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Database: UniProt
Entry: Q9Q6P4
LinkDB: Q9Q6P4
Original site: Q9Q6P4 
ID   POLG_WNV9               Reviewed;        3433 AA.
AC   Q9Q6P4;
DT   27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 2.
DT   13-NOV-2019, entry version 176.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Peptide 2k;
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=Serine protease subunit NS2B;
DE     AltName: Full=Flavivirin protease NS2B regulatory subunit;
DE     AltName: Full=Non-structural protein 2B;
DE   Contains:
DE     RecName: Full=Serine protease NS3;
DE              EC=3.4.21.91;
DE              EC=3.6.1.15 {ECO:0000269|PubMed:19474250};
DE              EC=3.6.4.13 {ECO:0000269|PubMed:19474250};
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=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, ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:20685660};
DE              EC=2.1.1.57 {ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:20685660};
DE              EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE     AltName: Full=NS5;
GN   Name=GP1 {ECO:0000312|EMBL:ANW69091.1};
GN   ORFNames=MZ11_60484gpGP1 {ECO:0000312|EMBL:ANW69091.1},
GN   MZ11_60553gpGP1 {ECO:0000312|EMBL:ANW69112.1};
OS   West Nile virus (strain NY-99) (WNV) (West Nile virus (strain
OS   NY-1999)).
OC   Viruses; Riboviria; Flaviviridae; Flavivirus.
OX   NCBI_TaxID=1968826;
OH   NCBI_TaxID=7158; Aedes.
OH   NCBI_TaxID=34610; Amblyomma variegatum (Tropical bont tick).
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=53527; Culex.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=34627; Hyalomma marginatum.
OH   NCBI_TaxID=308735; Mansonia uniformis.
OH   NCBI_TaxID=308737; Mimomyia.
OH   NCBI_TaxID=34630; Rhipicephalus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
RC   STRAIN=Isolate US/NY99-flamingo382/1999;
RX   PubMed=10600742; DOI=10.1126/science.286.5448.2333;
RA   Lanciotti R.S., Roehrig J.T., Deubel V., Smith J., Parker M.,
RA   Steele K., Crise B., Volpe K.E., Crabtree M.B., Scherret J.H.,
RA   Hall R.A., MacKenzie J.S., Cropp C.B., Panigrahy B., Ostlund E.,
RA   Schmitt B., Malkinson M., Banet C., Weissman J., Komar N.,
RA   Savage H.M., Stone W., McNamara T., Gubler D.J.;
RT   "Origin of the West Nile virus responsible for an outbreak of
RT   encephalitis in the northeastern United States.";
RL   Science 286:2333-2337(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
RC   STRAIN=Isolate US/NY2000-grouse3282/2000;
RX   PubMed=12093177; DOI=10.1006/viro.2002.1449;
RA   Lanciotti R.S., Ebel G.D., Deubel V., Kerst A.J., Murri S., Meyer R.,
RA   Bowen M., McKinney N., Morrill W.E., Crabtree M.B., Kramer L.D.,
RA   Roehrig J.T.;
RT   "Complete genome sequences and phylogenetic analysis of West Nile
RT   virus strains isolated from the United States, Europe, and the Middle
RT   East.";
RL   Virology 298:96-105(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
RC   STRAIN=Isolate US/NY99-6922/1999;
RX   PubMed=15557236; DOI=10.1099/vir.0.80247-0;
RA   Shirato K., Miyoshi H., Goto A., Ako Y., Ueki T., Kariwa H.,
RA   Takashima I.;
RT   "Viral envelope protein glycosylation is a molecular determinant of
RT   the neuroinvasiveness of the New York strain of West Nile virus.";
RL   J. Gen. Virol. 85:3637-3645(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
RC   STRAIN=NV-1/US/BID-V4187/1999, US/BID-V4186/1999, US/BID-V4188/1999,
RC   and US/BID-V4189/1999;
RX   PubMed=21723580; DOI=10.1016/j.virol.2011.06.006;
RA   Armstrong P.M., Vossbrinck C.R., Andreadis T.G., Anderson J.F.,
RA   Pesko K.N., Newman R.M., Lennon N.J., Birren B.W., Ebel G.D.,
RA   Henn M.R.;
RT   "Molecular evolution of West Nile virus in a northern temperate
RT   region: Connecticut, USA 1999-2008.";
RL   Virology 417:203-210(2011).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
RA   Gao Y.W., Fan S.T., Sun H.T., Wang Z., Gao X.L., Li Y.G., Wang T.C.,
RA   Zhang K., Xu W.W., Yu Z.J., Xia X.Z.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
RC   STRAIN=US/NY99-P2/1999;
RA   Grinev A., Anez G., Rios M.;
RT   "Complete genome sequence of West Nile virus strains used for the
RT   formulation of CBER/FDA RNA reference reagents and lot release panels
RT   for nucleic acid testing.";
RL   Genome Announc. 2:E00811-E00814(2014).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
RC   STRAIN=Culex/USA/29000529/2000, and Culex/USA/33020090/2002;
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN   [8]
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   [9]
RP   FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5).
RX   PubMed=15650160; DOI=10.1128/jvi.79.3.1343-1350.2005;
RA   Guo J.T., Hayashi J., Seeger C.;
RT   "West Nile virus inhibits the signal transduction pathway of alpha
RT   interferon.";
RL   J. Virol. 79:1343-1350(2005).
RN   [10]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 1), AND INTERACTION WITH HOST
RP   COMPLEMENT REGULATORY PROTEIN FACTOR H (NON-STRUCTURAL PROTEIN 1).
RX   PubMed=17132743; DOI=10.1073/pnas.0605668103;
RA   Chung K.M., Liszewski M.K., Nybakken G., Davis A.E., Townsend R.R.,
RA   Fremont D.H., Atkinson J.P., Diamond M.S.;
RT   "West Nile virus nonstructural protein NS1 inhibits complement
RT   activation by binding the regulatory protein factor H.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:19111-19116(2006).
RN   [11]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 4A), CATALYTIC ACTIVITY (SERINE
RP   PROTEASE NS3), AND MUTAGENESIS OF 2169-GLU--ASP-2173.
RX   PubMed=19474250; DOI=10.1099/vir.0.012864-0;
RA   Shiryaev S.A., Chernov A.V., Aleshin A.E., Shiryaeva T.N.,
RA   Strongin A.Y.;
RT   "NS4A regulates the ATPase activity of the NS3 helicase: a novel
RT   cofactor role of the non-structural protein NS4A from West Nile
RT   virus.";
RL   J. Gen. Virol. 90:2081-2085(2009).
RN   [12]
RP   FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), CATALYTIC ACTIVITY
RP   (RNA-DIRECTED RNA POLYMERASE NS5), AND MUTAGENESIS OF LYS-2557.
RX   PubMed=19850911; DOI=10.1261/rna.1609709;
RA   Issur M., Geiss B.J., Bougie I., Picard-Jean F., Despins S.,
RA   Mayette J., 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   [13]
RP   FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5).
RX   PubMed=20106931; DOI=10.1128/jvi.01161-09;
RA   Laurent-Rolle M., Boer E.F., Lubick K.J., Wolfinbarger J.B.,
RA   Carmody A.B., Rockx B., Liu W., Ashour J., Shupert W.L.,
RA   Holbrook M.R., Barrett A.D., Mason P.W., Bloom M.E., Garcia-Sastre A.,
RA   Khromykh A.A., Best S.M.;
RT   "The NS5 protein of the virulent West Nile virus NY99 strain is a
RT   potent antagonist of type I interferon-mediated JAK-STAT signaling.";
RL   J. Virol. 84:3503-3515(2010).
