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 POLG_WNV9               Reviewed;        3433 AA.
Q9Q6P4;
27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 2.
22-NOV-2017, entry version 160.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Peptide 2k;
Contains:
RecName: Full=Capsid protein C;
AltName: Full=Core protein;
Contains:
RecName: Full=Protein prM;
Contains:
RecName: Full=Peptide pr;
Contains:
RecName: Full=Small envelope protein M;
AltName: Full=Matrix protein;
Contains:
RecName: Full=Envelope protein E;
Contains:
RecName: Full=Non-structural protein 1;
Short=NS1;
Contains:
RecName: Full=Non-structural protein 2A;
Short=NS2A;
Contains:
RecName: Full=Serine protease subunit NS2B;
AltName: Full=Flavivirin protease NS2B regulatory subunit;
AltName: Full=Non-structural protein 2B;
Contains:
RecName: Full=Serine protease NS3;
EC=3.4.21.91;
EC=3.6.1.15 {ECO:0000269|PubMed:19474250};
EC=3.6.4.13 {ECO:0000269|PubMed:19474250};
AltName: Full=Flavivirin protease NS3 catalytic subunit;
AltName: Full=Non-structural protein 3;
Contains:
RecName: Full=Non-structural protein 4A;
Short=NS4A;
Contains:
RecName: Full=Non-structural protein 4B;
Short=NS4B;
Contains:
RecName: Full=RNA-directed RNA polymerase NS5;
EC=2.1.1.56 {ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:20685660};
EC=2.1.1.57 {ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:20685660};
EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
AltName: Full=NS5;
Name=GP1 {ECO:0000312|EMBL:ANW69091.1};
ORFNames=MZ11_60484gpGP1 {ECO:0000312|EMBL:ANW69091.1},
MZ11_60553gpGP1 {ECO:0000312|EMBL:ANW69112.1};
West Nile virus (strain NY-99) (WNV) (West Nile virus (strain
NY-1999)).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; Japanese encephalitis virus group.
NCBI_TaxID=1968826;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
STRAIN=Isolate US/NY99-flamingo382/1999;
PubMed=10600742; DOI=10.1126/science.286.5448.2333;
Lanciotti R.S., Roehrig J.T., Deubel V., Smith J., Parker M.,
Steele K., Crise B., Volpe K.E., Crabtree M.B., Scherret J.H.,
Hall R.A., MacKenzie J.S., Cropp C.B., Panigrahy B., Ostlund E.,
Schmitt B., Malkinson M., Banet C., Weissman J., Komar N.,
Savage H.M., Stone W., McNamara T., Gubler D.J.;
"Origin of the West Nile virus responsible for an outbreak of
encephalitis in the northeastern United States.";
Science 286:2333-2337(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
STRAIN=Isolate US/NY2000-grouse3282/2000;
PubMed=12093177; DOI=10.1006/viro.2002.1449;
Lanciotti R.S., Ebel G.D., Deubel V., Kerst A.J., Murri S., Meyer R.,
Bowen M., McKinney N., Morrill W.E., Crabtree M.B., Kramer L.D.,
Roehrig J.T.;
"Complete genome sequences and phylogenetic analysis of West Nile
virus strains isolated from the United States, Europe, and the Middle
East.";
Virology 298:96-105(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
STRAIN=Isolate US/NY99-6922/1999;
PubMed=15557236; DOI=10.1099/vir.0.80247-0;
Shirato K., Miyoshi H., Goto A., Ako Y., Ueki T., Kariwa H.,
Takashima I.;
"Viral envelope protein glycosylation is a molecular determinant of
the neuroinvasiveness of the New York strain of West Nile virus.";
J. Gen. Virol. 85:3637-3645(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
STRAIN=NV-1/US/BID-V4187/1999, US/BID-V4186/1999, US/BID-V4188/1999,
and US/BID-V4189/1999;
PubMed=21723580; DOI=10.1016/j.virol.2011.06.006;
Armstrong P.M., Vossbrinck C.R., Andreadis T.G., Anderson J.F.,
Pesko K.N., Newman R.M., Lennon N.J., Birren B.W., Ebel G.D.,
Henn M.R.;
"Molecular evolution of West Nile virus in a northern temperate
region: Connecticut, USA 1999-2008.";
Virology 417:203-210(2011).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
Gao Y.W., Fan S.T., Sun H.T., Wang Z., Gao X.L., Li Y.G., Wang T.C.,
Zhang K., Xu W.W., Yu Z.J., Xia X.Z.;
Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
STRAIN=US/NY99-P2/1999;
Grinev A., Anez G., Rios M.;
"Complete genome sequence of West Nile virus strains used for the
formulation of CBER/FDA RNA reference reagents and lot release panels
for nucleic acid testing.";
Genome Announc. 2:E00811-E00814(2014).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
STRAIN=Culex/USA/29000529/2000, and Culex/USA/33020090/2002;
Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION (NON-STRUCTURAL PROTEIN 4B).
