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 03-AUG-2022, entry version 204.
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; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; 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; DOI=10.1128/jvi.68.6.3794-3802.1994;
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; DOI=10.1128/jvi.65.11.6042-6050.1991;
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; DOI=10.1128/jvi.69.3.1600-1605.1995;
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; DOI=10.1128/jvi.67.4.2327-2335.1993;
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; DOI=10.1128/jvi.71.1.291-298.1997;
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; DOI=10.1128/jvi.71.12.9608-9617.1997;
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; DOI=10.1128/jvi.72.7.6199-6206.1998;
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; DOI=10.1128/jvi.73.6.4611-4621.1999;
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; DOI=10.1128/jvi.73.10.8083-8094.1999;
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:0007744|PDB:3EVA, ECO:0007744|PDB:3EVB, ECO:0007744|PDB:3EVC, ECO:0007744|PDB:3EVD, ECO:0007744|PDB:3EVE, ECO:0007744|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:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539,
CC 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)-(ribonucleoside) in mRNA +
CC S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC ChEBI:CHEBI:167617; 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)-ribonucleoside
CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
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
CC (via N-terminus) with host EXOC1 (via C-terminus); this interaction
CC results in EXOC1 degradation through the proteasome degradation pathway
CC (By similarity). {ECO:0000250|UniProtKB:P17763,
CC ECO:0000269|PubMed:12768036}.
CC -!- SUBUNIT: [Protein prM]: Forms heterodimers with envelope protein E in
CC the endoplasmic reticulum and Golgi (By similarity).
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Envelope protein E]: Homodimer; in the endoplasmic reticulum
CC and Golgi (By similarity). Interacts with protein prM (By similarity).
CC Interacts with non-structural protein 1 (By similarity).
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Non-structural protein 1]: Homodimer; Homohexamer when
CC secreted (By similarity). Interacts with envelope protein E (By
CC similarity). {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Non-structural protein 2A]: Interacts (via N-terminus) with
CC serine protease NS3 (PubMed:25694595). {ECO:0000269|PubMed:25694595}.
CC -!- SUBUNIT: [Serine protease subunit NS2B]: Forms a heterodimer with
CC serine protease NS3 (By similarity). May form homooligomers (By
CC similarity). {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Serine protease NS3]: Forms a heterodimer with NS2B (By
CC similarity). Interacts with non-structural protein 2A (via N-terminus)
CC (PubMed:25694595). Interacts with NS4B (By similarity). Interacts with
CC unphosphorylated RNA-directed RNA polymerase NS5; this interaction
CC stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity
CC (By similarity). NS3 interacts with host PDCD6IP; this interaction
CC contributes to virion release (PubMed:21044891).
CC {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:21044891,
CC ECO:0000269|PubMed:25694595}.
CC -!- SUBUNIT: [Non-structural protein 4B]: Interacts with serine protease
CC NS3 (By similarity). {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [RNA-directed RNA polymerase NS5]: Homodimer (By similarity).
CC Interacts with host STAT2; this interaction prevents the establishment
CC of cellular antiviral state (PubMed:25211074). Interacts with serine
CC protease NS3 (By similarity). Interacts with host TRIM23; this
CC interaction leads to NS5 ubiquitination (PubMed:25211074).
CC {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:25211074}.
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}.
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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 PDB; 6QSN; X-ray; 3.00 A; A/B=2507-3411.
DR PDB; 6SS7; X-ray; 2.50 A; C/F=2470-2478.
DR PDB; 6SS8; X-ray; 2.24 A; C/F=2470-2478.
DR PDB; 6SS9; X-ray; 2.70 A; C/F=2470-2478.
DR PDB; 6SSA; X-ray; 2.11 A; C/F/I/L=2470-2478.
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 PDBsum; 6QSN; -.
DR PDBsum; 6SS7; -.
DR PDBsum; 6SS8; -.
DR PDBsum; 6SS9; -.
DR PDBsum; 6SSA; -.
DR BMRB; P03314; -.
DR SMR; P03314; -.
DR ChEMBL; CHEMBL4523585; -.
DR MEROPS; S07.001; -.
DR iPTMnet; P03314; -.
DR PRIDE; P03314; -.
DR ABCD; P03314; 7 sequenced antibodies.
DR GeneID; 1502173; -.
DR KEGG; vg:1502173; -.
DR BRENDA; 2.7.7.50; 6740.
DR BRENDA; 3.4.21.91; 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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039564; P:suppression by virus of host JAK-STAT cascade via inhibition of 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:0140533; P:suppression of host RNAi-mediated antiviral immune response; IDA:UniProtKB.
