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Database: UniProt
Entry: POLG_YEFV1
LinkDB: POLG_YEFV1
Original site: POLG_YEFV1 
ID   POLG_YEFV1              Reviewed;        3411 AA.
AC   P03314; O42028; O91857; P19901; Q102J3; Q45RQ2; Q89275; Q89276; Q9W878;
AC   Q9YWN0; Q9YWN1; Q9YWN2;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   11-DEC-2019, entry version 191.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Capsid protein C;
DE     AltName: Full=Core protein;
DE   Contains:
DE     RecName: Full=Protein prM;
DE   Contains:
DE     RecName: Full=Peptide pr;
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=Non-structural protein 2A-alpha {ECO:0000303|PubMed:3008425};
DE              Short=NS2A-alpha;
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 {ECO:0000269|PubMed:21419753};
DE              EC=3.6.1.15 {ECO:0000269|PubMed:16051820};
DE              EC=3.6.4.13 {ECO:0000269|PubMed:16051820};
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   Yellow fever virus (strain 17D vaccine) (YFV).
OC   Viruses; Riboviria; Flaviviridae; Flavivirus.
OX   NCBI_TaxID=11090;
OH   NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OH   NCBI_TaxID=299629; Aedes luteocephalus (Mosquito).
OH   NCBI_TaxID=7161; Aedes simpsoni.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=314293; Simiiformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=4023707; DOI=10.1126/science.4023707;
RA   Rice C.M., Lenches E.M., Eddy S.R., Shin S.J., Sheets R.L., Strauss J.H.;
RT   "Nucleotide sequence of yellow fever virus: implications for flavivirus
RT   gene expression and evolution.";
RL   Science 229:726-733(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate 17D-213 vaccine, and Isolate 17DD vaccine;
RX   PubMed=7754673; DOI=10.1016/0168-1702(94)00076-o;
RA   dos Santos C.N., Post P.R., Carvalho R., Ferreira I.I., Rice C.M.,
RA   Galler R.;
RT   "Complete nucleotide sequence of yellow fever virus vaccine strains 17DD
RT   and 17D-213.";
RL   Virus Res. 35:35-41(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate 17D-204-USA HONG1 vaccine,
RC   Isolate 17D-204-USA HONG2 vaccine, and Isolate 17D-204-USA HONG3 vaccine;
RX   PubMed=9712515; DOI=10.1016/s0168-1702(98)00036-7;
RA   Xie H., Cass A.R., Barrett A.D.T.;
RT   "Yellow fever 17D vaccine virus isolated from healthy vaccinees accumulates
RT   very few mutations.";
RL   Virus Res. 55:93-99(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Pasteur 17D-204 vaccine;
RX   PubMed=2734112; DOI=10.1093/nar/17.10.3989;
RA   Dupuy A., Despres P., Cahour A., Girard M., Bouloy M.;
RT   "Nucleotide sequence comparison of the genome of two 17D-204 yellow fever
RT   vaccines.";
RL   Nucleic Acids Res. 17:3989-3989(1989).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate 17D-204-South Africa vaccine,
RC   Isolate 17D-204-South Africa vaccine large plaque variant, and
RC   Isolate 17D-204-South Africa vaccine medium plaque variant;
RX   PubMed=9714237; DOI=10.1099/0022-1317-79-8-1895;
RA   Xie H., Ryman K.D., Campbell G.A., Barrett A.D.T.;
RT   "Mutation in NS5 protein attenuates mouse neurovirulence of yellow fever
RT   17D vaccine virus.";
RL   J. Gen. Virol. 79:1895-1899(1998).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Spain/AVD2791-93F/2004 vaccine;
RX   PubMed=16597510; DOI=10.1016/j.jcv.2006.02.005;
RA   Doblas A., Domingo C., Bae H.G., Bohorquez C.L., de Ory F., Niedrig M.,
RA   Mora D., Carrasco F.J., Tenorio A.;
RT   "Yellow fever vaccine-associated viscerotropic disease and death in
RT   Spain.";
RL   J. Clin. Virol. 36:156-158(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Brazil/YF-VAVD/1975 vaccine;
RX   PubMed=16464518; DOI=10.1016/j.vaccine.2006.01.009;
RA   Engel A.R., Vasconcelos P.F., McArthur M.A., Barrett A.D.;
RT   "Characterization of a viscerotropic yellow fever vaccine variant from a
RT   patient in Brazil.";
RL   Vaccine 24:2803-2809(2006).
RN   [8]
RP   PROTEIN SEQUENCE OF 779-798; 1485-1497 AND 2507-2510, AND PROTEOLYTIC
RP   CLEAVAGE (GENOME POLYPROTEIN).
RX   PubMed=3008425; DOI=10.1016/0042-6822(86)90098-x;
RA   Rice C.M., Aebersold R., Teplow D.B., Pata J., Bell J.R., Vorndam A.V.,
RA   Trent D.W., Brandriss M.W., Schlesinger J.J., Strauss J.H.;
RT   "Partial N-terminal amino acid sequences of three nonstructural proteins of
RT   two flaviviruses.";
RL   Virology 151:1-9(1986).
RN   [9]
RP   PROTEIN SEQUENCE OF 2257-2276.
RX   PubMed=2922923; DOI=10.1016/0042-6822(89)90045-7;
RA   Chambers T.J., McCourt D.W., Rice C.M.;
RT   "Yellow fever virus proteins NS2A, NS2B, and NS4B: identification and
RT   partial N-terminal amino acid sequence analysis.";
RL   Virology 169:100-109(1989).
RN   [10]
RP   PROTEIN SEQUENCE OF 102-121, AND PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
RX   PubMed=8189517;
RA   Amberg S.M., Nestorowicz A., McCourt D.W., Rice C.M.;
RT   "NS2B-3 proteinase-mediated processing in the yellow fever virus structural
RT   region: in vitro and in vivo studies.";
RL   J. Virol. 68:3794-3802(1994).
RN   [11]
RP   CHARACTERIZATION (SERINE PROTEASE NS3), AND MUTAGENESIS OF HIS-1537;
RP   ASP-1561 AND SER-1622.
RX   PubMed=2147282; DOI=10.1073/pnas.87.22.8898;
RA   Chambers T.J., Weir R.C., Grakoui A., McCourt D.W., Bazan J.F.,
RA   Fletterick R.J., Rice C.M.;
RT   "Evidence that the N-terminal domain of nonstructural protein NS3 from
RT   yellow fever virus is a serine protease responsible for site-specific
RT   cleavages in the viral polyprotein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:8898-8902(1990).
RN   [12]
RP   PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
RX   PubMed=1833562;
RA   Chambers T.J., Grakoui A., Rice C.M.;
RT   "Processing of the yellow fever virus nonstructural polyprotein: a
RT   catalytically active NS3 proteinase domain and NS2B are required for
RT   cleavages at dibasic sites.";
RL   J. Virol. 65:6042-6050(1991).
RN   [13]
RP   CHARACTERIZATION (SERINE PROTEASE NS3).
RX   PubMed=7853494;
RA   Chambers T.J., Nestorowicz A., Rice C.M.;
RT   "Mutagenesis of the yellow fever virus NS2B/3 cleavage site: determinants
RT   of cleavage site specificity and effects on polyprotein processing and
RT   viral replication.";
RL   J. Virol. 69:1600-1605(1995).
RN   [14]
RP   MUTAGENESIS OF ARG-2107; ARG-2505 AND ARG-2506, AND PROTEOLYTIC CLEAVAGE
RP   (GENOME POLYPROTEIN).
RX   PubMed=8421901; DOI=10.1006/viro.1993.1076;
RA   Lin C., Chambers T.J., Rice C.M.;
RT   "Mutagenesis of conserved residues at the yellow fever virus 3/4A and 4B/5
RT   dibasic cleavage sites: effects on cleavage efficiency and polyprotein
RT   processing.";
RL   Virology 192:596-604(1993).
RN   [15]
RP   MUTAGENESIS OF ARG-2107; SER-2234 AND ARG-2506, AND PROTEOLYTIC CLEAVAGE
RP   (GENOME POLYPROTEIN).
RX   PubMed=8445732;
RA   Lin C., Amberg S.M., Chambers T.J., Rice C.M.;
RT   "Cleavage at a novel site in the NS4A region by the yellow fever virus
RT   NS2B-3 proteinase is a prerequisite for processing at the downstream 4A/4B
RT   signalase site.";
RL   J. Virol. 67:2327-2335(1993).