RN   [14]
RP   INTERACTION WITH NON-STRUCTURAL PROTEIN 4B (NON-STRUCTURAL PROTEIN 1),
RP   AND INTERACTION WITH NON-STRUCTURAL PROTEIN 1 (NON-STRUCTURAL PROTEIN
RP   4B).
RX   PubMed=22553322; DOI=10.1128/jvi.00157-12;
RA   Youn S., Li T., McCune B.T., Edeling M.A., Fremont D.H., Cristea I.M.,
RA   Diamond M.S.;
RT   "Evidence for a genetic and physical interaction between nonstructural
RT   proteins NS1 and NS4B that modulates replication of West Nile virus.";
RL   J. Virol. 86:7360-7371(2012).
RN   [15]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 1).
RX   PubMed=24245822; DOI=10.1186/1743-422x-10-339;
RA   Youn S., Ambrose R.L., Mackenzie J.M., Diamond M.S.;
RT   "Non-structural protein-1 is required for West Nile virus replication
RT   complex formation and viral RNA synthesis.";
RL   Virol. J. 10:339-339(2013).
RN   [16]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 4B), SUBCELLULAR LOCATION
RP   (NON-STRUCTURAL PROTEIN 4B), SUBCELLULAR LOCATION (NON-STRUCTURAL
RP   PROTEIN 1), SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 4A), AND
RP   FUNCTION (NON-STRUCTURAL PROTEIN 1).
RX   PubMed=24465392; DOI=10.1371/journal.pone.0084040;
RA   Kaufusi P.H., Kelley J.F., Yanagihara R., Nerurkar V.R.;
RT   "Induction of endoplasmic reticulum-derived replication-competent
RT   membrane structures by West Nile virus non-structural protein 4B.";
RL   PLoS ONE 9:E84040-E84040(2014).
RN   [17]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 1), AND MUTAGENESIS OF THR-968;
RP   ASN-982; GLU-1029; ASN-1046; GLY-1086; THR-1108; PRO-1111 AND
RP   MET-1124.
RX   PubMed=24889229; DOI=10.1016/j.virol.2014.03.017;
RA   Morrison C.R., Scholle F.;
RT   "Abrogation of TLR3 inhibition by discrete amino acid changes in the
RT   C-terminal half of the West Nile virus NS1 protein.";
RL   Virology 456:96-107(2014).
RN   [18]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 1), AND SUBCELLULAR LOCATION
RP   (NON-STRUCTURAL PROTEIN 1).
RX   PubMed=24928049; DOI=10.1016/j.virol.2014.04.036;
RA   Crook K.R., Miller-Kittrell M., Morrison C.R., Scholle F.;
RT   "Modulation of innate immune signaling by the secreted form of the
RT   West Nile virus NS1 glycoprotein.";
RL   Virology 458:172-182(2014).
RN   [19]
RP   FUNCTION (NON-STRUCTURAL PROTEIN 4A), SUBCELLULAR LOCATION
RP   (NON-STRUCTURAL PROTEIN 4A), AND INTERACTION WITH HOST RTN3.
RX   PubMed=29117567; DOI=10.1016/j.celrep.2017.10.055;
RA   Aktepe T.E., Liebscher S., Prier J.E., Simmons C.P., Mackenzie J.M.;
RT   "The host protein reticulon 3.1A is utilized by flaviviruses to
RT   facilitate membrane remodelling.";
RL   Cell Rep. 21:1639-1654(2017).
RN   [20]
RP   INTERACTION WITH HUMAN SPCS1.
RX   PubMed=29593046; DOI=10.1128/jvi.00197-18;
RA   Ma L., Li F., Zhang J.W., Li W., Zhao D.M., Wang H., Hua R.H.,
RA   Bu Z.G.;
RT   "Host Factor SPCS1 Regulates the Replication of Japanese Encephalitis
RT   Virus through Interactions with Transmembrane Domains of NS2B.";
RL   J. Virol. 92:0-0(2018).
RN   [21] {ECO:0000244|PDB:2OY0}
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2534-2795 IN COMPLEX WITH
RP   S-ADENOSYL-L-HOMOCYSTEINE, ACTIVE SITE, AND MUTAGENESIS OF LYS-2589;
RP   ASP-2674; LYS-2710 AND GLU-2746.
RX   PubMed=17267492; DOI=10.1128/jvi.02704-06;
RA   Zhou Y., Ray D., Zhao Y., Dong H., Ren S., Li Z., Guo Y.,
RA   Bernard K.A., Shi P.-Y., Li H.;
RT   "Structure and function of flavivirus NS5 methyltransferase.";
RL   J. Virol. 81:3891-3903(2007).
RN   [22] {ECO:0000244|PDB:3I50}
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 291-692, AND DISULFIDE
RP   BONDS.
RX   PubMed=19713934; DOI=10.1038/emboj.2009.245;
RA   Cherrier M.V., Kaufmann B., Nybakken G.E., Lok S.M., Warren J.T.,
RA   Chen B.R., Nelson C.A., Kostyuchenko V.A., Holdaway H.A.,
RA   Chipman P.R., Kuhn R.J., Diamond M.S., Rossmann M.G., Fremont D.H.;
RT   "Structural basis for the preferential recognition of immature
RT   flaviviruses by a fusion-loop antibody.";
RL   EMBO J. 28:3269-3276(2009).
RN   [23] {ECO:0000244|PDB:3LKZ}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2529-2828 IN COMPLEX WITH
RP   SIN INHIBITOR, CATALYTIC ACTIVITY (RNA-DIRECTED RNA POLYMERASE NS5),
RP   FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), AND MUTAGENESIS OF
RP   GLY-2676; ARG-2688; ARG-2691; VAL-2692 AND LEU-2712.
RX   PubMed=20685660; DOI=10.1074/jbc.m110.129197;
RA   Dong H., Liu L., Zou G., Zhao Y., Li Z., Lim S.P., Shi P.Y., Li H.;
RT   "Structural and functional analyses of a conserved hydrophobic pocket
RT   of flavivirus methyltransferase.";
RL   J. Biol. Chem. 285:32586-32595(2010).
RN   [24] {ECO:0000244|PDB:3IYW}
RP   STRUCTURE BY ELECTRON MICROSCOPY (13.70 ANGSTROMS) OF 291-690,
RP   DISULFIDE BONDS, AND SUBUNIT (ENVELOPE PROTEIN E).
RX   PubMed=20956322; DOI=10.1073/pnas.1011036107;
RA   Kaufmann B., Vogt M.R., Goudsmit J., Holdaway H.A., Aksyuk A.A.,
RA   Chipman P.R., Kuhn R.J., Diamond M.S., Rossmann M.G.;
RT   "Neutralization of West Nile virus by cross-linking of its surface
RT   proteins with Fab fragments of the human monoclonal antibody CR4354.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:18950-18955(2010).
RN   [25] {ECO:0000244|PDB:3J0B}
RP   STRUCTURE BY ELECTRON MICROSCOPY (10.30 ANGSTROMS) OF 291-690.
RX   PubMed=23602814; DOI=10.1016/j.jsb.2013.04.005;
RA   Zhang W., Kaufmann B., Chipman P.R., Kuhn R.J., Rossmann M.G.;
RT   "Membrane curvature in flaviviruses.";
RL   J. Struct. Biol. 183:86-94(2013).
RN   [26] {ECO:0000244|PDB:4OIE, ECO:0000244|PDB:4OII}
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 963-1143, DISULFIDE BONDS,
RP   AND SUBUNIT (NON-STRUCTURAL PROTEIN 1).
RX   PubMed=24594604; DOI=10.1073/pnas.1322036111;
RA   Edeling M.A., Diamond M.S., Fremont D.H.;
RT   "Structural basis of flavivirus NS1 assembly and antibody
RT   recognition.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:4285-4290(2014).