PubMed=15956546; DOI=10.1128/JVI.79.13.8004-8013.2005;
Munoz-Jordan J.L., Laurent-Rolle M., Ashour J., Martinez-Sobrido L.,
Ashok M., Lipkin W.I., Garcia-Sastre A.;
"Inhibition of alpha/beta interferon signaling by the NS4B protein of
flaviviruses.";
J. Virol. 79:8004-8013(2005).
[9]
FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5).
PubMed=15650160; DOI=10.1128/JVI.79.3.1343-1350.2005;
Guo J.T., Hayashi J., Seeger C.;
"West Nile virus inhibits the signal transduction pathway of alpha
interferon.";
J. Virol. 79:1343-1350(2005).
[10]
FUNCTION (NON-STRUCTURAL PROTEIN 1), AND INTERACTION WITH HOST
COMPLEMENT REGULATORY PROTEIN FACTOR H (NON-STRUCTURAL PROTEIN 1).
PubMed=17132743; DOI=10.1073/pnas.0605668103;
Chung K.M., Liszewski M.K., Nybakken G., Davis A.E., Townsend R.R.,
Fremont D.H., Atkinson J.P., Diamond M.S.;
"West Nile virus nonstructural protein NS1 inhibits complement
activation by binding the regulatory protein factor H.";
Proc. Natl. Acad. Sci. U.S.A. 103:19111-19116(2006).
[11]
FUNCTION (NON-STRUCTURAL PROTEIN 4A), CATALYTIC ACTIVITY (SERINE
PROTEASE NS3), AND MUTAGENESIS OF 2169-GLU--ASP-2173.
PubMed=19474250; DOI=10.1099/vir.0.012864-0;
Shiryaev S.A., Chernov A.V., Aleshin A.E., Shiryaeva T.N.,
Strongin A.Y.;
"NS4A regulates the ATPase activity of the NS3 helicase: a novel
cofactor role of the non-structural protein NS4A from West Nile
virus.";
J. Gen. Virol. 90:2081-2085(2009).
[12]
FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), CATALYTIC ACTIVITY
(RNA-DIRECTED RNA POLYMERASE NS5), AND MUTAGENESIS OF LYS-2557.
PubMed=19850911; DOI=10.1261/rna.1609709;
Issur M., Geiss B.J., Bougie I., Picard-Jean F., Despins S.,
Mayette J., Hobdey S.E., Bisaillon M.;
"The flavivirus NS5 protein is a true RNA guanylyltransferase that
catalyzes a two-step reaction to form the RNA cap structure.";
RNA 15:2340-2350(2009).
[13]
FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5).
PubMed=20106931; DOI=10.1128/JVI.01161-09;
Laurent-Rolle M., Boer E.F., Lubick K.J., Wolfinbarger J.B.,
Carmody A.B., Rockx B., Liu W., Ashour J., Shupert W.L.,
Holbrook M.R., Barrett A.D., Mason P.W., Bloom M.E., Garcia-Sastre A.,
Khromykh A.A., Best S.M.;
"The NS5 protein of the virulent West Nile virus NY99 strain is a
potent antagonist of type I interferon-mediated JAK-STAT signaling.";
J. Virol. 84:3503-3515(2010).
[14]
INTERACTION WITH NON-STRUCTURAL PROTEIN 4B (NON-STRUCTURAL PROTEIN 1),
AND INTERACTION WITH NON-STRUCTURAL PROTEIN 1 (NON-STRUCTURAL PROTEIN
4B).
PubMed=22553322; DOI=10.1128/JVI.00157-12;
Youn S., Li T., McCune B.T., Edeling M.A., Fremont D.H., Cristea I.M.,
Diamond M.S.;
"Evidence for a genetic and physical interaction between nonstructural
proteins NS1 and NS4B that modulates replication of West Nile virus.";
J. Virol. 86:7360-7371(2012).
[15]
FUNCTION (NON-STRUCTURAL PROTEIN 1).