RN   [16]
RP   MUTAGENESIS OF PHE-1351; GLY-1352; ARG-1353; ARG-1354 AND SER-1355, AND
RP   PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
RX   PubMed=8116234; DOI=10.1006/viro.1994.1103;
RA   Nestorowicz A., Chambers T.J., Rice C.M.;
RT   "Mutagenesis of the yellow fever virus NS2A/2B cleavage site: effects on
RT   proteolytic processing, viral replication, and evidence for alternative
RT   processing of the NS2A protein.";
RL   Virology 199:114-123(1994).
RN   [17]
RP   MUTAGENESIS OF ASN-908; SER-910; ASN-986 AND THR-988.
RX   PubMed=8806496; DOI=10.1006/viro.1996.0406;
RA   Muylaert I.R., Chambers T.J., Galler R., Rice C.M.;
RT   "Mutagenesis of the N-linked glycosylation sites of the yellow fever virus
RT   NS1 protein: effects on virus replication and mouse neurovirulence.";
RL   Virology 222:159-168(1996).
RN   [18]
RP   MUTAGENESIS OF ARG-1077.
RX   PubMed=8985349;
RA   Muylaert I.R., Galler R., Rice C.M.;
RT   "Genetic analysis of the yellow fever virus NS1 protein: identification of
RT   a temperature-sensitive mutation which blocks RNA accumulation.";
RL   J. Virol. 71:291-298(1997).
RN   [19]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 1).
RX   PubMed=9371625;
RA   Lindenbach B.D., Rice C.M.;
RT   "Trans-complementation of yellow fever virus NS1 reveals a role in early
RT   RNA replication.";
RL   J. Virol. 71:9608-9617(1997).
RN   [20]
RP   PHOSPHORYLATION (RNA-DIRECTED RNA POLYMERASE NS5).
RX   PubMed=9621090;
RA   Reed K.E., Gorbalenya A.E., Rice C.M.;
RT   "The NS5A/NS5 proteins of viruses from three genera of the family
RT   flaviviridae are phosphorylated by associated serine/threonine kinases.";
RL   J. Virol. 72:6199-6206(1998).
RN   [21]
RP   INTERACTION WITH NON-STRUCTURAL PROTEIN 4A (NON-STRUCTURAL PROTEIN 1), AND
RP   INTERACTION WITH NON-STRUCTURAL PROTEIN 1 (NON-STRUCTURAL PROTEIN 4A).
RX   PubMed=10233920;
RA   Lindenbach B.D., Rice C.M.;
RT   "Genetic interaction of flavivirus nonstructural proteins NS1 and NS4A as a
RT   determinant of replicase function.";
RL   J. Virol. 73:4611-4621(1999).
RN   [22]
RP   MUTAGENESIS OF 99-ARG--ARG-101.
RX   PubMed=10482557;
RA   Amberg S.M., Rice C.M.;
RT   "Mutagenesis of the NS2B-NS3-mediated cleavage site in the flavivirus
RT   capsid protein demonstrates a requirement for coordinated processing.";
RL   J. Virol. 73:8083-8094(1999).
RN   [23]
RP   MUTAGENESIS OF 116-LEU--GLY-121.
RX   PubMed=10590087; DOI=10.1128/jvi.74.1.24-32.2000;
RA   Lee E., Stocks C.E., Amberg S.M., Rice C.M., Lobigs M.;
RT   "Mutagenesis of the signal sequence of yellow fever virus prM protein:
RT   enhancement of signalase cleavage In vitro is lethal for virus
RT   production.";
RL   J. Virol. 74:24-32(2000).
RN   [24]
RP   MUTAGENESIS OF 1406-GLU--LYS-1409.
RX   PubMed=10998334; DOI=10.1006/viro.2000.0488;
RA   Droll D.A., Krishna Murthy H.M., Chambers T.J.;
RT   "Yellow fever virus NS2B-NS3 protease: charged-to-alanine mutagenesis and
RT   deletion analysis define regions important for protease complex formation
RT   and function.";
RL   Virology 275:335-347(2000).
RN   [25]
RP   MUTAGENESIS OF 1319-GLN--THR-1321.
RX   PubMed=11967294; DOI=10.1128/jvi.76.10.4773-4784.2002;
RA   Kummerer B.M., Rice C.M.;
RT   "Mutations in the yellow fever virus nonstructural protein NS2A selectively
RT   block production of infectious particles.";
RL   J. Virol. 76:4773-4784(2002).
RN   [26]
RP   SUBUNIT (CAPSID PROTEIN C).
RX   PubMed=12768036; DOI=10.1128/jvi.77.12.7143-7149.2003;
RA   Jones C.T., Ma L., Burgner J.W., Groesch T.D., Post C.B., Kuhn R.J.;
RT   "Flavivirus capsid is a dimeric alpha-helical protein.";
RL   J. Virol. 77:7143-7149(2003).
RN   [27]
RP   SUBCELLULAR LOCATION (SMALL ENVELOPE PROTEIN M), AND SUBCELLULAR LOCATION
RP   (ENVELOPE PROTEIN E).
RX   PubMed=15507646; DOI=10.1128/jvi.78.22.12591-12602.2004;
RA   Op De Beeck A., Rouille Y., Caron M., Duvet S., Dubuisson J.;
RT   "The transmembrane domains of the prM and E proteins of yellow fever virus
RT   are endoplasmic reticulum localization signals.";
RL   J. Virol. 78:12591-12602(2004).
RN   [28]
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   [29]
RP   PHOSPHORYLATION AT SER-2562, AND MUTAGENESIS OF SER-2562.
RX   PubMed=18757072; DOI=10.1016/j.virol.2008.07.013;
RA   Bhattacharya D., Hoover S., Falk S.P., Weisblum B., Vestling M.,
RA   Striker R.;
RT   "Phosphorylation of yellow fever virus NS5 alters methyltransferase
RT   activity.";
RL   Virology 380:276-284(2008).
RN   [30]
RP   FUNCTION (SERINE PROTEASE NS3), AND MUTAGENESIS OF TRP-1833.
RX   PubMed=18199634; DOI=10.1128/jvi.02447-07;
RA   Patkar C.G., Kuhn R.J.;
RT   "Yellow Fever virus NS3 plays an essential role in virus assembly
RT   independent of its known enzymatic functions.";
RL   J. Virol. 82:3342-3352(2008).
RN   [31]
RP   FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5).
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   [32]
RP   INTERACTION WITH HUMAN PDCD6IP (SERINE PROTEASE NS3).
RX   PubMed=21044891; DOI=10.1016/j.micinf.2010.10.010;
RA   Carpp L.N., Galler R., Bonaldo M.C.;
RT   "Interaction between the yellow fever virus nonstructural protein NS3 and
RT   the host protein Alix contributes to the release of infectious particles.";
RL   Microbes Infect. 13:85-95(2011).
RN   [33]
RP   BIOPHYSICOCHEMICAL PROPERTIES (SERINE PROTEASE NS3), CATALYTIC ACTIVITY
RP   (SERINE PROTEASE NS3), AND PROTEOLYTIC CLEAVAGE (POLYPROTEIN).
RX   PubMed=21419753; DOI=10.1016/j.bbrc.2011.03.054;
RA   Kondo M.Y., Oliveira L.C., Okamoto D.N., de Araujo M.R.,
RA   Duarte dos Santos C.N., Juliano M.A., Juliano L., Gouvea I.E.;
RT   "Yellow fever virus NS2B/NS3 protease: hydrolytic properties and substrate
RT   specificity.";
RL   Biochem. Biophys. Res. Commun. 407:640-644(2011).
RN   [34]
RP   FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), UBIQUITINATION AT LYS-5
RP   (RNA-DIRECTED RNA POLYMERASE NS5), INTERACTION WITH HOST STAT2
RP   (RNA-DIRECTED RNA POLYMERASE NS5), MUTAGENESIS OF LYS-2512, AND INTERACTION
RP   WITH HOST TRIM23 (RNA-DIRECTED RNA POLYMERASE NS5).
RX   PubMed=25211074; DOI=10.1016/j.chom.2014.07.015;
RA   Laurent-Rolle M., Morrison J., Rajsbaum R., Macleod J.M., Pisanelli G.,
RA   Pham A., Ayllon J., Miorin L., Martinez-Romero C., tenOever B.R.,
RA   Garcia-Sastre A.;
RT   "The interferon signaling antagonist function of yellow fever virus NS5
RT   protein is activated by type I interferon.";
RL   Cell Host Microbe 16:314-327(2014).