RN   [27] {ECO:0000244|PDB:4O6C, ECO:0000244|PDB:4O6D}
RP   X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 791-1143, GLYCOSYLATION AT
RP   ASN-921; ASN-966 AND ASN-998, DISULFIDE BONDS, AND SUBUNIT
RP   (NON-STRUCTURAL PROTEIN 1).
RX   PubMed=24505133; DOI=10.1126/science.1247749;
RA   Akey D.L., Brown W.C., Dutta S., Konwerski J., Jose J., Jurkiw T.J.,
RA   DelProposto J., Ogata C.M., Skiniotis G., Kuhn R.J., Smith J.L.;
RT   "Flavivirus NS1 structures reveal surfaces for associations with
RT   membranes and the immune system.";
RL   Science 343:881-885(2014).
CC   -!- FUNCTION: Capsid protein C: Plays a role in virus budding by
CC       binding to the cell membrane and gathering the viral RNA into a
CC       nucleocapsid that forms the core of a mature virus particle.
CC       During virus entry, may induce genome penetration into the host
CC       cytoplasm after hemifusion induced by the surface proteins. Can
CC       migrate to the cell nucleus where it modulates host functions.
CC       Overcomes the anti-viral effects of host EXOC1 by sequestering and
CC       degrading the latter through the proteasome degradation pathway.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: Capsid protein C: Inhibits RNA silencing by interfering
CC       with host Dicer. {ECO:0000250|UniProtKB:P03314}.
CC   -!- FUNCTION: Peptide pr: Prevents premature fusion activity of
CC       envelope proteins in trans-Golgi by binding to envelope protein E
CC       at pH6.0. After virion release in extracellular space, gets
CC       dissociated from E 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
CC       Golgi compartment prior to virion release. 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: Small envelope protein M: May play a role in virus
CC       budding. Exerts cytotoxic effects by activating a mitochondrial
CC       apoptotic pathway through M ectodomain. May display a viroporin
CC       activity. {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: Envelope protein E: Binds to host cell surface receptor
CC       and mediates fusion between viral and cellular membranes. Envelope
CC       protein is synthesized in the endoplasmic reticulum in the form of
CC       heterodimer with protein prM. They play a role in virion budding
CC       in the ER, and the newly formed immature particle is covered with
CC       60 spikes composed of heterodimer between precursor prM and
CC       envelope protein E. The virion is transported to the Golgi
CC       apparatus where the low pH causes dissociation of PrM-E
CC       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
CC       polyprotein, is targeted to three destinations: the viral
CC       replication cycle, the plasma membrane and the extracellular
CC       compartment. Essential for viral replication. Required for
CC       formation of the replication complex and recruitment of other non-
CC       structural proteins to the ER-derived membrane structures.
CC       Excreted as a hexameric lipoparticle that plays a role against
CC       host immune response. Antagonizing the complement function. Binds
CC       to the host macrophages and dendritic cells. Inhibits signal
CC       transduction originating from Toll-like receptor 3 (TLR3).
CC       {ECO:0000269|PubMed:17132743, ECO:0000269|PubMed:24245822,
CC       ECO:0000269|PubMed:24465392, ECO:0000269|PubMed:24889229,
CC       ECO:0000269|PubMed:24928049}.
CC   -!- FUNCTION: Non-structural protein 2A: Component of the viral RNA
CC       replication complex that functions in virion assembly and
CC       antagonizes the host alpha/beta interferon antiviral response.
CC       {ECO:0000250|UniProtKB:P14335}.
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-
CC       ProRule:PRU00859}.
CC   -!- FUNCTION: Serine protease NS3: Displays three enzymatic
CC       activities: serine protease, NTPase and RNA helicase. NS3 serine
CC       protease, in association with NS2B, performs its autocleavage and
CC       cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM,
CC       NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA
CC       helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.
CC       {ECO:0000255|PROSITE-ProRule:PRU00860,
CC       ECO:0000269|PubMed:19474250}.
CC   -!- FUNCTION: Non-structural protein 4A: Facilitates host membrane
CC       remodelling necessary for viral replication by interacting with
CC       host RTN3. Regulates the ATPase activity of the NS3 helicase
CC       activity. NS4A allows NS3 helicase to conserve energy during
CC       unwinding. {ECO:0000269|PubMed:19474250,
CC       ECO:0000269|PubMed:29117567}.
CC   -!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and
CC       is 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       (PubMed:24465392). Inhibits interferon (IFN)-induced host STAT1
CC       phosphorylation and nuclear translocation, thereby preventing the
CC       establishment of cellular antiviral state by blocking the IFN-
CC       alpha/beta pathway (PubMed:15956546). Inhibits STAT2 translocation
CC       in the nucleus after IFN-alpha treatment (PubMed:15956546).
CC       {ECO:0000269|PubMed:15956546, ECO:0000269|PubMed:24465392}.
CC   -!- FUNCTION: RNA-directed RNA polymerase NS5: Replicates the viral
CC       (+) and (-) genome, and performs the capping of genomes in the
CC       cytoplasm (PubMed:19850911). NS5 methylates viral RNA cap at
CC       guanine N-7 and ribose 2'-O positions (PubMed:19850911,
CC       PubMed:20685660). Besides its role in RNA genome replication, also
CC       prevents the establishment of cellular antiviral state by blocking
CC       the interferon-alpha/beta (IFN-alpha/beta) signaling pathway
CC       (PubMed:20106931). Inhibits host JAK1 and TYK2 phosphorylation,
CC       thereby preventing activation of JAK-STAT signaling pathway
CC       (PubMed:15650160). {ECO:0000269|PubMed:15650160,
CC       ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:20106931,
CC       ECO:0000269|PubMed:20685660}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which
CC         each of the Xaa can be either Arg or Lys and Yaa can be either
CC         Ser or Ala.; EC=3.4.21.91;
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,
CC         ChEBI:CHEBI:83400; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside
CC         5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000269|PubMed:19474250};
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-
CC         homocysteine; Xref=Rhea:RHEA:60856, Rhea:RHEA-COMP:15681,
CC         Rhea:RHEA-COMP:15683, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:143971, ChEBI:CHEBI:143975; EC=2.1.1.56;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00924,
CC         ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:20685660};
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-
CC         homocysteine; Xref=Rhea:RHEA:60852, Rhea:RHEA-COMP:15680,
CC         Rhea:RHEA-COMP:15682, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:143973, ChEBI:CHEBI:143974; EC=2.1.1.56;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00924,
CC         ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:20685660};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-guanosine
CC         in 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-
CC         COMP:15683, Rhea:RHEA-COMP:15685, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143975,
CC         ChEBI:CHEBI:143977; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00924, ECO:0000269|PubMed:19850911,
CC         ECO:0000269|PubMed:20685660};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-adenosine
CC         in 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-
CC         COMP:15682, Rhea:RHEA-COMP:15684, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143974,
CC         ChEBI:CHEBI:143976; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00924, ECO:0000269|PubMed:19850911,
CC         ECO:0000269|PubMed:20685660};
CC   -!- SUBUNIT: Capsid protein C: Homodimer. Interacts (via N-terminus)
CC       with host EXOC1 (via C-terminus); this interaction results in
CC       EXOC1 degradation through the proteasome degradation pathway (By
CC       similarity). Protein prM: Forms heterodimers with envelope protein
CC       E in the endoplasmic reticulum and Golgi (By similarity). Envelope
CC       protein E: Homodimer; in the endoplasmic reticulum and Golgi
CC       (PubMed:20956322). Non-structural protein 1: Homodimer;
CC       Homohexamer when secreted (PubMed:24505133, PubMed:24594604). NS1
CC       interacts with NS4B (PubMed:22553322). Interacts with host
CC       complement protein CFH; this interaction leads to the degradation
CC       of C3 (PubMed:17132743). Non-structural protein 2B: Forms a
CC       heterodimer with serine protease NS3. May form homooligomers (By
CC       similarity). Interacts with human SPCS1 (PubMed:29593046). Serine
CC       protease NS3: Forms a heterodimer with NS2B. Interacts with NS4B.