PubMed=24245822; DOI=10.1186/1743-422X-10-339;
Youn S., Ambrose R.L., Mackenzie J.M., Diamond M.S.;
"Non-structural protein-1 is required for West Nile virus replication
complex formation and viral RNA synthesis.";
Virol. J. 10:339-339(2013).
[16]
FUNCTION (NON-STRUCTURAL PROTEIN 4B), SUBCELLULAR LOCATION
(NON-STRUCTURAL PROTEIN 4B), SUBCELLULAR LOCATION (NON-STRUCTURAL
PROTEIN 1), SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 4A), AND
FUNCTION (NON-STRUCTURAL PROTEIN 1).
PubMed=24465392; DOI=10.1371/journal.pone.0084040;
Kaufusi P.H., Kelley J.F., Yanagihara R., Nerurkar V.R.;
"Induction of endoplasmic reticulum-derived replication-competent
membrane structures by West Nile virus non-structural protein 4B.";
PLoS ONE 9:E84040-E84040(2014).
[17]
FUNCTION (NON-STRUCTURAL PROTEIN 1), AND MUTAGENESIS OF THR-968;
ASN-982; GLU-1029; ASN-1046; GLY-1086; THR-1108; PRO-1111 AND
MET-1124.
PubMed=24889229; DOI=10.1016/j.virol.2014.03.017;
Morrison C.R., Scholle F.;
"Abrogation of TLR3 inhibition by discrete amino acid changes in the
C-terminal half of the West Nile virus NS1 protein.";
Virology 456:96-107(2014).
[18]
FUNCTION (NON-STRUCTURAL PROTEIN 1), AND SUBCELLULAR LOCATION
(NON-STRUCTURAL PROTEIN 1).
PubMed=24928049; DOI=10.1016/j.virol.2014.04.036;
Crook K.R., Miller-Kittrell M., Morrison C.R., Scholle F.;
"Modulation of innate immune signaling by the secreted form of the
West Nile virus NS1 glycoprotein.";
Virology 458:172-182(2014).
[19] {ECO:0000244|PDB:2OY0}
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2534-2795 IN COMPLEX WITH
S-ADENOSYL-L-HOMOCYSTEINE, ACTIVE SITE, AND MUTAGENESIS OF LYS-2589;
ASP-2674; LYS-2710 AND GLU-2746.
PubMed=17267492; DOI=10.1128/JVI.02704-06;
Zhou Y., Ray D., Zhao Y., Dong H., Ren S., Li Z., Guo Y.,
Bernard K.A., Shi P.-Y., Li H.;
"Structure and function of flavivirus NS5 methyltransferase.";
J. Virol. 81:3891-3903(2007).
[20] {ECO:0000244|PDB:3I50}
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 291-692, AND DISULFIDE
BONDS.
PubMed=19713934; DOI=10.1038/emboj.2009.245;
Cherrier M.V., Kaufmann B., Nybakken G.E., Lok S.M., Warren J.T.,
Chen B.R., Nelson C.A., Kostyuchenko V.A., Holdaway H.A.,
Chipman P.R., Kuhn R.J., Diamond M.S., Rossmann M.G., Fremont D.H.;
"Structural basis for the preferential recognition of immature
flaviviruses by a fusion-loop antibody.";
EMBO J. 28:3269-3276(2009).
[21] {ECO:0000244|PDB:3LKZ}
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2529-2828 IN COMPLEX WITH
SIN INHIBITOR, CATALYTIC ACTIVITY (RNA-DIRECTED RNA POLYMERASE NS5),
FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), AND MUTAGENESIS OF
GLY-2676; ARG-2688; ARG-2691; VAL-2692 AND LEU-2712.
PubMed=20685660; DOI=10.1074/jbc.M110.129197;
Dong H., Liu L., Zou G., Zhao Y., Li Z., Lim S.P., Shi P.Y., Li H.;
"Structural and functional analyses of a conserved hydrophobic pocket
of flavivirus methyltransferase.";
J. Biol. Chem. 285:32586-32595(2010).
[22] {ECO:0000244|PDB:3IYW}
STRUCTURE BY ELECTRON MICROSCOPY (13.70 ANGSTROMS) OF 291-690,
DISULFIDE BONDS, AND SUBUNIT (ENVELOPE PROTEIN E).