RN   [35]
RP   INTERACTION WITH SERINE PROTEASE NS3 (NON-STRUCTURAL PROTEIN 2A),
RP   INTERACTION WITH NON-STRUCTURAL PROTEIN 2A (SERINE PROTEASE NS3),
RP   MUTAGENESIS OF 1152-ARG--ARG-1154; 1229-ARG--ARG-1231 AND GLN-1319, AND
RP   TOPOLOGY (NON-STRUCTURAL PROTEIN 2A).
RX   PubMed=25694595; DOI=10.1128/jvi.03351-14;
RA   Vossmann S., Wieseler J., Kerber R., Kuemmerer B.M.;
RT   "A basic cluster in the N terminus of yellow fever virus NS2A contributes
RT   to infectious particle production.";
RL   J. Virol. 89:4951-4965(2015).
RN   [36]
RP   FUNCTION (CAPSID PROTEIN C).
RX   PubMed=27849599; DOI=10.1073/pnas.1600544113;
RA   Samuel G.H., Wiley M.R., Badawi A., Adelman Z.N., Myles K.M.;
RT   "Yellow fever virus capsid protein is a potent suppressor of RNA silencing
RT   that binds double-stranded RNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:13863-13868(2016).
RN   [37]
RP   STRUCTURE BY ELECTRON MICROSCOPY (25 ANGSTROMS) OF IMMATURE PARTICLES.
RX   PubMed=12773377; DOI=10.1093/emboj/cdg270;
RA   Zhang Y., Corver J., Chipman P.R., Zhang W., Pletnev S.V., Sedlak D.,
RA   Baker T.S., Strauss J.H., Kuhn R.J., Rossmann M.G.;
RT   "Structures of immature flavivirus particles.";
RL   EMBO J. 22:2604-2613(2003).
RN   [38]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1671-2107, AND CATALYTIC ACTIVITY
RP   (SERINE PROTEASE NS3).
RX   PubMed=16051820; DOI=10.1128/jvi.79.16.10268-10277.2005;
RA   Wu J., Bera A.K., Kuhn R.J., Smith J.L.;
RT   "Structure of the Flavivirus helicase: implications for catalytic activity,
RT   protein interactions, and proteolytic processing.";
RL   J. Virol. 79:10268-10277(2005).
RN   [39] {ECO:0000244|PDB:3EVA, ECO:0000244|PDB:3EVB, ECO:0000244|PDB:3EVC, ECO:0000244|PDB:3EVD, ECO:0000244|PDB:3EVE, ECO:0000244|PDB:3EVF}
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 2507-2772 IN COMPLEX WITH GTP;
RP   GUANOSINE-P3-ADENOSINE-5',5'-TRIPHOSPHATE;
RP   P1-7-METHYLGUANOSINE-P3-ADENOSINE-5',5'-TRIPHOSPHATE AND
RP   S-ADENOSYL-L-HOMOCYSTEINE.
RX   PubMed=19101564; DOI=10.1016/j.jmb.2008.11.058;
RA   Geiss B.J., Thompson A.A., Andrews A.J., Sons R.L., Gari H.H., Keenan S.M.,
RA   Peersen O.B.;
RT   "Analysis of flavivirus NS5 methyltransferase cap binding.";
RL   J. Mol. Biol. 385:1643-1654(2009).
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. During virus entry, may
CC       induce genome penetration into the host cytoplasm after hemifusion
CC       induced by the surface proteins. Can migrate to the cell nucleus where
CC       it modulates host functions. {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering
CC       with host Dicer. {ECO:0000269|PubMed:27849599}.
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:0000250|UniProtKB:P17763}.
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. prM-E cleavage is inefficient, and
CC       many virions are only partially matured. These uncleaved prM would play
CC       a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Small envelope protein M]: May play a role in virus budding.
CC       Exerts cytotoxic effects by activating a mitochondrial apoptotic
CC       pathway through M ectodomain. May display a viroporin activity.
CC       {ECO:0000250|UniProtKB:P17763}.
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. prM-E cleavage is
CC       inefficient, and many virions are only partially matured. These
CC       uncleaved prM would play a role in immune evasion.
CC       {ECO:0000250|UniProtKB:P17763}.
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, ECO:0000269|PubMed:9371625}.
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:0000250|UniProtKB:P17763}.
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 (By similarity).
CC       {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}.
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. Also plays a role in virus
CC       assembly (PubMed:18199634). {ECO:0000255|PROSITE-ProRule:PRU00860,
CC       ECO:0000269|PubMed:18199634}.
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. {ECO:0000250|UniProtKB:Q9Q6P4}.
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:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-
CC       derived membrane vesicles where the viral replication takes place.
CC       Inhibits interferon (IFN)-induced host STAT1 phosphorylation and
CC       nuclear translocation, thereby preventing the establishment of cellular
CC       antiviral state by blocking the IFN-alpha/beta pathway
CC       (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 (PubMed:19850911). NS5 methylates viral RNA cap at guanine N-
CC       7 and ribose 2'-O positions (PubMed:19850911). Besides its role in RNA
CC       genome replication, also prevents the establishment of cellular
CC       antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta)
CC       signaling pathway (PubMed:25211074). IFN-I induces binding of NS5 to
CC       host IFN-activated transcription factor STAT2, preventing its
CC       transcriptional activity. Host TRIM23 is the E3 ligase that interacts
CC       with and polyubiquitinates NS5 to promote its binding to STAT2 and
CC       trigger IFN-I signaling inhibition (PubMed:25211074).
CC       {ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:25211074}.
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:21419753};
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         ECO:0000269|PubMed:16051820};
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         Evidence={ECO:0000269|PubMed:16051820};
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 9. {ECO:0000269|PubMed:21419753};
CC   -!- SUBUNIT: Capsid protein C: Homodimer (PubMed:12768036). Interacts (via
CC       N-terminus) with host EXOC1 (via C-terminus); this interaction results
CC       in EXOC1 degradation through the proteasome degradation pathway (By
CC       similarity). Protein prM: Forms heterodimers with envelope protein E in
CC       the endoplasmic reticulum and Golgi (By similarity). Envelope protein
CC       E: Homodimer; in the endoplasmic reticulum and Golgi. Interacts with
CC       protein prM. Interacts with non-structural protein 1 (By similarity).
CC       Non-structural protein 1: Homodimer; Homohexamer when secreted.
CC       Interacts with envelope protein E (By similarity). Non-structural
CC       protein 2A: Interacts (via N-terminus) with serine protease NS3
CC       (PubMed:25694595). Non-structural protein 2B: Forms a heterodimer with
CC       serine protease NS3. May form homooligomers (By similarity). Serine
CC       protease NS3: Forms a heterodimer with NS2B (By similarity). Interacts
CC       with non-structural protein 2A (via N-terminus) (PubMed:25694595).
CC       Interacts with NS4B (By similarity). Interacts with unphosphorylated
CC       RNA-directed RNA polymerase NS5; this interaction stimulates RNA-
CC       directed RNA polymerase NS5 guanylyltransferase activity (By
CC       similarity). NS3 interacts with host PDCD6IP; this interaction
CC       contributes to virion release (PubMed:21044891). Non-structural protein
CC       4B: Interacts with serine protease NS3 (By similarity). RNA-directed
CC       RNA polymerase NS5: Homodimer (By similarity). Interacts with host
CC       STAT2; this interaction prevents the establishment of cellular
CC       antiviral state (PubMed:25211074). Interacts with host TRIM23; this
CC       interaction leads to NS5 ubiquitination (PubMed:25211074).
CC       {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:12768036,
CC       ECO:0000269|PubMed:21044891, ECO:0000269|PubMed:25211074,
CC       ECO:0000269|PubMed:25694595}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein C]: Virion
CC       {ECO:0000250|UniProtKB:P17763}. Host nucleus
CC       {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region
CC       {ECO:0000250|UniProtKB:P17763}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Peptide pr]: Secreted
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane
CC       {ECO:0000269|PubMed:15507646}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:15507646}. Host endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:15507646}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=ER membrane retention is mediated by the
CC       transmembrane domains. {ECO:0000269|PubMed:15507646}.
CC   -!- SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane
CC       {ECO:0000305}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:15507646}. Host endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:3008425}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=ER membrane retention is mediated by the
CC       transmembrane domains. {ECO:0000269|PubMed:15507646}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted
CC       {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane;
CC       Peripheral membrane protein; Lumenal side
CC       {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles
CC       hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic
CC       reticulum membrane; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P17763}.
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:0000250|UniProtKB:P17763}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated
CC       vesicles hosting the replication complex.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:P17763}. 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; Peripheral membrane protein;
CC       Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}.
CC       Note=Located in RE-associated vesicles hosting the replication complex.