CC       Interacts with unphosphorylated RNA-directed RNA polymerase NS5;
CC       this interaction stimulates RNA-directed RNA polymerase NS5
CC       guanylyltransferase activity (By similarity). Non-structural
CC       protein 4A: Interacts with host RTN3; this interaction is
CC       important to remodel host cell membranes (PubMed:29117567). Non-
CC       structural protein 4B: Interacts with serine protease NS3 (By
CC       similarity). Interacts with NS1 (PubMed:22553322). RNA-directed
CC       RNA polymerase NS5: Homodimer (By similarity). Interacts with host
CC       STAT2; this interaction inhibits the phosphorylation of the
CC       latter, and, when all viral proteins are present (polyprotein),
CC       targets STAT2 for degradation (By similarity).
CC       {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:17132743,
CC       ECO:0000269|PubMed:20956322, ECO:0000269|PubMed:22553322,
CC       ECO:0000269|PubMed:24505133, ECO:0000269|PubMed:24594604,
CC       ECO:0000269|PubMed:29117567, ECO:0000269|PubMed:29593046}.
CC   -!- SUBCELLULAR LOCATION: Capsid protein C: Virion
CC       {ECO:0000250|UniProtKB:P17763}. Host nucleus
CC       {ECO:0000250|UniProtKB:P17763}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear
CC       region {ECO:0000250|UniProtKB:P06935}.
CC   -!- SUBCELLULAR LOCATION: Peptide pr: Secreted
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane
CC       {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum
CC       membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
CC       protein {ECO:0000255}. Note=ER membrane retention is mediated by
CC       the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
CC   -!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
CC       {ECO:0000305}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum
CC       membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
CC       protein {ECO:0000255}. Note=ER membrane retention is mediated by
CC       the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted
CC       {ECO:0000269|PubMed:24928049}. Host endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:24465392}; Peripheral membrane protein;
CC       Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-
CC       derived vesicles hosting the replication complex.
CC       {ECO:0000269|PubMed:24465392}.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass
CC       membrane protein {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host
CC       endoplasmic reticulum membrane; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic
CC       reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860};
CC       Peripheral membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}. Note=Remains non-covalently associated to
CC       serine protease subunit NS2B. {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic
CC       reticulum membrane {ECO:0000269|PubMed:24465392}; Multi-pass
CC       membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in
CC       RE-derived vesicles hosting the replication complex.
CC       {ECO:0000269|PubMed:24465392, ECO:0000269|PubMed:29117567}.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic
CC       reticulum membrane {ECO:0000269|PubMed:24465392}; Multi-pass
CC       membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in
CC       RE-derived vesicles hosting the replication complex.
CC       {ECO:0000269|PubMed:24465392}.
CC   -!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase NS5: Host
CC       endoplasmic reticulum membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}.
CC       Note=Located in RE-associated vesicles hosting the replication
CC       complex. NS5 protein is mainly localized in the nucleus rather
CC       than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
CC   -!- DOMAIN: The transmembrane domains of the small envelope protein M
CC       and envelope protein E contain an endoplasmic reticulum retention
CC       signal. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: Genome polyprotein: Specific enzymatic cleavages in vivo
CC       yield mature proteins. Cleavages in the lumen of endoplasmic
CC       reticulum are performed by host signal peptidase, whereas
CC       cleavages in the cytoplasmic side are performed by serine protease
CC       NS3. Signal cleavage at the 2K-4B site requires a prior NS3
CC       protease-mediated cleavage at the 4A-2K site.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: Protein prM: Cleaved in post-Golgi vesicles by a host furin,
CC       releasing the mature small envelope protein M, and peptide pr.
CC       This cleavage is incomplete as up to 30% of viral particles still
CC       carry 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 (PubMed:24505133).
CC       The excreted form is glycosylated and this is required for
CC       efficient secretion of the protein from infected cells (By
CC       similarity). {ECO:0000250|UniProtKB:P17763,
CC       ECO:0000269|PubMed:24505133}.
CC   -!- PTM: RNA-directed RNA polymerase NS5: Phosphorylated on serines
CC       residues. This phosphorylation may trigger NS5 nuclear
CC       localization. {ECO:0000250|UniProtKB:P17763}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the class I-like
CC       SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type
CC       methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}.
DR   EMBL; AF196835; AAF20092.2; -; Genomic_RNA.
DR   EMBL; AF404755; AAM81751.1; -; Genomic_RNA.
DR   EMBL; HM488125; ADL27936.1; -; Genomic_RNA.
DR   EMBL; HM488126; ADL27937.1; -; Genomic_RNA.
DR   EMBL; HM488127; ADL27938.1; -; Genomic_RNA.
DR   EMBL; HM488128; ADL27939.1; -; Genomic_RNA.
DR   EMBL; KC407666; AGI15883.1; -; Genomic_RNA.
DR   EMBL; KM083619; AIO10814.1; -; Genomic_RNA.
DR   EMBL; KX547386; ANW69091.1; -; Genomic_RNA.
DR   EMBL; KX547393; ANW69112.1; -; Genomic_RNA.
DR   EMBL; AB185914; BAD34488.1; -; Genomic_RNA.
DR   PDB; 2OY0; X-ray; 2.80 A; A/B=2534-2795.
DR   PDB; 3I50; X-ray; 3.00 A; E=291-692.
DR   PDB; 3IYW; EM; 13.70 A; A/B/C=291-690.
DR   PDB; 3J0B; EM; 10.30 A; A/B/C=291-690.
DR   PDB; 3LKZ; X-ray; 2.00 A; A/B=2529-2828.
DR   PDB; 4O6C; X-ray; 2.75 A; A/B/C/D/E/F=791-1143.
DR   PDB; 4O6D; X-ray; 2.59 A; A/B=791-1143.
DR   PDB; 4OIE; X-ray; 1.85 A; A=963-1143.
DR   PDB; 4OII; X-ray; 3.00 A; A/B=963-1143.
DR   PDBsum; 2OY0; -.
DR   PDBsum; 3I50; -.
DR   PDBsum; 3IYW; -.
DR   PDBsum; 3J0B; -.
DR   PDBsum; 3LKZ; -.
DR   PDBsum; 4O6C; -.
DR   PDBsum; 4O6D; -.
DR   PDBsum; 4OIE; -.
DR   PDBsum; 4OII; -.
DR   SMR; Q9Q6P4; -.
DR   iPTMnet; Q9Q6P4; -.
DR   ABCD; Q9Q6P4; -.
DR   EvolutionaryTrace; Q9Q6P4; -.
DR   Proteomes; UP000096925; Genome.
DR   Proteomes; UP000107647; Genome.
DR   Proteomes; UP000123900; Genome.
DR   Proteomes; UP000138291; Genome.
DR   Proteomes; UP000139973; Genome.
DR   Proteomes; UP000146770; Genome.
DR   Proteomes; UP000163596; Genome.
DR   Proteomes; UP000169485; 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; IEA:InterPro.
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: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: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:0039690; P:positive stranded viral RNA replication; IDA:UniProtKB.
DR   GO; GO:0039573; P:suppression by virus of host complement activation; IDA:UniProtKB.
DR   GO; GO:0039503; P:suppression by virus of host innate immune response; IDA:UniProtKB.