PubMed=20956322; DOI=10.1073/pnas.1011036107;
Kaufmann B., Vogt M.R., Goudsmit J., Holdaway H.A., Aksyuk A.A.,
Chipman P.R., Kuhn R.J., Diamond M.S., Rossmann M.G.;
"Neutralization of West Nile virus by cross-linking of its surface
proteins with Fab fragments of the human monoclonal antibody CR4354.";
Proc. Natl. Acad. Sci. U.S.A. 107:18950-18955(2010).
[23] {ECO:0000244|PDB:3J0B}
STRUCTURE BY ELECTRON MICROSCOPY (10.30 ANGSTROMS) OF 291-690.
PubMed=23602814; DOI=10.1016/j.jsb.2013.04.005;
Zhang W., Kaufmann B., Chipman P.R., Kuhn R.J., Rossmann M.G.;
"Membrane curvature in flaviviruses.";
J. Struct. Biol. 183:86-94(2013).
[24] {ECO:0000244|PDB:4OIE, ECO:0000244|PDB:4OII}
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 963-1143, DISULFIDE BONDS,
AND SUBUNIT (NON-STRUCTURAL PROTEIN 1).
PubMed=24594604; DOI=10.1073/pnas.1322036111;
Edeling M.A., Diamond M.S., Fremont D.H.;
"Structural basis of flavivirus NS1 assembly and antibody
recognition.";
Proc. Natl. Acad. Sci. U.S.A. 111:4285-4290(2014).
[25] {ECO:0000244|PDB:4O6C, ECO:0000244|PDB:4O6D}
X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 791-1143, GLYCOSYLATION AT
ASN-921; ASN-966 AND ASN-998, DISULFIDE BONDS, AND SUBUNIT
(NON-STRUCTURAL PROTEIN 1).
PubMed=24505133; DOI=10.1126/science.1247749;
Akey D.L., Brown W.C., Dutta S., Konwerski J., Jose J., Jurkiw T.J.,
DelProposto J., Ogata C.M., Skiniotis G., Kuhn R.J., Smith J.L.;
"Flavivirus NS1 structures reveal surfaces for associations with
membranes and the immune system.";
Science 343:881-885(2014).
-!- FUNCTION: Capsid protein C: Plays a role in virus budding by
binding to the cell membrane and gathering the viral RNA into a
nucleocapsid that forms the core of a mature virus particle.
During virus entry, may induce genome penetration into the host
cytoplasm after hemifusion induced by the surface proteins. Can
migrate to the cell nucleus where it modulates host functions.
Overcomes the anti-viral effects of host EXOC1 by sequestering and
degrading the latter through the proteasome degradation pathway.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Capsid protein C: Inhibits RNA silencing by interfering
with host Dicer. {ECO:0000250|UniProtKB:P03314}.
-!- FUNCTION: Peptide pr: Prevents premature fusion activity of
envelope proteins in trans-Golgi by binding to envelope protein E
at pH6.0. After virion release in extracellular space, gets
dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Protein prM: Acts as a chaperone for envelope protein E
during intracellular virion assembly by masking and inactivating
envelope protein E fusion peptide. prM is the only viral peptide
matured by host furin in the trans-Golgi network probably to avoid
catastrophic activation of the viral fusion activity in acidic
Golgi compartment prior to virion release. prM-E cleavage is
inefficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Small envelope protein M: May play a role in virus
budding. Exerts cytotoxic effects by activating a mitochondrial
apoptotic pathway through M ectodomain. May display a viroporin
activity. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Envelope protein E: Binds to host cell surface receptor
and mediates fusion between viral and cellular membranes. Envelope
protein is synthesized in the endoplasmic reticulum in the form of
heterodimer with protein prM. They play a role in virion budding
in the ER, and the newly formed immature particle is covered with
60 spikes composed of heterodimer between precursor prM and
envelope protein E. The virion is transported to the Golgi
apparatus where the low pH causes dissociation of PrM-E
heterodimers and formation of E homodimers. prM-E cleavage is
inefficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 1: Involved in immune evasion,
pathogenesis and viral replication. Once cleaved off the
polyprotein, is targeted to three destinations: the viral
replication cycle, the plasma membrane and the extracellular
compartment. Essential for viral replication. Required for
formation of the replication complex and recruitment of other non-
structural proteins to the ER-derived membrane structures.