CC       NS5 protein is mainly localized in the nucleus rather than in ER
CC       vesicles. {ECO:0000250|UniProtKB:P17763}.
CC   -!- DOMAIN: The transmembrane domains of the small envelope protein M and
CC       envelope protein E contain an endoplasmic reticulum retention signal.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield
CC       mature proteins. The nascent capsid protein C contains a C-terminal
CC       hydrophobic domain that act as a signal sequence for translocation of
CC       prM into the lumen of the ER. Mature capsid protein C is cleaved at a
CC       site upstream of this hydrophobic domain by NS3. prM is cleaved in
CC       post-Golgi vesicles by a host furin, releasing the mature small
CC       envelope protein M, and peptide pr. Non-structural protein 2A-alpha, a
CC       C-terminally truncated form of non-structural protein 2A, results from
CC       partial cleavage by NS3. Specific enzymatic cleavages in vivo yield
CC       mature proteins peptide 2K acts as a signal sequence and is removed
CC       from the N-terminus of NS4B by the host signal peptidase in the ER
CC       lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-
CC       mediated cleavage at the 4A-2K site. {ECO:0000269|PubMed:1833562,
CC       ECO:0000269|PubMed:21419753, ECO:0000269|PubMed:3008425,
CC       ECO:0000269|PubMed:8116234, ECO:0000269|PubMed:8189517,
CC       ECO:0000269|PubMed:8421901, ECO:0000269|PubMed:8445732}.
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:0000250|UniProtKB:P17763}.
CC   -!- PTM: [Envelope protein E]: N-glycosylated.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is
CC       glycosylated and this is required for efficient secretion of the
CC       protein from infected cells. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: Polyubiquitinated; ubiquitination is probably mediated by host
CC       TRIM23 and is prerequisite for NS5-STAT2 interaction. NS5 is not
CC       ISGylated or sumoylated. {ECO:0000269|PubMed:25211074}.
CC   -!- PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines
CC       residues. This phosphorylation may trigger NS5 nuclear localization.
CC       {ECO:0000269|PubMed:9621090}.
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}.
DR   EMBL; X03700; CAA27332.1; -; Genomic_RNA.
DR   EMBL; X15062; CAB37419.1; -; Genomic_RNA.
DR   EMBL; U17066; AAC54267.1; -; Genomic_RNA.
DR   EMBL; U17067; AAC54268.1; -; Genomic_RNA.
DR   EMBL; AF052437; AAC35899.1; -; Genomic_RNA.
DR   EMBL; AF052438; AAC35900.1; -; Genomic_RNA.
DR   EMBL; AF052439; AAC35901.1; -; Genomic_RNA.
DR   EMBL; AF052444; AAC35906.1; -; Genomic_RNA.
DR   EMBL; AF052445; AAC35907.1; -; Genomic_RNA.
DR   EMBL; AF052446; AAC35908.1; -; Genomic_RNA.
DR   EMBL; DQ118157; AAZ31436.1; -; Genomic_RNA.
DR   EMBL; DQ100292; AAZ07885.1; -; Genomic_RNA.
DR   PIR; A03914; GNWVY.
DR   PIR; S07757; GNWVYP.
DR   RefSeq; NP_041726.1; NC_002031.1.
DR   PDB; 1NA4; EM; -; -.
DR   PDB; 1YKS; X-ray; 1.80 A; A=1671-2107.
DR   PDB; 3EVA; X-ray; 1.50 A; A=2507-2772.
DR   PDB; 3EVB; X-ray; 1.85 A; A=2507-2772.
DR   PDB; 3EVC; X-ray; 1.60 A; A=2507-2772.
DR   PDB; 3EVD; X-ray; 1.50 A; A=2507-2772.
DR   PDB; 3EVE; X-ray; 1.70 A; A=2507-2772.
DR   PDB; 3EVF; X-ray; 1.45 A; A=2507-2772.
DR   PDB; 5FFM; X-ray; 2.60 A; A=1671-2107.
DR   PDB; 5N6B; X-ray; 1.71 A; C/F=2470-2478.
DR   PDB; 6EPK; X-ray; 2.70 A; B/E=122-210.
DR   PDB; 6IW0; X-ray; 3.60 A; A=286-680.
DR   PDB; 6IW1; X-ray; 3.10 A; A/B/C=286-680.
DR   PDB; 6IW2; X-ray; 2.90 A; A/D/G/J/M/P=286-680.
DR   PDB; 6IW4; X-ray; 2.80 A; A/B=286-680.
DR   PDBsum; 1NA4; -.
DR   PDBsum; 1YKS; -.
DR   PDBsum; 3EVA; -.
DR   PDBsum; 3EVB; -.
DR   PDBsum; 3EVC; -.
DR   PDBsum; 3EVD; -.
DR   PDBsum; 3EVE; -.
DR   PDBsum; 3EVF; -.
DR   PDBsum; 5FFM; -.
DR   PDBsum; 5N6B; -.
DR   PDBsum; 6EPK; -.
DR   PDBsum; 6IW0; -.
DR   PDBsum; 6IW1; -.
DR   PDBsum; 6IW2; -.
DR   PDBsum; 6IW4; -.
DR   SMR; P03314; -.
DR   iPTMnet; P03314; -.
DR   PRIDE; P03314; -.
DR   ABCD; P03314; -.
DR   GeneID; 1502173; -.
DR   KEGG; vg:1502173; -.
DR   BRENDA; 2.7.7.50; 6740.
DR   BRENDA; 3.6.4.13; 6740.
DR   EvolutionaryTrace; P03314; -.
DR   Proteomes; UP000000360; Genome.
DR   Proteomes; UP000119912; Genome.
DR   Proteomes; UP000138083; Genome.
DR   Proteomes; UP000141075; Genome.
DR   Proteomes; UP000158765; Genome.
DR   Proteomes; UP000158778; Genome.
DR   Proteomes; UP000180827; Genome.
DR   Proteomes; UP000180883; Genome.
DR   Proteomes; UP000180940; Genome.
DR   Proteomes; UP000181442; Genome.
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: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:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IMP:CACAO.
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:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IDA:UniProtKB.
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:1900369; P:negative regulation of RNA interference; IDA:UniProtKB.
DR   GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IDA:UniProtKB.
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   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; 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; 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; Direct protein sequencing;
KW   Disulfide bond; Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein; GTP-binding;
KW   Helicase; Host cytoplasm; Host endoplasmic reticulum; Host membrane;
KW   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 STAT2 by virus; Isopeptide bond; Membrane;
KW   Metal-binding; Methyltransferase; mRNA capping; mRNA processing;
KW   Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW   Phosphoprotein; Protease; Reference proteome; RNA-binding;
KW   RNA-directed RNA polymerase; S-adenosyl-L-methionine; Secreted;
KW   Serine protease; Suppressor of RNA silencing; Transcription;
KW   Transcription regulation; Transferase; Transmembrane; Transmembrane helix;
KW   Ubl conjugation; Viral attachment to host cell; Viral envelope protein;
KW   Viral immunoevasion; Viral penetration into host cytoplasm;
KW   Viral RNA replication; Virion; Virus endocytosis by host;
KW   Virus entry into host cell; Zinc.