DR   GO; GO:0039563; P:suppression by virus of host STAT1 activity; 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:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   CDD; cd12149; Flavi_E_C; 1.
DR   DisProt; DP02203; -.
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   InterPro; IPR011492; DEAD_Flavivir.
DR   InterPro; IPR000069; Env_glycoprot_M_flavivir.
DR   InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
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; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR000208; RNA-dir_pol_flavivirus.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF01003; Flavi_capsid; 1.
DR   Pfam; PF07652; Flavi_DEAD; 1.
DR   Pfam; PF02832; Flavi_glycop_C; 1.
DR   Pfam; PF00869; Flavi_glycoprot; 1.
DR   Pfam; PF01004; Flavi_M; 1.
DR   Pfam; PF00948; Flavi_NS1; 1.
DR   Pfam; PF01005; Flavi_NS2A; 1.
DR   Pfam; PF01002; Flavi_NS2B; 1.
DR   Pfam; PF01350; Flavi_NS4A; 1.
DR   Pfam; PF01349; Flavi_NS4B; 1.
DR   Pfam; PF00972; Flavi_NS5; 1.
DR   Pfam; PF01570; Flavi_propep; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF00949; Peptidase_S7; 1.
DR   PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF101257; SSF101257; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF56983; SSF56983; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   TIGRFAMs; TIGR04240; flavi_E_stem; 1.
DR   PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
DR   PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activation of host autophagy by virus; ATP-binding;
KW   Capsid protein; Complete proteome; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
KW   Host cytoplasm; Host endoplasmic reticulum; Host membrane;
KW   Host 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 STAT1 by virus; Inhibition of host STAT2 by virus;
KW   Membrane; Metal-binding; Methyltransferase; mRNA capping;
KW   mRNA processing; Nucleotide-binding; Nucleotidyltransferase;
KW   Phosphoprotein; Protease; RNA-binding; RNA-directed RNA polymerase;
KW   S-adenosyl-L-methionine; Secreted; Serine protease;
KW   Suppressor of RNA silencing; Transferase; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell;
KW   Viral immunoevasion; Viral penetration into host cytoplasm;
KW   Viral RNA replication; Virion; Virus entry into host cell; Zinc.
FT   CHAIN         1   3433       Genome polyprotein.
FT                                /FTId=PRO_0000441576.
FT   CHAIN         1    105       Capsid protein C.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441577.
FT   PROPEP      106    123       ER anchor for the capsid protein C,
FT                                removed in mature form by serine protease
FT                                NS3. {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441578.
FT   CHAIN       124    290       Protein prM.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441579.
FT   CHAIN       124    215       Peptide pr.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441580.
FT   CHAIN       216    290       Small envelope protein M.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441581.
FT   CHAIN       291    791       Envelope protein E.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441582.
FT   CHAIN       792   1143       Non-structural protein 1.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441583.
FT   CHAIN      1144   1374       Non-structural protein 2A.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441584.
FT   CHAIN      1375   1505       Serine protease subunit NS2B.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441585.
FT   CHAIN      1506   2124       Serine protease NS3.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441586.
FT   CHAIN      2125   2250       Non-structural protein 4A.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441587.
FT   PEPTIDE    2251   2273       Peptide 2k.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441588.
FT   CHAIN      2274   2528       Non-structural protein 4B.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441589.
FT   CHAIN      2529   3433       RNA-directed RNA polymerase NS5.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441590.
FT   TOPO_DOM      2    108       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    109    129       Helical. {ECO:0000255}.
FT   TOPO_DOM    130    248       Extracellular. {ECO:0000255}.
FT   TRANSMEM    249    269       Helical. {ECO:0000255}.
FT   TOPO_DOM    270    275       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    276    290       Helical. {ECO:0000305}.
FT   TOPO_DOM    291    743       Extracellular. {ECO:0000255}.
FT   TRANSMEM    744    764       Helical. {ECO:0000255}.
FT   TOPO_DOM    765    770       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    771    791       Helical. {ECO:0000255}.
FT   TOPO_DOM    792   1216       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1217   1237       Helical. {ECO:0000255}.
FT   TOPO_DOM   1238   1245       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1246   1268       Helical. {ECO:0000255}.
FT   TOPO_DOM   1269   1288       Lumenal. {ECO:0000255}.
FT   TRANSMEM   1289   1309       Helical. {ECO:0000255}.
FT   TOPO_DOM   1310   1313       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1314   1331       Helical. {ECO:0000255}.
FT   TOPO_DOM   1332   1345       Lumenal. {ECO:0000255}.
FT   TRANSMEM   1346   1366       Helical. {ECO:0000255}.
FT   TOPO_DOM   1367   1375       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1376   1396       Helical. {ECO:0000255}.
FT   TOPO_DOM   1397   1399       Lumenal. {ECO:0000255}.
FT   TRANSMEM   1400   1420       Helical. {ECO:0000255}.
FT   TOPO_DOM   1421   1477       Cytoplasmic. {ECO:0000255}.
FT   INTRAMEM   1478   1498       Helical. {ECO:0000255}.
FT   TOPO_DOM   1499   2174       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2175   2195       Helical. {ECO:0000255}.
FT   TOPO_DOM   2196   2200       Lumenal. {ECO:0000255}.
FT   INTRAMEM   2201   2221       Helical. {ECO:0000255}.
FT   TOPO_DOM   2222   2222       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2223   2243       Helical. {ECO:0000255}.
FT   TOPO_DOM   2244   2258       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2259   2279       Helical; Note=Signal for NS4B.
FT                                {ECO:0000255}.
FT   TOPO_DOM   2280   2312       Lumenal. {ECO:0000255}.
FT   INTRAMEM   2313   2333       Helical. {ECO:0000255}.
FT   TOPO_DOM   2334   2380       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2381   2401       Helical. {ECO:0000255}.
FT   TOPO_DOM   2402   2444       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2445   2465       Helical. {ECO:0000255}.
FT   TOPO_DOM   2466   2470       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2471   2491       Helical. {ECO:0000255}.
FT   TOPO_DOM   2492   3433       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN     1506   1683       Peptidase S7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   DOMAIN     1686   1842       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1853   2018       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     2529   2794       mRNA cap 0-1 NS5-type MT.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   DOMAIN     3058   3210       RdRp catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00539}.
FT   NP_BIND    1699   1706       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION        2     15       Interaction with host EXOC1.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   REGION       37     72       Hydrophobic; homodimerization of capsid
FT                                protein C.
FT                                {ECO:0000250|UniProtKB:P29990}.
FT   REGION      388    401       Fusion peptide.
FT                                {ECO:0000250|UniProtKB:P14336}.
FT   REGION     1428   1467       Interacts with and activates NS3
FT                                protease. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00859}.
FT   REGION     1690   1693       Important for RNA-binding.
FT                                {ECO:0000250|UniProtKB:P14340}.
FT   REGION     2169   2173       Regulates the ATPase activity of NS3
FT                                helicase. {ECO:0000269|PubMed:19474250}.
FT   REGION     2614   2615       S-adenosyl-L-methionine binding.
FT                                {ECO:0000244|PDB:2OY0}.
FT   REGION     2659   2660       S-adenosyl-L-methionine binding.
FT                                {ECO:0000244|PDB:2OY0}.
FT   MOTIF      1790   1793       DEAH box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COMPBIAS    281    284       Poly-Leu. {ECO:0000255}.
FT   ACT_SITE   1556   1556       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   ACT_SITE   1580   1580       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   ACT_SITE   1640   1640       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   ACT_SITE   2589   2589       For 2'-O-MTase activity.
FT                                {ECO:0000269|PubMed:17267492}.