Excreted as a hexameric lipoparticle that plays a role against
host immune response. Antagonizing the complement function. Binds
to the host macrophages and dendritic cells. Inhibits signal
transduction originating from Toll-like receptor 3 (TLR3).
{ECO:0000269|PubMed:17132743, ECO:0000269|PubMed:24245822,
ECO:0000269|PubMed:24465392, ECO:0000269|PubMed:24889229,
ECO:0000269|PubMed:24928049}.
-!- FUNCTION: Non-structural protein 2A: Component of the viral RNA
replication complex that functions in virion assembly and
antagonizes the host alpha/beta interferon antiviral response.
{ECO:0000250|UniProtKB:P14335}.
-!- FUNCTION: Serine protease subunit NS2B: Required cofactor for the
serine protease function of NS3. May have membrane-destabilizing
activity and form viroporins (By similarity).
{ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00859}.
-!- FUNCTION: Serine protease NS3: Displays three enzymatic
activities: serine protease, NTPase and RNA helicase. NS3 serine
protease, in association with NS2B, performs its autocleavage and
cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM,
NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA
helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.
{ECO:0000255|PROSITE-ProRule:PRU00860,
ECO:0000269|PubMed:19474250}.
-!- FUNCTION: Non-structural protein 4A: Regulates the ATPase activity
of the NS3 helicase activity. NS4A allows NS3 helicase to conserve
energy during unwinding. {ECO:0000269|PubMed:19474250}.
-!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and
is required for the interferon antagonism activity of the latter.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 4B: Induces the formation of ER-
derived membrane vesicles where the viral replication takes place
(PubMed:24465392). Inhibits interferon (IFN)-induced host STAT1
phosphorylation and nuclear translocation, thereby preventing the
establishment of cellular antiviral state by blocking the IFN-
alpha/beta pathway (PubMed:15956546). Inhibits STAT2 translocation
in the nucleus after IFN-alpha treatment (PubMed:15956546).
{ECO:0000269|PubMed:15956546, ECO:0000269|PubMed:24465392}.
-!- FUNCTION: RNA-directed RNA polymerase NS5: Replicates the viral
(+) and (-) genome, and performs the capping of genomes in the
cytoplasm (PubMed:19850911). NS5 methylates viral RNA cap at
guanine N-7 and ribose 2'-O positions (PubMed:19850911,
PubMed:20685660). Besides its role in genome replication, also
prevents the establishment of cellular antiviral state by blocking
the interferon-alpha/beta (IFN-alpha/beta) signaling pathway
(PubMed:20106931). Inhibits host JAK1 and TYK2 phosphorylation,
thereby preventing activation of JAK-STAT signaling pathway
(PubMed:15650160). {ECO:0000269|PubMed:15650160,
ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:20106931,
ECO:0000269|PubMed:20685660}.
-!- CATALYTIC ACTIVITY: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds
in which each of the Xaa can be either Arg or Lys and Yaa can be
either Ser or Ala.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:19474250}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. {ECO:0000255|PROSITE-
ProRule:PRU00924, ECO:0000269|PubMed:19850911,
ECO:0000269|PubMed:20685660}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl
5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-
adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-
triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].
{ECO:0000255|PROSITE-ProRule:PRU00924,
ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:20685660}.
-!- SUBUNIT: Capsid protein C: Homodimer. Interacts (via N-terminus)
with host EXOC1 (via C-terminus); this interaction results in
EXOC1 degradation through the proteasome degradation pathway (By
similarity). Protein prM: Forms heterodimers with envelope protein
E in the endoplasmic reticulum and Golgi (By similarity). Envelope
protein E: Homodimer; in the endoplasmic reticulum and Golgi
(PubMed:20956322). Non-structural protein 1: Homodimer;
Homohexamer when secreted (PubMed:24505133, PubMed:24594604). NS1
interacts with NS4B (PubMed:22553322). Interacts with host
complement protein CFH; this interaction leads to the degradation
of C3 (PubMed:17132743). Non-structural protein 2B: Forms a
heterodimer with serine protease NS3. May form homooligomers (By
similarity). Serine protease NS3: Forms a heterodimer with NS2B.