FT   CHAIN           1..3411
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000405153"
FT   CHAIN           1..101
FT                   /note="Capsid protein C"
FT                   /evidence="ECO:0000269|PubMed:8189517"
FT                   /id="PRO_0000037754"
FT   PROPEP          102..121
FT                   /note="ER anchor for the capsid protein C, removed in
FT                   mature form by serine protease NS3"
FT                   /evidence="ECO:0000269|PubMed:8189517"
FT                   /id="PRO_0000261384"
FT   CHAIN           122..285
FT                   /note="Protein prM"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000261385"
FT   CHAIN           122..210
FT                   /note="Peptide pr"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000037755"
FT   CHAIN           211..285
FT                   /note="Small envelope protein M"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000037756"
FT   CHAIN           286..778
FT                   /note="Envelope protein E"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000037757"
FT   CHAIN           779..1130
FT                   /note="Non-structural protein 1"
FT                   /evidence="ECO:0000269|PubMed:3008425"
FT                   /id="PRO_0000037758"
FT   CHAIN           1131..1354
FT                   /note="Non-structural protein 2A"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000037759"
FT   CHAIN           1131..1320
FT                   /note="Non-structural protein 2A-alpha"
FT                   /evidence="ECO:0000269|PubMed:8806496"
FT                   /id="PRO_0000261386"
FT   CHAIN           1355..1484
FT                   /note="Serine protease subunit NS2B"
FT                   /evidence="ECO:0000269|PubMed:3008425"
FT                   /id="PRO_0000037760"
FT   CHAIN           1485..2107
FT                   /note="Serine protease NS3"
FT                   /evidence="ECO:0000269|PubMed:1833562,
FT                   ECO:0000269|PubMed:8421901"
FT                   /id="PRO_0000037761"
FT   CHAIN           2108..2233
FT                   /note="Non-structural protein 4A"
FT                   /evidence="ECO:0000269|PubMed:8445732"
FT                   /id="PRO_0000037762"
FT   PEPTIDE         2234..2256
FT                   /note="Peptide 2k"
FT                   /evidence="ECO:0000269|PubMed:2922923"
FT                   /id="PRO_0000261387"
FT   CHAIN           2257..2506
FT                   /note="Non-structural protein 4B"
FT                   /evidence="ECO:0000269|PubMed:8421901"
FT                   /id="PRO_0000037763"
FT   CHAIN           2507..3411
FT                   /note="RNA-directed RNA polymerase NS5"
FT                   /evidence="ECO:0000269|PubMed:1833562,
FT                   ECO:0000269|PubMed:3008425"
FT                   /id="PRO_0000037764"
FT   TOPO_DOM        1..104
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..244
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        266..270
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        286..730
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        731..751
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        752..757
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        758..778
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        779..1132
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1133..1153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1154..1201
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1202..1222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1223..1287
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1288..1308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1309..1355
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1356..1376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1377..1378
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1379..1399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1400..1456
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        1457..1477
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1478..2157
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2158..2178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2179..2186
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        2187..2207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2208..2209
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2210..2230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2231..2241
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2242..2262
FT                   /note="Helical; Note=Signal for NS4B"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2263..2293
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        2294..2314
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2315..2360
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2361..2381
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2382..2421
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2422..2442
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2443..2445
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2446..2466
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2467..3411
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1485..1665
FT                   /note="Peptidase S7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT   DOMAIN          1669..1825
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1820..1997
FT                   /note="Helicase C-terminal"
FT   DOMAIN          2507..2771
FT                   /note="mRNA cap 0-1 NS5-type MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   DOMAIN          3035..3187
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   NP_BIND         1682..1689
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   REGION          38..72
FT                   /note="Hydrophobic; homodimerization of capsid protein C"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   REGION          383..396
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000250|UniProtKB:P14336"
FT   REGION          1407..1446
FT                   /note="Interacts with and activates NS3 protease"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00859"
FT   REGION          1673..1676
FT                   /note="Important for RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P14340"
FT   MOTIF           1773..1776
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           2878..2911
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        2656..2660
FT                   /note="Poly-Ser"
FT   ACT_SITE        1537
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT   ACT_SITE        1561
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT   ACT_SITE        1622
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT   ACT_SITE        2567
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   ACT_SITE        2652
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   ACT_SITE        2688
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   ACT_SITE        2724
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   METAL           2945
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   METAL           2949
FT                   /note="Zinc 1; via tele nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   METAL           2954
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   METAL           2957
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   METAL           3222
FT                   /note="Zinc 2; via tele nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   METAL           3238
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   METAL           3357
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   BINDING         2562
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2592
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2593
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2610
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2611
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2637
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2638
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2653
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2726
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            101..102
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000269|PubMed:8189517"
FT   SITE            121..122
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000269|PubMed:8189517"
FT   SITE            210..211
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            285..286
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            778..779
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000269|PubMed:3008425"
FT   SITE            1130..1131
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            1320..1321
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000269|PubMed:8806496"
FT   SITE            1354..1355
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000269|PubMed:21419753,
FT                   ECO:0000269|PubMed:8116234"
FT   SITE            1484..1485
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000269|PubMed:21419753,
FT                   ECO:0000269|PubMed:3008425"
FT   SITE            1945
FT                   /note="Involved in NS3 ATPase and RTPase activities"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   SITE            1948
FT                   /note="Involved in NS3 ATPase and RTPase activities"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   SITE            2107..2108
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000269|PubMed:21419753,
FT                   ECO:0000269|PubMed:8421901, ECO:0000269|PubMed:8445732"
FT   SITE            2233..2234
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000269|PubMed:8445732"
FT   SITE            2256..2257
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            2506..2507
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000269|PubMed:3008425,
FT                   ECO:0000269|PubMed:8421901, ECO:0000269|PubMed:8445732"
FT   SITE            2519
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT                   ECO:0000269|PubMed:19101564"
FT   SITE            2522
FT                   /note="mRNA cap binding; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT                   ECO:0000269|PubMed:19101564"
FT   SITE            2523
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT                   ECO:0000269|PubMed:19101564"
FT   SITE            2525
FT                   /note="mRNA cap binding; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT                   ECO:0000269|PubMed:19101564"
FT   SITE            2530
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2534
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT                   ECO:0000269|PubMed:19101564"
FT   SITE            2567
FT                   /note="Essential for 2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2652
FT                   /note="Essential for 2'-O-methyltransferase and N-7
FT                   methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT                   ECO:0000269|PubMed:18757072"
FT   SITE            2656
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT                   ECO:0000269|PubMed:19101564"
FT   SITE            2688
FT                   /note="Essential for 2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2719
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT                   ECO:0000269|PubMed:19101564"
FT   SITE            2721
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924,
FT                   ECO:0000269|PubMed:19101564"
FT   SITE            2724
FT                   /note="Essential for 2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   MOD_RES         2562
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18757072"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        908
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   DISULFID        288..315
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        345..406
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        345..401
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT   DISULFID        359..390
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        377..406
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT   DISULFID        377..401
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        467..568
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        585..615
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        782..793
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        833..921
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        957..1002
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        1058..1107
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        1069..1091
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        1090..1094
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   VARIANT         341
FT                   /note="V -> A (in strain: Isolate Brazil/YF-VAVD/75 vaccine
FT                   and Isolate 17DD vaccine)"
FT   VARIANT         438
FT                   /note="N -> T (in strain: Isolate 17D-204-USA HONG1
FT                   vaccine, Isolate 17D-204-USA HONG2 vaccine and Isolate 17D-
FT                   204-USA HONG3 vaccine)"
FT   VARIANT         440
FT                   /note="D -> S (in strain: Isolate 17DD vaccine)"
FT   VARIANT         610
FT                   /note="S -> P (in strain: Isolate Brazil/YF-VAVD/75 vaccine
FT                   and Isolate 17DD vaccine)"
FT   VARIANT         629
FT                   /note="I -> V (in strain: Isolate Brazil/YF-VAVD/75
FT                   vaccine)"
FT   VARIANT         701
FT                   /note="T -> V (in strain: Isolate 17DD vaccine)"
FT   VARIANT         744
FT                   /note="A -> V (in strain: Isolate 17D-204-South Africa
FT                   vaccine large plaque variant)"
FT   VARIANT         764
FT                   /note="L -> M (in strain: Isolate 17D-204-South Africa
FT                   vaccine large plaque variant)"
FT   VARIANT         1299
FT                   /note="F -> L (in strain: Isolate Brazil/YF-VAVD/75 vaccine
FT                   and Isolate 17DD vaccine)"
FT   VARIANT         1666
FT                   /note="Q -> R (in strain: Isolate 17DD vaccine)"
FT   VARIANT         1669
FT                   /note="P -> S (in strain: Isolate Brazil/YF-VAVD/75
FT                   vaccine)"
FT   VARIANT         1679
FT                   /note="V -> I (in strain: Isolate Brazil/YF-VAVD/75 vaccine
FT                   and Isolate 17DD vaccine)"
FT   VARIANT         2214
FT                   /note="V -> I (in strain: Isolate 17D-204-USA HONG1
FT                   vaccine, Isolate 17D-204-USA HONG2 vaccine, Isolate 17D-
FT                   204-USA HONG3 vaccine, Isolate Spain/AVD2791-93F/04
FT                   vaccine, Isolate Brazil/YF-VAVD/75 vaccine, Isolate 17DD
FT                   vaccine and Isolate Pasteur 17D-204 vaccine)"
FT   VARIANT         2277
FT                   /note="P -> S (in strain: Isolate Brazil/YF-VAVD/75
FT                   vaccine)"
FT   VARIANT         2401
FT                   /note="E -> K (in strain: Isolate 17D-204-South Africa
FT                   vaccine large plaque variant, Isolate 17D-204-South Africa
FT                   vaccine medium plaque variant, Isolate 17D-204-South Africa
FT                   vaccine, Isolate 17D-204-USA HONG1 vaccine, Isolate 17D-
FT                   204-USA HONG2 vaccine, Isolate 17D-204-USA HONG3 vaccine,
FT                   Isolate Brazil/YF-VAVD/75 vaccine, Isolate Spain/AVD2791-
FT                   93F/04 vaccine, Isolate 17DD vaccine and Isolate Pasteur
FT                   17D-204 vaccine)"
FT   VARIANT         2460
FT                   /note="L -> S (in strain: Isolate 17D-204-USA HONG
FT                   vaccine1, Isolate 17D-204-USA HONG2 vaccine and Isolate
FT                   17D-204-USA HONG3 vaccine)"
FT   VARIANT         2528
FT                   /note="R -> Q (in strain: Isolate Brazil/YF-VAVD/75 vaccine
FT                   and Isolate 17DD vaccine)"
FT   VARIANT         2643
FT                   /note="P -> S (in strain: Isolate 17D-204-South Africa
FT                   vaccine medium plaque variant)"
FT   VARIANT         2661
FT                   /note="V -> I (in strain: Isolate Brazil/YF-VAVD/75
FT                   vaccine)"
FT   VARIANT         2897
FT                   /note="N -> S (in strain: Isolate Brazil/YF-VAVD/75 vaccine
FT                   and Isolate 17DD vaccine)"
FT   VARIANT         3110
FT                   /note="G -> R (in strain: Isolate 17D-204-USA HONG2
FT                   vaccine)"
FT   VARIANT         3135
FT                   /note="M -> N (in strain: Isolate Brazil/YF-VAVD/75
FT                   vaccine)"
FT   VARIANT         3163
FT                   /note="D -> N (in strain: Isolate 17D-204-South Africa
FT                   vaccine large plaque variant, Isolate 17D-204-South Africa
FT                   vaccine medium plaque variant, Isolate 17D-204-South Africa
FT                   vaccine, Isolate 17D-204-USA HONG1 vaccine, Isolate 17D-
FT                   204-USA HONG2 vaccine, Isolate 17D-204-USA HONG3 vaccine,
FT                   Isolate Brazil/YF-VAVD/75 vaccine, Isolate Spain/AVD2791-
FT                   93F/04 vaccine, Isolate 17DD vaccine and Isolate Pasteur
FT                   17D-204 vaccine)"
FT   VARIANT         3222
FT                   /note="H -> R (in strain: Isolate Brazil/YF-VAVD/75
FT                   vaccine)"
FT   MUTAGEN         98..101
FT                   /note="RKRR->AAAA: Complete loss of NS2B-NS3 cleavage."
