STRAND          1073..1076
FT                   /evidence="ECO:0000244|PDB:4OIG"
FT   STRAND          1085..1090
FT                   /evidence="ECO:0000244|PDB:4OIG"
FT   STRAND          1096..1099
FT                   /evidence="ECO:0000244|PDB:4OIG"
FT   STRAND          1104..1106
FT                   /evidence="ECO:0000244|PDB:4OIG"
FT   STRAND          1111..1114
FT                   /evidence="ECO:0000244|PDB:4OIG"
FT   STRAND          1501..1504
FT                   /evidence="ECO:0000244|PDB:3LKW"
FT   STRAND          1507..1517
FT                   /evidence="ECO:0000244|PDB:3LKW"
FT   STRAND          1520..1523
FT                   /evidence="ECO:0000244|PDB:3LKW"
FT   HELIX           1525..1528
FT                   /evidence="ECO:0000244|PDB:3LKW"
FT   STRAND          1533..1535
FT                   /evidence="ECO:0000244|PDB:3LKW"
FT   STRAND          1538..1540
FT                   /evidence="ECO:0000244|PDB:3LKW"
FT   STRAND          1542..1546
FT                   /evidence="ECO:0000244|PDB:3LKW"
FT   TURN            1547..1550
FT                   /evidence="ECO:0000244|PDB:3LKW"
FT   STRAND          1551..1557
FT                   /evidence="ECO:0000244|PDB:3LKW"
FT   STRAND          1570..1574
FT                   /evidence="ECO:0000244|PDB:3LKW"
FT   STRAND          1582..1586
FT                   /evidence="ECO:0000244|PDB:3LKW"
FT   STRAND          1589..1593
FT                   /evidence="ECO:0000244|PDB:3LKW"
FT   STRAND          1596..1601
FT                   /evidence="ECO:0000244|PDB:3LKW"
FT   STRAND          1613..1615
FT                   /evidence="ECO:0000244|PDB:3LKW"
FT   STRAND          1621..1625
FT                   /evidence="ECO:0000244|PDB:3LKW"
FT   STRAND          1628..1630
FT                   /evidence="ECO:0000244|PDB:3LKW"
FT   STRAND          1636..1639
FT                   /evidence="ECO:0000244|PDB:3LKW"
SQ   SEQUENCE   3392 AA;  378702 MW;  3A7C57D3054D2972 CRC64;
     MNNQRKKTGR PSFNMLKRAR NRVSTVSQLA KRFSKGLLSG QGPMKLVMAF IAFLRFLAIP
     PTAGILARWG SFKKNGAIKV LRGFKKEISN MLNIMNRRKR SVTMLLMLLP TALAFHLTTR
     GGEPHMIVSK QERGKSLLFK TSAGVNMCTL IAMDLGELCE DTMTYKCPRI TETEPDDVDC
     WCNATETWVT YGTCSQTGEH RRDKRSVALA PHVGLGLETR TETWMSSEGA WKQIQKVETW
     ALRHPGFTVI ALFLAHAIGT SITQKGIIFI LLMLVTPSMA MRCVGIGNRD FVEGLSGATW
     VDVVLEHGSC VTTMAKDKPT LDIELLKTEV TNPAVLRKLC IEAKISNTTT DSRCPTQGEA
     TLVEEQDTNF VCRRTFVDRG WGNGCGLFGK GSLITCAKFK CVTKLEGKIV QYENLKYSVI
     VTVHTGDQHQ VGNETTEHGT TATITPQAPT SEIQLTDYGA LTLDCSPRTG LDFNEMVLLT
     MEKKSWLVHK QWFLDLPLPW TSGASTSQET WNRQDLLVTF KTAHAKKQEV VVLGSQEGAM
     HTALTGATEI QTSGTTTIFA GHLKCRLKMD KLTLKGMSYV MCTGSFKLEK EVAETQHGTV
     LVQVKYEGTD APCKIPFSSQ DEKGVTQNGR LITANPIVTD KEKPVNIEAE PPFGESYIVV
     GAGEKALKLS WFKKGSSIGK MFEATARGAR RMAILGDTAW DFGSIGGVFT SVGKLIHQIF
     GTAYGVLFSG VSWTMKIGIG ILLTWLGLNS RSTSLSMTCI AVGMVTLYLG VMVQADSGCV
     INWKGRELKC GSGIFVTNEV HTWTEQYKFQ ADSPKRLSAA IGKAWEEGVC GIRSATRLEN
     IMWKQISNEL NHILLENDMK FTVVVGDVSG ILAQGKKMIR PQPMEHKYSW KSWGKAKIIG