Interacts with NS4B. Interacts with unphosphorylated RNA-directed
RNA polymerase NS5; this interaction stimulates RNA-directed RNA
polymerase NS5 guanylyltransferase activity (By similarity). Non-
structural protein 4B: Interacts with serine protease NS3 (By
similarity). Interacts with NS1 (PubMed:22553322). RNA-directed
RNA polymerase NS5: Homodimer (By similarity). Interacts with host
STAT2; this interaction inhibits the phosphorylation of the
latter, and, when all viral proteins are present (polyprotein),
targets STAT2 for degradation (By similarity).
{ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:17132743,
ECO:0000269|PubMed:20956322, ECO:0000269|PubMed:22553322,
ECO:0000269|PubMed:24505133, ECO:0000269|PubMed:24594604}.
-!- SUBCELLULAR LOCATION: Capsid protein C: Virion
{ECO:0000250|UniProtKB:P17763}. Host nucleus
{ECO:0000250|UniProtKB:P17763}. Host cytoplasm
{ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear
region {ECO:0000250|UniProtKB:P06935}.
-!- SUBCELLULAR LOCATION: Peptide pr: Secreted
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane
{ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
protein {ECO:0000255}. Note=ER membrane retention is mediated by
the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
-!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
{ECO:0000305}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
protein {ECO:0000255}. Note=ER membrane retention is mediated by
the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
-!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted
{ECO:0000269|PubMed:24928049}. Host endoplasmic reticulum membrane
{ECO:0000269|PubMed:24465392}; Peripheral membrane protein;
Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-
derived vesicles hosting the replication complex.
{ECO:0000269|PubMed:24465392}.
-!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host
endoplasmic reticulum membrane; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic
reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860};
Peripheral membrane protein {ECO:0000255|PROSITE-
ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-
ProRule:PRU00860}. Note=Remains non-covalently associated to
serine protease subunit NS2B. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic
reticulum membrane {ECO:0000269|PubMed:24465392}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in
RE-derived vesicles hosting the replication complex.
{ECO:0000269|PubMed:24465392}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic
reticulum membrane {ECO:0000269|PubMed:24465392}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in
RE-derived vesicles hosting the replication complex.
{ECO:0000269|PubMed:24465392}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase NS5: Host
endoplasmic reticulum membrane; Peripheral membrane protein;
Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}.
Note=Located in RE-associated vesicles hosting the replication
complex. NS5 protein is mainly localized in the nucleus rather
than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
-!- DOMAIN: The transmembrane domains of the small envelope protein M
and envelope protein E contain an endoplasmic reticulum retention
signal. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Genome polyprotein: Specific enzymatic cleavages in vivo
yield mature proteins. Cleavages in the lumen of endoplasmic
reticulum are performed by host signal peptidase, whereas
cleavages in the cytoplasmic side are performed by serine protease
NS3. Signal cleavage at the 2K-4B site requires a prior NS3
protease-mediated cleavage at the 4A-2K site.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: Protein prM: Cleaved in post-Golgi vesicles by a host furin,
releasing the mature small envelope protein M, and peptide pr.
This cleavage is incomplete as up to 30% of viral particles still
carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Envelope protein E: N-glycosylated.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: Non-structural protein 1: N-glycosylated (PubMed:24505133).
The excreted form is glycosylated and this is required for
efficient secretion of the protein from infected cells (By
similarity). {ECO:0000250|UniProtKB:P17763,
ECO:0000269|PubMed:24505133}.
-!- PTM: RNA-directed RNA polymerase NS5: Phosphorylated on serines
residues. This phosphorylation may trigger NS5 nuclear
localization. {ECO:0000250|UniProtKB:P17763}.
-!- SIMILARITY: In the N-terminal section; belongs to the class I-like
SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}.
-----------------------------------------------------------------------
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EMBL; AF196835; AAF20092.2; -; Genomic_RNA.
EMBL; AF404755; AAM81751.1; -; Genomic_RNA.
EMBL; HM488125; ADL27936.1; -; Genomic_RNA.
EMBL; HM488126; ADL27937.1; -; Genomic_RNA.
EMBL; HM488127; ADL27938.1; -; Genomic_RNA.
EMBL; HM488128; ADL27939.1; -; Genomic_RNA.
EMBL; KC407666; AGI15883.1; -; Genomic_RNA.
EMBL; KM083619; AIO10814.1; -; Genomic_RNA.