FT   MUTAGEN         98..101
FT                   /note="RKRR->AKAA: Complete loss of NS2B-NS3 cleavage."
FT   MUTAGEN         98..101
FT                   /note="RKRR->AKRA: Reduces NS2B-NS3 cleavage efficiency."
FT   MUTAGEN         98..100
FT                   /note="RKR->AAA: Complete loss of NS2B-NS3 cleavage."
FT   MUTAGEN         98..100
FT                   /note="RKR->AKA: Complete loss of NS2B-NS3 cleavage."
FT   MUTAGEN         98..99
FT                   /note="RK->AA: Reduces NS2B-NS3 cleavage efficiency."
FT   MUTAGEN         99..101
FT                   /note="KRR->ARA: Complete loss of NS2B-NS3 cleavage."
FT                   /evidence="ECO:0000269|PubMed:10482557"
FT   MUTAGEN         99..100
FT                   /note="KR->AA: Complete loss of NS2B-NS3 cleavage."
FT   MUTAGEN         100..101
FT                   /note="RR->AA: Reduces NS2B-NS3 cleavage efficiency."
FT   MUTAGEN         116..121
FT                   /note="LLMTGG->VPQAQA: Complete loss of infectious virus
FT                   production. Enhances signal peptidase cleavage in vitro of
FT                   nascent capsid protein C."
FT                   /evidence="ECO:0000269|PubMed:10590087"
FT   MUTAGEN         908
FT                   /note="N->A: Reduces viral RNA accumulation and NS1
FT                   secretion."
FT                   /evidence="ECO:0000269|PubMed:8806496"
FT   MUTAGEN         910
FT                   /note="S->A: Reduces viral RNA accumulation and NS1
FT                   secretion."
FT                   /evidence="ECO:0000269|PubMed:8806496"
FT   MUTAGEN         986
FT                   /note="N->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:8806496"
FT   MUTAGEN         988
FT                   /note="T->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:8806496"
FT   MUTAGEN         1077
FT                   /note="R->A: Blocks RNA replication."
FT                   /evidence="ECO:0000269|PubMed:8985349"
FT   MUTAGEN         1152..1154
FT                   /note="RKR->AAA: Defective in infectious particle
FT                   production; almost no effect on viral replication."
FT                   /evidence="ECO:0000269|PubMed:25694595"
FT   MUTAGEN         1229..1231
FT                   /note="RER->AAA: Defective in infectious particle
FT                   production; almost no effect on viral replication."
FT                   /evidence="ECO:0000269|PubMed:25694595"
FT   MUTAGEN         1319..1321
FT                   /note="QKT->RRS: Increases NS2A-alpha processing, complete
FT                   loss of NS2A."
FT   MUTAGEN         1319
FT                   /note="Q->A: Almost no effect on viral replication."
FT                   /evidence="ECO:0000269|PubMed:25694595"
FT   MUTAGEN         1319
FT                   /note="Q->S: Complete loss of cleavage and NS2A alpha.
FT                   Complete loss of infectivity."
FT                   /evidence="ECO:0000269|PubMed:11967294"
FT   MUTAGEN         1320
FT                   /note="K->E,I,Q,S: Complete loss of cleavage and NS2A-alpha
FT                   processing. Complete loss of infectivity."
FT                   /evidence="ECO:0000269|PubMed:11967294"
FT   MUTAGEN         1320
FT                   /note="K->R: No effect on NS2A-alpha processing."
FT                   /evidence="ECO:0000269|PubMed:11967294"
FT   MUTAGEN         1321
FT                   /note="T->V: Complete loss of cleavage and NS2A alpha
FT                   synthesis. Complete loss of infectivity."
FT                   /evidence="ECO:0000269|PubMed:11967294"
FT   MUTAGEN         1351
FT                   /note="F->C,I,V: Enhances NS2A-NS2B cleavage efficiency."
FT                   /evidence="ECO:0000269|PubMed:8116234"
FT   MUTAGEN         1351
FT                   /note="F->G: No effect on NS2A-NS2B cleavage efficiency."
FT                   /evidence="ECO:0000269|PubMed:8116234"
FT   MUTAGEN         1352
FT                   /note="G->A,K: Enhances NS2A-NS2B cleavage efficiency."
FT                   /evidence="ECO:0000269|PubMed:8116234"
FT   MUTAGEN         1352
FT                   /note="G->E,V: Reduces NS2A-NS2B cleavage efficiency."
FT                   /evidence="ECO:0000269|PubMed:8116234"
FT   MUTAGEN         1353
FT                   /note="R->H,K,R,T: Reduces NS2A-NS2B cleavage efficiency."
FT                   /evidence="ECO:0000269|PubMed:8116234"
FT   MUTAGEN         1353
FT                   /note="R->L,P: Complete loss of NS2A-NS2B cleavage."
FT                   /evidence="ECO:0000269|PubMed:8116234"
FT   MUTAGEN         1354
FT                   /note="R->I,N,S,T: Complete loss of NS2A-NS2B cleavage."
FT                   /evidence="ECO:0000269|PubMed:8116234"
FT   MUTAGEN         1354
FT                   /note="R->K: Reduces of NS2A-NS2B cleavage efficiency."
FT                   /evidence="ECO:0000269|PubMed:8116234"
FT   MUTAGEN         1355
FT                   /note="S->D,K,R,V: Complete loss of NS2A-NS2B cleavage."
FT                   /evidence="ECO:0000269|PubMed:8116234"
FT   MUTAGEN         1355
FT                   /note="S->G: Reduces of NS2A-NS2B cleavage efficiency."
FT                   /evidence="ECO:0000269|PubMed:8116234"
FT   MUTAGEN         1406..1409
FT                   /note="ELKK->ALAA: Complete loss of polyprotein cleavage."
FT                   /evidence="ECO:0000269|PubMed:10998334"
FT   MUTAGEN         1537
FT                   /note="H->A: Complete loss NS3 protease activity."
FT                   /evidence="ECO:0000269|PubMed:2147282"
FT   MUTAGEN         1561
FT                   /note="D->A,N: Complete loss NS3 protease activity."