FT   ACT_SITE   2674   2674       For 2'-O-MTase activity.
FT                                {ECO:0000269|PubMed:17267492}.
FT   ACT_SITE   2710   2710       For 2'-O-MTase activity.
FT                                {ECO:0000269|PubMed:17267492}.
FT   ACT_SITE   2746   2746       For 2'-O-MTase activity.
FT                                {ECO:0000269|PubMed:17267492}.
FT   METAL      2968   2968       Zinc 1. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      2972   2972       Zinc 1; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   METAL      2977   2977       Zinc 1. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      2980   2980       Zinc 1. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      3245   3245       Zinc 2; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   METAL      3261   3261       Zinc 2. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      3380   3380       Zinc 2. {ECO:0000250|UniProtKB:P14335}.
FT   BINDING    2584   2584       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924,
FT                                ECO:0000269|PubMed:17267492}.
FT   BINDING    2614   2614       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2615   2615       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2632   2632       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2633   2633       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2639   2639       S-adenosyl-L-methionine.
FT                                {ECO:0000269|PubMed:17267492}.
FT   BINDING    2659   2659       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2660   2660       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2674   2674       S-adenosyl-L-methionine.
FT                                {ECO:0000269|PubMed:17267492}.
FT   BINDING    2675   2675       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2748   2748       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE        105    106       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE        123    124       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE        215    216       Cleavage; by host furin.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE        290    291       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE        791    792       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       1143   1144       Cleavage; by host.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       1374   1375       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       1505   1506       Cleavage; by autolysis.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       1963   1963       Involved in NS3 ATPase and RTPase
FT                                activities.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   SITE       1966   1966       Involved in NS3 ATPase and RTPase
FT                                activities.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   SITE       2124   2125       Cleavage; by autolysis.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       2250   2251       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       2273   2274       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       2528   2529       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       2541   2541       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2544   2544       mRNA cap binding; via carbonyl oxygen.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE       2545   2545       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2547   2547       mRNA cap binding; via carbonyl oxygen.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE       2552   2552       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924,
FT                                ECO:0000269|PubMed:17267492}.
FT   SITE       2556   2556       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2589   2589       Essential for 2'-O-methyltransferase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2674   2674       Essential for 2'-O-methyltransferase and
FT                                N-7 methyltransferase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE       2678   2678       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2710   2710       Essential for 2'-O-methyltransferase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2741   2741       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2743   2743       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2746   2746       Essential for 2'-O-methyltransferase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   MOD_RES    2584   2584       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   CARBOHYD    138    138       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   CARBOHYD    921    921       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000269|PubMed:24505133}.
FT   CARBOHYD    966    966       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000269|PubMed:24505133}.
FT   CARBOHYD    998    998       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000269|PubMed:24505133}.
FT   DISULFID    293    320       {ECO:0000269|PubMed:20956322}.
FT   DISULFID    350    411       {ECO:0000269|PubMed:19713934,
FT                                ECO:0000269|PubMed:20956322}.
FT   DISULFID    350    406       {ECO:0000250|UniProtKB:P06935}.
FT   DISULFID    364    395       {ECO:0000269|PubMed:19713934,
FT                                ECO:0000269|PubMed:20956322}.
FT   DISULFID    382    411       {ECO:0000250|UniProtKB:P06935}.
FT   DISULFID    382    406       {ECO:0000269|PubMed:19713934,
FT                                ECO:0000269|PubMed:20956322}.
FT   DISULFID    480    578       {ECO:0000269|PubMed:19713934,
FT                                ECO:0000269|PubMed:20956322}.
FT   DISULFID    595    626       {ECO:0000269|PubMed:20956322}.
FT   DISULFID    795    806       {ECO:0000269|PubMed:24505133}.
FT   DISULFID    846    934       {ECO:0000269|PubMed:24505133}.
FT   DISULFID    970   1014       {ECO:0000269|PubMed:24505133,
FT                                ECO:0000269|PubMed:24594604}.
FT   DISULFID   1071   1120       {ECO:0000269|PubMed:24505133,
FT                                ECO:0000269|PubMed:24594604}.
FT   DISULFID   1082   1103       {ECO:0000269|PubMed:24505133,
FT                                ECO:0000269|PubMed:24594604}.
FT   DISULFID   1104   1107       {ECO:0000269|PubMed:24505133,
FT                                ECO:0000269|PubMed:24594604}.
FT   MUTAGEN     968    968       T->N: No effect on TL3 signaling
FT                                inhibition by NS1.
FT                                {ECO:0000269|PubMed:24889229}.
FT   MUTAGEN     982    982       N->I: No effect on TL3 signaling
FT                                inhibition by NS1.
FT                                {ECO:0000269|PubMed:24889229}.
FT   MUTAGEN    1029   1029       E->V: No effect on TL3 signaling
FT                                inhibition by NS1.
FT                                {ECO:0000269|PubMed:24889229}.
FT   MUTAGEN    1046   1046       N->D: Complete loss of TL3 signaling
FT                                inhibition by NS1.
FT                                {ECO:0000269|PubMed:24889229}.
FT   MUTAGEN    1086   1086       G->R: Almost no effect on TL3 signaling
FT                                inhibition by NS1.
FT                                {ECO:0000269|PubMed:24889229}.
FT   MUTAGEN    1108   1108       T->I: Complete loss of TL3 signaling
FT                                inhibition by NS1.
FT                                {ECO:0000269|PubMed:24889229}.
FT   MUTAGEN    1111   1111       P->S: About 50% loss of TL3 signaling
FT                                inhibition by NS1.
FT                                {ECO:0000269|PubMed:24889229}.
FT   MUTAGEN    1124   1124       M->V: About 50% loss of TL3 signaling
FT                                inhibition by NS1.
FT                                {ECO:0000269|PubMed:24889229}.
FT   MUTAGEN    2169   2173       EELPD->KKLPK: Complete loss of regulation
FT                                of the ATPase activity of NS3 helicase by
FT                                NS4A. {ECO:0000269|PubMed:19474250}.
FT   MUTAGEN    2557   2557       K->A: 85% loss of NS5-GMP formation.
FT                                {ECO:0000269|PubMed:19850911}.
FT   MUTAGEN    2589   2589       K->A,E,R: Complete loss of 2'-O-
FT                                methyltransferase activity.
FT                                {ECO:0000269|PubMed:17267492}.
FT   MUTAGEN    2674   2674       D->A,N,K: Complete loss of 2'-O-
FT                                methyltransferase activity.
FT                                {ECO:0000269|PubMed:17267492}.
FT   MUTAGEN    2676   2676       G->A: 86% loss of N7 guanine
FT                                methyltransferase activity; 60% loss of
FT                                2'-O-methyltransferase activity.
FT                                {ECO:0000269|PubMed:20685660}.
FT   MUTAGEN    2688   2688       R->A: 78% loss of N7 guanine
FT                                methyltransferase activity; no effect 2'-
FT                                O-methyltransferase activity.
FT                                {ECO:0000269|PubMed:20685660}.
FT   MUTAGEN    2691   2691       R->A: 50% loss of N7 guanine
FT                                methyltransferase activity; no effect 2'-
FT                                O-methyltransferase activity.
FT                                {ECO:0000269|PubMed:20685660}.
FT   MUTAGEN    2692   2692       V->A: 10% loss of N7 guanine
FT                                methyltransferase activity; 50% loss of
FT                                2'-O-methyltransferase activity.
FT                                {ECO:0000269|PubMed:20685660}.
FT   MUTAGEN    2710   2710       K->A,E,N: Complete loss of 2'-O-
FT                                methyltransferase activity.
FT                                {ECO:0000269|PubMed:17267492}.