     ADVQNTTFII DGPNTPECPD NQRAWNIWEV EDYGFGIFTT NIWLKLRDSY TQVCDHRLMS
     AAIKDSKAVH ADMGYWIESE KNETWKLARA SFIEVKTCIW PKSHTLWSNG VLESEMIIPK
     IYGGPISQHN YRPGYFTQTA GPWHLGKLEL DFDLCEGTTV VVDEHCGNRG PSLRTTTVTG
     KTIHEWCCRS CTLPPLRFKG EDGCWYGMEI RPVKEKEENL VKSMVSAGSG EVDSFSLGLL
     CISIMIEEVM RSRWSRKMLM TGTLAVFLLL TMGQLTWNDL IRLCIMVGAN ASDKMGMGTT
     YLALMATFRM RPMFAVGLLF RRLTSREVLL LTVGLSLVAS VELPNSLEEL GDGLAMGIMM
     LKLLTDFQSH QLWATLLSLT FVKTTFSLHY AWKTMAMILS IVSLFPLCLS TTSQKTTWLP
     VLLGSLGCKP LTMFLITENK IWGRKSWPLN EGIMAVGIVS ILLSSLLKND VPLAGPLIAG
     GMLIACYVIS GSSADLSLEK AAEVSWEEEA EHSGASHNIL VEVQDDGTMK IKDEERDDTL
     TILLKATLLA ISGVYPMSIP ATLFVWYFWQ KKKQRSGVLW DTPSPPEVER AVLDDGIYRI
     LQRGLLGRSQ VGVGVFQEGV FHTMWHVTRG AVLMYQGKRL EPSWASVKKD LISYGGGWRF
     QGSWNAGEEV QVIAVEPGKN PKNVQTAPGT FKTPEGEVGA IALDFKPGTS GSPIVNREGK
     IVGLYGNGVV TTSGTYVSAI AQAKASQEGP LPEIEDEVFR KRNLTIMDLH PGSGKTRRYL
     PAIVREAIRR NVRTLVLAPT RVVASEMAEA LKGMPIRYQT TAVKSEHTGK EIVDLMCHAT
     FTMRLLSPVR VPNYNMIIMD EAHFTDPASI AARGYISTRV GMGEAAAIFM TATPPGSVEA
     FPQSNAVIQD EERDIPERSW NSGYDWITDF PGKTVWFVPS IKSGNDIANC LRKNGKRVVQ
     LSRKTFDTEY QKTKNNDWDY VVTTDISEMG ANFRADRVID PRRCLKPVIL KDGPERVILA
     GPMPVTVASA AQRRGRIGRN QNKEGDQYIY MGQPLNNDED HAHWTEAKML LDNINTPEGI
     IPALFEPERE KSAAIDGEYR LRGEARKTFV ELMRRGDLPV WLSYKVASEG FQYSDRRWCF
     DGERNNQVLE ENMDVEIWTK EGERKKLRPR WLDARTYSDP LALREFKEFA AGRRSVSGDL
     ILEIGKLPQH LTQRAQNALD NLVMLHNSEQ GGKAYRHAME ELPDTIETLM LLALIAVLTG
     GVTLFFLSGR GLGKTSIGLL CVIASSALLW MASVEPHWIA ASIILEFFLM VLLIPEPDRQ
     RTPQDNQLAY VVIGLLFMIL TAAANEMGLL ETTKKDLGIG HAAAENHHHA AMLDVDLHPA
     SAWTLYAVAT TIITPMMRHT IENTTANISL TAIANQAAIL MGLDKGWPIS KMDIGVPLLA
     LGCYSQVNPL TLTAAVFMLV AHYAIIGPGL QAKATREAQK RTAAGIMKNP TVDGIVAIDL
     DPVVYDAKFE KQLGQIMLLI LCTSQILLMR TTWALCESIT LATGPLTTLW EGSPGKFWNT
     TIAVSMANIF RGSYLAGAGL AFSLMKSLGG GRRGTGAQGE TLGEKWKRQL NQLSKSEFNT
     YKRSGIIEVD RSEAKEGLKR GEPTKHAVSR GTAKLRWFVE RNLVKPEGKV IDLGCGRGGW
     SYYCAGLKKV TEVKGYTKGG PGHEEPIPMA TYGWNLVKLY SGKDVFFTPP EKCDTLLCDI
     GESSPNPTIE EGRTLRVLKM VEPWLRGNQF CIKILNPYMP SVVETLEQMQ RKHGGMLVRN
     PLSRNSTHEM YWVSCGTGNI VSAVNMTSRM LLNRFTMAHR KPTYERDVDL GAGTRHVAVE
     PEVANLDIIG QRIENIKNGH KSTWHYDEDN PYKTWAYHGS YEVKPSGSAS SMVNGVVRLL
     TKPWDVIPMV TQIAMTDTTP FGQQRVFKEK VDTRTPKAKR GTAQIMEVTA RWLWGFLSRN
     KKPRICTREE FTRKVRSNAA IGAVFVDENQ WNSAKEAVED ERFWDLVHRE RELHKQGKCA
     TCVYNMMGKR EKKLGEFGKA KGSRAIWYMW LGARFLEFEA LGFMNEDHWF SRENSLSGVE
     GEGLHKLGYI LRDISKIPGG NMYADDTAGW DTRITEDDLQ NEAKITDIME PEHALLATSI
     FKLTYQNKVV RVQRPAKNGT VMDVISRRDQ RGSGQVGTYG LNTFTNMEAQ LIRQMESEGI
     FSPSELETPN LAERVLDWLK KHGTERLKRM AISGDDCVVK PIDDRFATAL TALNDMGKVR
     KDIPQWEPSK GWNDWQQVPF CSHHFHQLIM KDGREIVVPC RNQDELVGRA RVSQGAGWSL
     RETACLGKSY AQMWQLMYFH RRDLRLAANA ICSAVPVDWV PTSRTTWSIH AHHQWMTTED
     MLSVWNRVWI EENPWMEDKT HVSSWEDVPY LGKREDRWCG SLIGLTARAT WATNIQVAIN
     QVRRLIGNEN YLDFMTSMKR FKNESDPEGA LW
//
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