DR GO; GO:0046762; P:viral budding from endoplasmic reticulum 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; cd20761; capping_2-OMTase_Flaviviridae; 1.
DR CDD; cd12149; Flavi_E_C; 1.
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 Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011492; DEAD_Flavivir.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
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; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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; SSF56672; SSF56672; 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 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 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 BINDING 1682..1689
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 2562
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2592
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2593
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2610
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2611
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2637
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2638
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2653
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2726
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2945
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2949
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2954
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2957
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
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:0007829|PDB:6EPK"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:6EPK"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:6EPK"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:6EPK"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:6EPK"
FT STRAND 160..169
FT /evidence="ECO:0007829|PDB:6EPK"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:6EPK"
FT STRAND 191..199
FT /evidence="ECO:0007829|PDB:6EPK"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:6IW2"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 305..311
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 326..335
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 340..357
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 370..385
FT /evidence="ECO:0007829|PDB:6IW4"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 394..414
FT /evidence="ECO:0007829|PDB:6IW4"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 421..428
FT /evidence="ECO:0007829|PDB:6IW4"
FT HELIX 434..439
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 442..446
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 460..465
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:6IW4"
FT TURN 473..475
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 479..483
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:6IW4"
FT HELIX 492..496
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:6IW4"
FT HELIX 513..516
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:6IW4"
FT HELIX 536..542
FT /evidence="ECO:0007829|PDB:6IW4"
FT TURN 543..545
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 548..551
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 559..562
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 565..571
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 582..584
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 589..597
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 599..601
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 603..611
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 619..626
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 633..636
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 640..643
FT /evidence="ECO:0007829|PDB:6IW1"
FT STRAND 646..653
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 656..666
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 670..676
FT /evidence="ECO:0007829|PDB:6IW4"
FT STRAND 1677..1680
FT /evidence="ECO:0007829|PDB:1YKS"
FT TURN 1688..1691
FT /evidence="ECO:0007829|PDB:1YKS"
FT HELIX 1692..1702
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 1707..1713
FT /evidence="ECO:0007829|PDB:1YKS"
FT HELIX 1714..1723
FT /evidence="ECO:0007829|PDB:1YKS"
FT TURN 1724..1726
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 1729..1731
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 1746..1750
FT /evidence="ECO:0007829|PDB:1YKS"
FT HELIX 1751..1758
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 1760..1762
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 1768..1772
FT /evidence="ECO:0007829|PDB:1YKS"
FT TURN 1773..1776
FT /evidence="ECO:0007829|PDB:1YKS"
FT HELIX 1780..1794
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 1799..1803
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 1821..1825
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 1834..1836
FT /evidence="ECO:0007829|PDB:1YKS"
FT HELIX 1839..1842
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 1847..1850
FT /evidence="ECO:0007829|PDB:1YKS"
FT HELIX 1854..1866
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 1871..1873
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 1876..1878
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 1892..1899
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 1909..1913
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 1916..1923
FT /evidence="ECO:0007829|PDB:1YKS"
FT TURN 1924..1927
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 1928..1936