FT   MUTAGEN    2712   2712       L->A: 20% loss of N7 guanine
FT                                methyltransferase activity7; 74% loss of
FT                                2'-O-methyltransferase activity.
FT                                {ECO:0000269|PubMed:20685660}.
FT   MUTAGEN    2746   2746       E->A,D,K: Complete loss of 2'-O-
FT                                methyltransferase activity.
FT                                {ECO:0000269|PubMed:17267492}.
FT   STRAND      299    303       {ECO:0000244|PDB:3I50}.
FT   STRAND      312    314       {ECO:0000244|PDB:3I50}.
FT   STRAND      320    324       {ECO:0000244|PDB:3I50}.
FT   STRAND      326    328       {ECO:0000244|PDB:3I50}.
FT   STRAND      331    342       {ECO:0000244|PDB:3I50}.
FT   STRAND      344    363       {ECO:0000244|PDB:3I50}.
FT   STRAND      365    367       {ECO:0000244|PDB:3I50}.
FT   HELIX       373    376       {ECO:0000244|PDB:3I50}.
FT   STRAND      380    389       {ECO:0000244|PDB:3I50}.
FT   HELIX       391    393       {ECO:0000244|PDB:3I50}.
FT   STRAND      399    412       {ECO:0000244|PDB:3I50}.
FT   STRAND      414    419       {ECO:0000244|PDB:3I50}.
FT   HELIX       422    424       {ECO:0000244|PDB:3I50}.
FT   STRAND      425    431       {ECO:0000244|PDB:3I50}.
FT   STRAND      461    463       {ECO:0000244|PDB:3I50}.
FT   HELIX       471    473       {ECO:0000244|PDB:3I50}.
FT   STRAND      474    479       {ECO:0000244|PDB:3I50}.
FT   STRAND      484    486       {ECO:0000244|PDB:3I50}.
FT   STRAND      490    495       {ECO:0000244|PDB:3I50}.
FT   STRAND      500    504       {ECO:0000244|PDB:3I50}.
FT   HELIX       505    508       {ECO:0000244|PDB:3I50}.
FT   HELIX       527    529       {ECO:0000244|PDB:3I50}.
FT   STRAND      530    532       {ECO:0000244|PDB:3I50}.
FT   STRAND      542    544       {ECO:0000244|PDB:3I50}.
FT   HELIX       549    553       {ECO:0000244|PDB:3I50}.
FT   STRAND      557    559       {ECO:0000244|PDB:3I50}.
FT   STRAND      567    570       {ECO:0000244|PDB:3I50}.
FT   STRAND      577    581       {ECO:0000244|PDB:3I50}.
FT   HELIX       582    584       {ECO:0000244|PDB:3I50}.
FT   STRAND      792    798       {ECO:0000244|PDB:4O6D}.
FT   HELIX       799    801       {ECO:0000244|PDB:4O6D}.
FT   STRAND      803    813       {ECO:0000244|PDB:4O6D}.
FT   TURN        816    818       {ECO:0000244|PDB:4O6D}.
FT   HELIX       819    822       {ECO:0000244|PDB:4O6D}.
FT   STRAND      823    828       {ECO:0000244|PDB:4O6D}.
FT   HELIX       830    841       {ECO:0000244|PDB:4O6D}.
FT   TURN        842    844       {ECO:0000244|PDB:4O6D}.
FT   HELIX       853    872       {ECO:0000244|PDB:4O6D}.
FT   STRAND      878    881       {ECO:0000244|PDB:4O6D}.
FT   STRAND      922    927       {ECO:0000244|PDB:4O6D}.
FT   STRAND      932    934       {ECO:0000244|PDB:4O6D}.
FT   HELIX       936    938       {ECO:0000244|PDB:4O6D}.
FT   STRAND      944    950       {ECO:0000244|PDB:4O6D}.
FT   STRAND      956    962       {ECO:0000244|PDB:4O6D}.
FT   HELIX       972    974       {ECO:0000244|PDB:4O6D}.
FT   STRAND      975    980       {ECO:0000244|PDB:4OIE}.
FT   STRAND      983   1010       {ECO:0000244|PDB:4OIE}.
FT   HELIX      1018   1020       {ECO:0000244|PDB:4OIE}.
FT   HELIX      1029   1031       {ECO:0000244|PDB:4OIE}.
FT   HELIX      1036   1038       {ECO:0000244|PDB:4OIE}.
FT   STRAND     1061   1069       {ECO:0000244|PDB:4OIE}.
FT   STRAND     1075   1078       {ECO:0000244|PDB:4OIE}.
FT   STRAND     1080   1082       {ECO:0000244|PDB:4O6C}.
FT   STRAND     1089   1092       {ECO:0000244|PDB:4OIE}.
FT   STRAND     1094   1096       {ECO:0000244|PDB:4O6D}.
FT   STRAND     1101   1106       {ECO:0000244|PDB:4OIE}.
FT   STRAND     1112   1116       {ECO:0000244|PDB:4OIE}.
FT   STRAND     1119   1122       {ECO:0000244|PDB:4OIE}.
FT   STRAND     1126   1129       {ECO:0000244|PDB:4OIE}.
FT   HELIX      2536   2544       {ECO:0000244|PDB:3LKZ}.
FT   HELIX      2549   2555       {ECO:0000244|PDB:3LKZ}.
FT   TURN       2556   2559       {ECO:0000244|PDB:3LKZ}.
FT   STRAND     2561   2563       {ECO:0000244|PDB:3LKZ}.
FT   HELIX      2566   2574       {ECO:0000244|PDB:3LKZ}.
FT   STRAND     2583   2585       {ECO:0000244|PDB:2OY0}.
FT   HELIX      2586   2595       {ECO:0000244|PDB:3LKZ}.
FT   STRAND     2603   2608       {ECO:0000244|PDB:3LKZ}.
FT   HELIX      2614   2619       {ECO:0000244|PDB:3LKZ}.
FT   STRAND     2625   2631       {ECO:0000244|PDB:3LKZ}.
FT   HELIX      2649   2651       {ECO:0000244|PDB:3LKZ}.
FT   STRAND     2652   2655       {ECO:0000244|PDB:3LKZ}.
FT   TURN       2660   2662       {ECO:0000244|PDB:2OY0}.
FT   STRAND     2669   2673       {ECO:0000244|PDB:3LKZ}.
FT   HELIX      2682   2700       {ECO:0000244|PDB:3LKZ}.
FT   STRAND     2706   2712       {ECO:0000244|PDB:3LKZ}.
FT   HELIX      2717   2730       {ECO:0000244|PDB:3LKZ}.
FT   STRAND     2733   2735       {ECO:0000244|PDB:3LKZ}.
FT   STRAND     2747   2750       {ECO:0000244|PDB:3LKZ}.
FT   HELIX      2757   2770       {ECO:0000244|PDB:3LKZ}.
FT   STRAND     2781   2783       {ECO:0000244|PDB:3LKZ}.