FT                   /evidence="ECO:0000269|PubMed:2147282"
FT   MUTAGEN         1622
FT                   /note="S->A: Complete loss NS3 protease activity."
FT                   /evidence="ECO:0000269|PubMed:2147282"
FT   MUTAGEN         1622
FT                   /note="S->C: Diminishes NS3 protease activity."
FT                   /evidence="ECO:0000269|PubMed:2147282"
FT   MUTAGEN         1833
FT                   /note="W->A: Complete loss of production of infectious
FT                   virus particles."
FT                   /evidence="ECO:0000269|PubMed:18199634"
FT   MUTAGEN         2107
FT                   /note="R->A,L,M,T,V: Reduces NS4A-NS4B cleavage
FT                   efficiency."
FT                   /evidence="ECO:0000269|PubMed:8421901"
FT   MUTAGEN         2107
FT                   /note="R->E: Complete loss of NS4A-NS4B cleavage."
FT                   /evidence="ECO:0000269|PubMed:8421901,
FT                   ECO:0000269|PubMed:8445732"
FT   MUTAGEN         2107
FT                   /note="R->K: No effect on NS4A-NS4B cleavage efficiency."
FT                   /evidence="ECO:0000269|PubMed:8421901"
FT   MUTAGEN         2107
FT                   /note="R->P: Complete loss of NS4A-NS4B cleavage."
FT                   /evidence="ECO:0000269|PubMed:8421901"
FT   MUTAGEN         2234
FT                   /note="S->A,T: No effect on NS4A-NS4B cleavage."
FT                   /evidence="ECO:0000269|PubMed:8445732"
FT   MUTAGEN         2234
FT                   /note="S->I,P: No effect on NS4A-NS4B cleavage."
FT                   /evidence="ECO:0000269|PubMed:8445732"
FT   MUTAGEN         2505
FT                   /note="R->A,I,L,Q,S,T: No effect on NS4B-NS5 cleavage
FT                   efficiency."
FT                   /evidence="ECO:0000269|PubMed:8421901"
FT   MUTAGEN         2505
FT                   /note="R->P: Reduces NS4B-NS5 cleavage efficiency."
FT                   /evidence="ECO:0000269|PubMed:8421901"
FT   MUTAGEN         2506
FT                   /note="R->E: Complete loss of NS4B-NS5 cleavage."
FT                   /evidence="ECO:0000269|PubMed:8421901,
FT                   ECO:0000269|PubMed:8445732"
FT   MUTAGEN         2506
FT                   /note="R->H,N,Q: Reduces NS4B-NS5 cleavage efficiency."
FT                   /evidence="ECO:0000269|PubMed:8421901"
FT   MUTAGEN         2506
FT                   /note="R->K: No effect on NS4B-NS5 cleavage efficiency."
FT                   /evidence="ECO:0000269|PubMed:8421901"
FT   MUTAGEN         2506
FT                   /note="R->Y: Complete loss of NS4B-NS5 cleavage."
FT                   /evidence="ECO:0000269|PubMed:8421901"
FT   MUTAGEN         2507
FT                   /note="G->A,S: Reduces NS4B-NS5 cleavage efficiency."
FT   MUTAGEN         2507
FT                   /note="G->E,K,L,M,N,V: Reduces NS4B-NS5 cleavage
FT                   efficiency."
FT   MUTAGEN         2512
FT                   /note="K->R: Completet loss of NS5 binding to STAT2 after
FT                   IFN-I stimulation."
FT                   /evidence="ECO:0000269|PubMed:25211074"
FT   MUTAGEN         2562
FT                   /note="S->A: Complete loss of 2'-O-MTase activity."
FT                   /evidence="ECO:0000269|PubMed:18757072"
FT   STRAND          123..127
FT                   /evidence="ECO:0000244|PDB:6EPK"
FT   STRAND          130..134
FT                   /evidence="ECO:0000244|PDB:6EPK"
FT   HELIX           137..139
FT                   /evidence="ECO:0000244|PDB:6EPK"
FT   STRAND          143..146
FT                   /evidence="ECO:0000244|PDB:6EPK"
FT   STRAND          149..153
FT                   /evidence="ECO:0000244|PDB:6EPK"
FT   STRAND          160..169
FT                   /evidence="ECO:0000244|PDB:6EPK"
FT   STRAND          183..188
FT                   /evidence="ECO:0000244|PDB:6EPK"
FT   STRAND          191..199
FT                   /evidence="ECO:0000244|PDB:6EPK"
FT   TURN            288..290
FT                   /evidence="ECO:0000244|PDB:6IW2"
FT   STRAND          292..298
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          305..311
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          315..319
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          326..335
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          340..357
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          370..385
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   HELIX           386..388
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          394..414
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   HELIX           417..419
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          421..428
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   HELIX           434..439
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          442..446
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          453..456
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          460..465
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          468..470
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   TURN            473..475
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          479..483
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          486..490
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   HELIX           492..496
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          505..507
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   HELIX           513..516
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          517..519
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          529..531
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   HELIX           536..542
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   TURN            543..545
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          548..551
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          559..562
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          565..571
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          582..584
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          589..597
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          599..601
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          603..611
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          613..616
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          619..626
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          633..636
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          640..643
FT                   /evidence="ECO:0000244|PDB:6IW1"
FT   STRAND          646..653
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          656..666
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          670..676
FT                   /evidence="ECO:0000244|PDB:6IW4"
FT   STRAND          1677..1680
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   TURN            1688..1691
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   HELIX           1692..1702
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          1707..1713
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   HELIX           1714..1723
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   TURN            1724..1726
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          1729..1731
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          1746..1750
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   HELIX           1751..1758
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          1760..1762
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          1768..1772
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   TURN            1773..1776
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   HELIX           1780..1794
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          1799..1803
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          1821..1825
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          1834..1836
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   HELIX           1839..1842