FT /evidence="ECO:0007829|PDB:1YKS"
FT HELIX 1939..1946
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 1958..1962
FT /evidence="ECO:0007829|PDB:1YKS"
FT HELIX 1974..1983
FT /evidence="ECO:0007829|PDB:1YKS"
FT HELIX 1989..1991
FT /evidence="ECO:0007829|PDB:1YKS"
FT HELIX 2000..2003
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 2004..2006
FT /evidence="ECO:0007829|PDB:1YKS"
FT TURN 2008..2011
FT /evidence="ECO:0007829|PDB:1YKS"
FT HELIX 2015..2026
FT /evidence="ECO:0007829|PDB:1YKS"
FT HELIX 2032..2040
FT /evidence="ECO:0007829|PDB:1YKS"
FT HELIX 2049..2051
FT /evidence="ECO:0007829|PDB:1YKS"
FT HELIX 2056..2058
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 2063..2065
FT /evidence="ECO:0007829|PDB:5FFM"
FT STRAND 2069..2071
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 2077..2079
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 2083..2086
FT /evidence="ECO:0007829|PDB:1YKS"
FT HELIX 2087..2089
FT /evidence="ECO:0007829|PDB:1YKS"
FT STRAND 2090..2092
FT /evidence="ECO:0007829|PDB:1YKS"
FT HELIX 2093..2103
FT /evidence="ECO:0007829|PDB:1YKS"
FT TURN 2104..2106
FT /evidence="ECO:0007829|PDB:1YKS"
FT HELIX 2514..2524
FT /evidence="ECO:0007829|PDB:3EVF"
FT HELIX 2527..2534
FT /evidence="ECO:0007829|PDB:3EVF"
FT STRAND 2536..2541
FT /evidence="ECO:0007829|PDB:3EVF"
FT HELIX 2544..2551
FT /evidence="ECO:0007829|PDB:3EVF"
FT STRAND 2561..2563
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 2564..2573
FT /evidence="ECO:0007829|PDB:3EVF"
FT STRAND 2581..2586
FT /evidence="ECO:0007829|PDB:3EVF"
FT HELIX 2592..2598
FT /evidence="ECO:0007829|PDB:3EVF"
FT STRAND 2603..2609
FT /evidence="ECO:0007829|PDB:3EVF"
FT HELIX 2627..2629
FT /evidence="ECO:0007829|PDB:3EVF"
FT STRAND 2630..2633
FT /evidence="ECO:0007829|PDB:3EVF"
FT TURN 2638..2640
FT /evidence="ECO:0007829|PDB:3EVF"
FT STRAND 2647..2651
FT /evidence="ECO:0007829|PDB:3EVF"
FT HELIX 2660..2678
FT /evidence="ECO:0007829|PDB:3EVF"
FT TURN 2679..2681
FT /evidence="ECO:0007829|PDB:3EVD"
FT STRAND 2683..2690
FT /evidence="ECO:0007829|PDB:3EVF"
FT HELIX 2695..2708
FT /evidence="ECO:0007829|PDB:3EVF"
FT STRAND 2711..2713
FT /evidence="ECO:0007829|PDB:3EVF"
FT STRAND 2725..2730
FT /evidence="ECO:0007829|PDB:3EVF"
FT HELIX 2735..2751
FT /evidence="ECO:0007829|PDB:3EVF"
FT STRAND 2757..2760
FT /evidence="ECO:0007829|PDB:3EVF"
FT HELIX 2781..2794
FT /evidence="ECO:0007829|PDB:6QSN"
FT TURN 2795..2798
FT /evidence="ECO:0007829|PDB:6QSN"
FT STRAND 2808..2819
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 2830..2835
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 2837..2839
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 2843..2846
FT /evidence="ECO:0007829|PDB:6QSN"
FT STRAND 2848..2850
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 2855..2865
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 2875..2892
FT /evidence="ECO:0007829|PDB:6QSN"
FT TURN 2893..2895
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 2903..2909
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 2929..2932
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 2936..2950
FT /evidence="ECO:0007829|PDB:6QSN"
FT STRAND 2959..2963
FT /evidence="ECO:0007829|PDB:6QSN"
FT STRAND 2967..2969
FT /evidence="ECO:0007829|PDB:6QSN"
FT STRAND 2980..2983
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 2986..2996
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 2998..3001
FT /evidence="ECO:0007829|PDB:6QSN"
FT TURN 3002..3005
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3007..3010
FT /evidence="ECO:0007829|PDB:6QSN"
FT STRAND 3011..3013
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3019..3031
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3045..3048
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3051..3057
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3058..3063
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3066..3078
FT /evidence="ECO:0007829|PDB:6QSN"
FT TURN 3079..3081
FT /evidence="ECO:0007829|PDB:6QSN"
FT STRAND 3085..3090
FT /evidence="ECO:0007829|PDB:6QSN"
FT STRAND 3095..3102
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3113..3133
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3139..3141
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3147..3166
FT /evidence="ECO:0007829|PDB:6QSN"
FT STRAND 3168..3171
FT /evidence="ECO:0007829|PDB:6QSN"
FT STRAND 3174..3177
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3182..3186
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3189..3193
FT /evidence="ECO:0007829|PDB:6QSN"
FT STRAND 3210..3212
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3213..3215
FT /evidence="ECO:0007829|PDB:6QSN"
FT STRAND 3221..3227
FT /evidence="ECO:0007829|PDB:6QSN"
FT STRAND 3233..3238
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3241..3248
FT /evidence="ECO:0007829|PDB:6QSN"
FT STRAND 3253..3255
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3258..3275
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3280..3292
FT /evidence="ECO:0007829|PDB:6QSN"
FT STRAND 3314..3317
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3319..3327
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3343..3345
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3351..3356
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3364..3384
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3392..3395
FT /evidence="ECO:0007829|PDB:6QSN"
FT HELIX 3397..3399
FT /evidence="ECO:0007829|PDB:6QSN"
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