SQ   SEQUENCE   3433 AA;  381176 MW;  A742A68D0E55947E CRC64;
     MSKKPGGPGK SRAVNMLKRG MPRVLSLIGL KRAMLSLIDG KGPIRFVLAL LAFFRFTAIA
     PTRAVLDRWR GVNKQTAMKH LLSFKKELGT LTSAINRRSS KQKKRGGKTG IAVMIGLIAS
     VGAVTLSNFQ GKVMMTVNAT DVTDVITIPT AAGKNLCIVR AMDVGYMCDD TITYECPVLS
     AGNDPEDIDC WCTKSAVYVR YGRCTKTRHS RRSRRSLTVQ THGESTLANK KGAWMDSTKA
     TRYLVKTESW ILRNPGYALV AAVIGWMLGS NTMQRVVFVV LLLLVAPAYS FNCLGMSNRD
     FLEGVSGATW VDLVLEGDSC VTIMSKDKPT IDVKMMNMEA ANLAEVRSYC YLATVSDLST
     KAACPTMGEA HNDKRADPAF VCRQGVVDRG WGNGCGLFGK GSIDTCAKFA CSTKAIGRTI
     LKENIKYEVA IFVHGPTTVE SHGNYSTQVG ATQAGRFSIT PAAPSYTLKL GEYGEVTVDC
     EPRSGIDTNA YYVMTVGTKT FLVHREWFMD LNLPWSSAGS TVWRNRETLM EFEEPHATKQ
     SVIALGSQEG ALHQALAGAI PVEFSSNTVK LTSGHLKCRV KMEKLQLKGT TYGVCSKAFK
     FLGTPADTGH GTVVLELQYT GTDGPCKVPI SSVASLNDLT PVGRLVTVNP FVSVATANAK
     VLIELEPPFG DSYIVVGRGE QQINHHWHKS GSSIGKAFTT TLKGAQRLAA LGDTAWDFGS
     VGGVFTSVGK AVHQVFGGAF RSLFGGMSWI TQGLLGALLL WMGINARDRS IALTFLAVGG
     VLLFLSVNVH ADTGCAIDIS RQELRCGSGV FIHNDVEAWM DRYKYYPETP QGLAKIIQKA
     HKEGVCGLRS VSRLEHQMWE AVKDELNTLL KENGVDLSVV VEKQEGMYKS APKRLTATTE
     KLEIGWKAWG KSILFAPELA NNTFVVDGPE TKECPTQNRA WNSLEVEDFG FGLTSTRMFL
     KVRESNTTEC DSKIIGTAVK NNLAIHSDLS YWIESRLNDT WKLERAVLGE VKSCTWPETH
     TLWGDGILES DLIIPVTLAG PRSNHNRRPG YKTQNQGPWD EGRVEIDFDY CPGTTVTLSE
     SCGHRGPATR TTTESGKLIT DWCCRSCTLP PLRYQTDSGC WYGMEIRPQR HDEKTLVQSQ
     VNAYNADMID PFQLGLLVVF LATQEVLRKR WTAKISMPAI LIALLVLVFG GITYTDVLRY
     VILVGAAFAE SNSGGDVVHL ALMATFKIQP VFMVASFLKA RWTNQENILL MLAAVFFQMA
     YHDARQILLW EIPDVLNSLA VAWMILRAIT FTTTSNVVVP LLALLTPGLR CLNLDVYRIL
     LLMVGIGSLI REKRSAAAKK KGASLLCLAL ASTGLFNPMI LAAGLIACDP NRKRGWPATE
     VMTAVGLMFA IVGGLAELDI DSMAIPMTIA GLMFAAFVIS GKSTDMWIER TADISWESDA
     EITGSSERVD VRLDDDGNFQ LMNDPGAPWK IWMLRMVCLA ISAYTPWAIL PSVVGFWITL
     QYTKRGGVLW DTPSPKEYKK GDTTTGVYRI MTRGLLGSYQ AGAGVMVEGV FHTLWHTTKG
     AALMSGEGRL DPYWGSVKED RLCYGGPWKL QHKWNGQDEV QMIVVEPGKN VKNVQTKPGV
     FKTPEGEIGA VTLDFPTGTS GSPIVDKNGD VIGLYGNGVI MPNGSYISAI VQGERMDEPI
     PAGFEPEMLR KKQITVLDLH PGAGKTRRIL PQIIKEAINR RLRTAVLAPT RVVAAEMAEA
     LRGLPIRYQT SAVPREHNGN EIVDVMCHAT LTHRLMSPHR VPNYNLFVMD EAHFTDPASI
     AARGYISTKV ELGEAAAIFM TATPPGTSDP FPESNSPISD LQTEIPDRAW NSGYEWITEY
     TGKTVWFVPS VKMGNEIALC LQRAGKKVVQ LNRKSYETEY PKCKNDDWDF VITTDISEMG
     ANFKASRVID SRKSVKPTII TEGEGRVILG EPSAVTAASA AQRRGRIGRN PSQVGDEYCY
     GGHTNEDDSN FAHWTEARIM LDNINMPNGL IAQFYQPERE KVYTMDGEYR LRGEERKNFL
     ELLRTADLPV WLAYKVAAAG VSYHDRRWCF DGPRTNTILE DNNEVEVITK LGERKILRPR
     WIDARVYSDH QALKAFKDFA SGKRSQIGLI EVLGKMPEHF MGKTWEALDT MYVVATAEKG
     GRAHRMALEE LPDALQTIAL IALLSVMTMG VFFLLMQRKG IGKIGLGGAV LGVATFFCWM
     AEVPGTKIAG MLLLSLLLMI VLIPEPEKQR SQTDNQLAVF LICVMTLVSA VAANEMGWLD
     KTKSDISSLF GQRIEVKENF SMGEFLLDLR PATAWSLYAV TTAVLTPLLK HLITSDYINT
     SLTSINVQAS ALFTLARGFP FVDVGVSALL LAAGCWGQVT LTVTVTAATL LFCHYAYMVP
     GWQAEAMRSA QRRTAAGIMK NAVVDGIVAT DVPELERTTP IMQKKVGQIM LILVSLAAVV
     VNPSVKTVRE AGILITAAAV TLWENGASSV WNATTAIGLC HIMRGGWLSC LSITWTLIKN
     MEKPGLKRGG AKGRTLGEVW KERLNQMTKE EFTRYRKEAI IEVDRSAAKH ARKEGNVTGG
     HPVSRGTAKL RWLVERRFLE PVGKVIDLGC GRGGWCYYMA TQKRVQEVRG YTKGGPGHEE
     PQLVQSYGWN IVTMKSGVDV FYRPSECCDT LLCDIGESSS SAEVEEHRTI RVLEMVEDWL
     HRGPREFCVK VLCPYMPKVI EKMELLQRRY GGGLVRNPLS RNSTHEMYWV SRASGNVVHS
     VNMTSQVLLG RMEKRTWKGP QYEEDVNLGS GTRAVGKPLL NSDTSKIKNR IERLRREYSS
     TWHHDENHPY RTWNYHGSYD VKPTGSASSL VNGVVRLLSK PWDTITNVTT MAMTDTTPFG
     QQRVFKEKVD TKAPEPPEGV KYVLNETTNW LWAFLAREKR PRMCSREEFI RKVNSNAALG
     AMFEEQNQWR SAREAVEDPK FWEMVDEERE AHLRGECHTC IYNMMGKREK KPGEFGKAKG
     SRAIWFMWLG ARFLEFEALG FLNEDHWLGR KNSGGGVEGL GLQKLGYILR EVGTRPGGKI
     YADDTAGWDT RITRADLENE AKVLELLDGE HRRLARAIIE LTYRHKVVKV MRPAADGRTV
     MDVISREDQR GSGQVVTYAL NTFTNLAVQL VRMMEGEGVI GPDDVEKLTK GKGPKVRTWL
     FENGEERLSR MAVSGDDCVV KPLDDRFATS LHFLNAMSKV RKDIQEWKPS TGWYDWQQVP
     FCSNHFTELI MKDGRTLVVP CRGQDELVGR ARISPGAGWN VRDTACLAKS YAQMWLLLYF
     HRRDLRLMAN AICSAVPVNW VPTGRTTWSI HAGGEWMTTE DMLEVWNRVW IEENEWMEDK
     TPVEKWSDVP YSGKREDIWC GSLIGTRARA TWAENIQVAI NQVRAIIGDE KYVDYMSSLK
     RYEDTTLVED TVL
//
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