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          1847..1850
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   HELIX           1854..1866
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          1871..1873
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          1876..1878
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          1892..1899
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          1909..1913
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          1916..1923
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   TURN            1924..1927
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          1928..1936
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   HELIX           1939..1946
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          1958..1962
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   HELIX           1974..1983
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   HELIX           1989..1991
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   HELIX           2000..2003
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          2004..2006
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   TURN            2008..2011
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   HELIX           2015..2026
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   HELIX           2032..2040
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   HELIX           2049..2051
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   HELIX           2056..2058
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          2063..2065
FT                   /evidence="ECO:0000244|PDB:5FFM"
FT   STRAND          2069..2071
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          2077..2079
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          2083..2086
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   HELIX           2087..2089
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   STRAND          2090..2092
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   HELIX           2093..2103
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   TURN            2104..2106
FT                   /evidence="ECO:0000244|PDB:1YKS"
FT   HELIX           2514..2524
FT                   /evidence="ECO:0000244|PDB:3EVF"
FT   HELIX           2527..2534
FT                   /evidence="ECO:0000244|PDB:3EVF"
FT   STRAND          2536..2541
FT                   /evidence="ECO:0000244|PDB:3EVF"
FT   HELIX           2544..2551
FT                   /evidence="ECO:0000244|PDB:3EVF"
FT   HELIX           2564..2573
FT                   /evidence="ECO:0000244|PDB:3EVF"
FT   STRAND          2581..2586
FT                   /evidence="ECO:0000244|PDB:3EVF"
FT   HELIX           2592..2598
FT                   /evidence="ECO:0000244|PDB:3EVF"
FT   STRAND          2603..2609
FT                   /evidence="ECO:0000244|PDB:3EVF"
FT   HELIX           2627..2629
FT                   /evidence="ECO:0000244|PDB:3EVF"
FT   STRAND          2630..2633
FT                   /evidence="ECO:0000244|PDB:3EVF"
FT   TURN            2638..2640
FT                   /evidence="ECO:0000244|PDB:3EVF"
FT   STRAND          2647..2651
FT                   /evidence="ECO:0000244|PDB:3EVF"
FT   HELIX           2660..2678
FT                   /evidence="ECO:0000244|PDB:3EVF"
FT   TURN            2679..2681
FT                   /evidence="ECO:0000244|PDB:3EVD"
FT   STRAND          2683..2690
FT                   /evidence="ECO:0000244|PDB:3EVF"
FT   HELIX           2695..2708
FT                   /evidence="ECO:0000244|PDB:3EVF"
FT   STRAND          2711..2713
FT                   /evidence="ECO:0000244|PDB:3EVF"
FT   STRAND          2725..2730
FT                   /evidence="ECO:0000244|PDB:3EVF"
FT   HELIX           2735..2751
FT                   /evidence="ECO:0000244|PDB:3EVF"
FT   STRAND          2757..2760
FT                   /evidence="ECO:0000244|PDB:3EVF"
SQ   SEQUENCE   3411 AA;  379518 MW;  680E0FACD23DCFA6 CRC64;
     MSGRKAQGKT LGVNMVRRGV RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF FLFNILTGKK
     ITAHLKRLWK MLDPRQGLAV LRKVKRVVAS LMRGLSSRKR RSHDVLTVQF LILGMLLMTG
     GVTLVRKNRW LLLNVTSEDL GKTFSVGTGN CTTNILEAKY WCPDSMEYNC PNLSPREEPD
     DIDCWCYGVE NVRVAYGKCD SAGRSRRSRR AIDLPTHENH GLKTRQEKWM TGRMGERQLQ
     KIERWFVRNP FFAVTALTIA YLVGSNMTQR VVIALLVLAV GPAYSAHCIG ITDRDFIEGV
     HGGTWVSATL EQDKCVTVMA PDKPSLDISL ETVAIDRPAE VRKVCYNAVL THVKINDKCP
     STGEAHLAEE NEGDNACKRT YSDRGWGNGC GLFGKGSIVA CAKFTCAKSM SLFEVDQTKI
     QYVIRAQLHV GAKQENWNTD IKTLKFDALS GSQEVEFIGY GKATLECQVQ TAVDFGNSYI
     AEMETESWIV DRQWAQDLTL PWQSGSGGVW REMHHLVEFE PPHAATIRVL ALGNQEGSLK
     TALTGAMRVT KDTNDNNLYK LHGGHVSCRV KLSALTLKGT SYKICTDKMF FVKNPTDTGH
     GTVVMQVKVS KGAPCRIPVI VADDLTAAIN KGILVTVNPI ASTNDDEVLI EVNPPFGDSY
     IIVGRGDSRL TYQWHKEGSS IGKLFTQTMK GVERLAVMGD TAWDFSSAGG FFTSVGKGIH
     TVFGSAFQGL FGGLNWITKV IMGAVLIWVG INTRNMTMSM SMILVGVIMM FLSLGVGADQ
     GCAINFGKRE LKCGDGIFIF RDSDDWLNKY SYYPEDPVKL ASIVKASFEE GKCGLNSVDS
     LEHEMWRSRA DEINAIFEEN EVDISVVVQD PKNVYQRGTH PFSRIRDGLQ YGWKTWGKNL
     VFSPGRKNGS FIIDGKSRKE CPFSNRVWNS FQIEEFGTGV FTTRVYMDAV FEYTIDCDGS
     ILGAAVNGKK SAHGSPTFWM GSHEVNGTWM IHTLEALDYK ECEWPLTHTI GTSVEESEMF
     MPRSIGGPVS SHNHIPGYKV QTNGPWMQVP LEVKREACPG TSVIIDGNCD GRGKSTRSTT
     DSGKVIPEWC CRSCTMPPVS FHGSDGCWYP MEIRPRKTHE SHLVRSWVTA GEIHAVPFGL
     VSMMIAMEVV LRKRQGPKQM LVGGVVLLGA MLVGQVTLLD LLKLTVAVGL HFHEMNNGGD
     AMYMALIAAF SIRPGLLIGF GLRTLWSPRE RLVLTLGAAM VEIALGGVMG GLWKYLNAVS
     LCILTINAVA SRKASNTILP LMALLTPVTM AEVRLAAMFF CAVVIIGVLH QNFKDTSMQK
     TIPLVALTLT SYLGLTQPFL GLCAFLATRI FGRRSIPVNE ALAAAGLVGV LAGLAFQEME
     NFLGPIAVGG LLMMLVSVAG RVDGLELKKL GEVSWEEEAE ISGSSARYDV ALSEQGEFKL
     LSEEKVPWDQ VVMTSLALVG AALHPFALLL VLAGWLFHVR GARRSGDVLW DIPTPKIIEE
     CEHLEDGIYG IFQSTFLGAS QRGVGVAQGG VFHTMWHVTR GAFLVRNGKK LIPSWASVKE
     DLVAYGGSWK LEGRWDGEEE VQLIAAVPGK NVVNVQTKPS LFKVRNGGEI GAVALDYPSG
     TSGSPIVNRN GEVIGLYGNG ILVGDNSFVS AISQTEVKEE GKEELQEIPT MLKKGMTTVL
     DFHPGAGKTR RFLPQILAEC ARRRLRTLVL APTRVVLSEM KEAFHGLDVK FHTQAFSAHG
     SGREVIDAMC HATLTYRMLE PTRVVNWEVI IMDEAHFLDP ASIAARGWAA HRARANESAT
     ILMTATPPGT SDEFPHSNGE IEDVQTDIPS EPWNTGHDWI LADKRPTAWF LPSIRAANVM
     AASLRKAGKS VVVLNRKTFE REYPTIKQKK PDFILATDIA EMGANLCVER VLDCRTAFKP
     VLVDEGRKVA IKGPLRISAS SAAQRRGRIG RNPNRDGDSY YYSEPTSENN AHHVCWLEAS
     MLLDNMEVRG GMVAPLYGVE GTKTPVSPGE MRLRDDQRKV FRELVRNCDL PVWLSWQVAK
     AGLKTNDRKW CFEGPEEHEI LNDSGETVKC RAPGGAKKPL RPRWCDERVS SDQSALSEFI
     KFAEGRRGAA EVLVVLSELP DFLAKKGGEA MDTISVFLHS EEGSRAYRNA LSMMPEAMTI
     VMLFILAGLL TSGMVIFFMS PKGISRMSMA MGTMAGCGYL MFLGGVKPTH ISYVMLIFFV
     LMVVVIPEPG QQRSIQDNQV AYLIIGILTL VSAVAANELG MLEKTKEDLF GKKNLIPSSA
     SPWSWPDLDL KPGAAWTVYV GIVTMLSPML HHWIKVEYGN LSLSGIAQSA SVLSFMDKGI
     PFMKMNISVI MLLVSGWNSI TVMPLLCGIG CAMLHWSLIL PGIKAQQSKL AQRRVFHGVA
     ENPVVDGNPT VDIEEAPEMP ALYEKKLALY LLLALSLASV AMCRTPFSLA EGIVLASAAL
     GPLIEGNTSL LWNGPMAVSM TGVMRGNHYA FVGVMYNLWK MKTGRRGSAN GKTLGEVWKR
     ELNLLDKRQF ELYKRTDIVE VDRDTARRHL AEGKVDTGVA VSRGTAKLRW FHERGYVKLE
     GRVIDLGCGR GGWCYYAAAQ KEVSGVKGFT LGRDGHEKPM NVQSLGWNII TFKDKTDIHR
     LEPVKCDTLL CDIGESSSSS VTEGERTVRV LDTVEKWLAC GVDNFCVKVL APYMPDVLEK
     LELLQRRFGG TVIRNPLSRN STHEMYYVSG ARSNVTFTVN QTSRLLMRRM RRPTGKVTLE
     ADVILPIGTR SVETDKGPLD KEAIEERVER IKSEYMTSWF YDNDNPYRTW HYCGSYVTKT
     SGSAASMVNG VIKILTYPWD RIEEVTRMAM TDTTPFGQQR VFKEKVDTRA KDPPAGTRKI
     MKVVNRWLFR HLAREKNPRL CTKEEFIAKV RSHAAIGAYL EEQEQWKTAN EAVQDPKFWE
     LVDEERKLHQ QGRCRTCVYN MMGKREKKLS EFGKAKGSRA IWYMWLGARY LEFEALGFLN
     EDHWASRENS GGGVEGIGLQ YLGYVIRDLA AMDGGGFYAD DTAGWDTRIT EADLDDEQEI
     LNYMSPHHKK LAQAVMEMTY KNKVVKVLRP APGGKAYMDV ISRRDQRGSG QVVTYALNTI
     TNLKVQLIRM AEAEMVIHHQ HVQDCDESVL TRLEAWLTEH GCDRLKRMAV SGDDCVVRPI
     DDRFGLALSH LNAMSKVRKD ISEWQPSKGW NDWENVPFCS HHFHELQLKD GRRIVVPCRE
     QDELIGRGRV SPGNGWMIKE TACLSKAYAN MWSLMYFHKR DMRLLSLAVS SAVPTSWVPQ
     GRTTWSIHGK GEWMTTEDML EVWNRVWITN NPHMQDKTMV KKWRDVPYLT KRQDKLCGSL
     IGMTNRATWA SHIHLVIHRI RTLIGQEKYT DYLTVMDRYS VDADLQLGEL I
//
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