EMBL; KX547386; ANW69091.1; -; Genomic_RNA.
EMBL; KX547393; ANW69112.1; -; Genomic_RNA.
EMBL; AB185914; BAD34488.1; -; Genomic_RNA.
PDB; 2OY0; X-ray; 2.80 A; A/B=2534-2795.
PDB; 3I50; X-ray; 3.00 A; E=291-692.
PDB; 3IYW; EM; 13.70 A; A/B/C=291-690.
PDB; 3J0B; EM; 10.30 A; A/B/C=291-690.
PDB; 3LKZ; X-ray; 2.00 A; A/B=2529-2828.
PDB; 4O6C; X-ray; 2.75 A; A/B/C/D/E/F=791-1143.
PDB; 4O6D; X-ray; 2.59 A; A/B=791-1143.
PDB; 4OIE; X-ray; 1.85 A; A=963-1143.
PDB; 4OII; X-ray; 3.00 A; A/B=963-1143.
PDBsum; 2OY0; -.
PDBsum; 3I50; -.
PDBsum; 3IYW; -.
PDBsum; 3J0B; -.
PDBsum; 3LKZ; -.
PDBsum; 4O6C; -.
PDBsum; 4O6D; -.
PDBsum; 4OIE; -.
PDBsum; 4OII; -.
SMR; Q9Q6P4; -.
Proteomes; UP000096925; Genome.
Proteomes; UP000107647; Genome.
Proteomes; UP000123900; Genome.
Proteomes; UP000138291; Genome.
Proteomes; UP000139973; Genome.
Proteomes; UP000146770; Genome.
Proteomes; UP000163596; Genome.
Proteomes; UP000169485; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:InterPro.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IDA:UniProtKB.
GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039690; P:positive stranded viral RNA replication; IDA:UniProtKB.
GO; GO:0039573; P:suppression by virus of host complement activation; IDA:UniProtKB.
GO; GO:0039503; P:suppression by virus of host innate immune response; IDA:UniProtKB.
GO; GO:0039563; P:suppression by virus of host STAT1 activity; IDA:UniProtKB.
GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd12149; Flavi_E_C; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 3.30.387.10; -; 1.
Gene3D; 3.30.67.10; -; 1.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR000069; Env_glycoprot_M_flavivir.
InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
InterPro; IPR001122; Flavi_capsidC.
InterPro; IPR037172; Flavi_capsidC_sf.
InterPro; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
InterPro; IPR001157; Flavi_NS1.
InterPro; IPR000752; Flavi_NS2A.
InterPro; IPR000487; Flavi_NS2B.
InterPro; IPR000404; Flavi_NS4A.
InterPro; IPR001528; Flavi_NS4B.
InterPro; IPR002535; Flavi_propep.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
InterPro; IPR013756; GlyE_cen_dom_subdom2.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR000208; RNA-dir_pol_flavivirus.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01003; Flavi_capsid; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF02832; Flavi_glycop_C; 1.
Pfam; PF00869; Flavi_glycoprot; 1.
Pfam; PF01004; Flavi_M; 1.
Pfam; PF00948; Flavi_NS1; 1.
Pfam; PF01005; Flavi_NS2A; 1.
Pfam; PF01002; Flavi_NS2B; 1.
Pfam; PF01350; Flavi_NS4A; 1.
Pfam; PF01349; Flavi_NS4B; 1.
Pfam; PF00972; Flavi_NS5; 1.
Pfam; PF01570; Flavi_propep; 1.
Pfam; PF01728; FtsJ; 1.
Pfam; PF00949; Peptidase_S7; 1.
PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF101257; SSF101257; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
TIGRFAMs; TIGR04240; flavi_E_stem; 1.
PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus; ATP-binding;
Capsid protein; Complete proteome; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
Host cytoplasm; Host endoplasmic reticulum; Host membrane;
Host nucleus; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host STAT1 by virus; Inhibition of host STAT2 by virus;
Membrane; Metal-binding; Methyltransferase; Nucleotide-binding;
Nucleotidyltransferase; Phosphoprotein; Protease; RNA-binding;
RNA-directed RNA polymerase; Secreted; Serine protease;
Suppressor of RNA silencing; Transferase; Transmembrane;
Transmembrane helix; Viral attachment to host cell;
Viral immunoevasion; Viral penetration into host cytoplasm;
Viral RNA replication; Virion; Virus entry into host cell; Zinc.
CHAIN 1 3433 Genome polyprotein.
/FTId=PRO_0000441576.
CHAIN 1 105 Capsid protein C.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441577.
PROPEP 106 123 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441578.
CHAIN 124 290 Protein prM.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441579.
CHAIN 124 215 Peptide pr.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441580.
CHAIN 216 290 Small envelope protein M.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441581.
CHAIN 291 791 Envelope protein E.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441582.
CHAIN 792 1143 Non-structural protein 1.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441583.
CHAIN 1144 1374 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441584.
CHAIN 1375 1505 Serine protease subunit NS2B.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441585.
CHAIN 1506 2124 Serine protease NS3.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441586.
CHAIN 2125 2250 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441587.
PEPTIDE 2251 2273 Peptide 2k.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441588.
CHAIN 2274 2528 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441589.
CHAIN 2529 3433 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000441590.
TOPO_DOM 2 108 Cytoplasmic. {ECO:0000255}.
TRANSMEM 109 129 Helical. {ECO:0000255}.
TOPO_DOM 130 248 Extracellular. {ECO:0000255}.
TRANSMEM 249 269 Helical. {ECO:0000255}.
TOPO_DOM 270 275 Cytoplasmic. {ECO:0000255}.
TRANSMEM 276 290 Helical. {ECO:0000305}.
TOPO_DOM 291 743 Extracellular. {ECO:0000255}.
TRANSMEM 744 764 Helical. {ECO:0000255}.
TOPO_DOM 765 770 Cytoplasmic. {ECO:0000255}.
TRANSMEM 771 791 Helical. {ECO:0000255}.
TOPO_DOM 792 1216 Extracellular. {ECO:0000255}.
TRANSMEM 1217 1237 Helical. {ECO:0000255}.
TOPO_DOM 1238 1245 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1246 1268 Helical. {ECO:0000255}.
TOPO_DOM 1269 1288 Lumenal. {ECO:0000255}.
TRANSMEM 1289 1309 Helical. {ECO:0000255}.
TOPO_DOM 1310 1313 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1314 1331 Helical. {ECO:0000255}.
TOPO_DOM 1332 1345 Lumenal. {ECO:0000255}.
TRANSMEM 1346 1366 Helical. {ECO:0000255}.
TOPO_DOM 1367 1375 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1376 1396 Helical. {ECO:0000255}.
TOPO_DOM 1397 1399 Lumenal. {ECO:0000255}.
TRANSMEM 1400 1420 Helical. {ECO:0000255}.
TOPO_DOM 1421 1477 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1478 1498 Helical. {ECO:0000255}.
TOPO_DOM 1499 2174 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2175 2195 Helical. {ECO:0000255}.
TOPO_DOM 2196 2200 Lumenal. {ECO:0000255}.
INTRAMEM 2201 2221 Helical. {ECO:0000255}.
TOPO_DOM 2222 2222 Lumenal. {ECO:0000255}.
TRANSMEM 2223 2243 Helical. {ECO:0000255}.
TOPO_DOM 2244 2258 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2259 2279 Helical; Note=Signal for NS4B.
{ECO:0000255}.
TOPO_DOM 2280 2312 Lumenal. {ECO:0000255}.
INTRAMEM 2313 2333 Helical. {ECO:0000255}.
TOPO_DOM 2334 2380 Lumenal. {ECO:0000255}.
TRANSMEM 2381 2401 Helical. {ECO:0000255}.
TOPO_DOM 2402 2444 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2445 2465 Helical. {ECO:0000255}.
TOPO_DOM 2466 2470 Lumenal. {ECO:0000255}.
TRANSMEM 2471 2491 Helical. {ECO:0000255}.
TOPO_DOM 2492 3433 Cytoplasmic. {ECO:0000255}.
DOMAIN 1506 1683 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1686 1842 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1853 2018 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2529 2794 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3058 3210 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1699 1706 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 2 15 Interaction with host EXOC1.
{ECO:0000250|UniProtKB:P06935}.
REGION 37 72 Hydrophobic; homodimerization of capsid
protein C.
{ECO:0000250|UniProtKB:P29990}.
REGION 388 401 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
REGION 1428 1467 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
REGION 1690 1693 Important for RNA-binding.
{ECO:0000250|UniProtKB:P14340}.
REGION 2169 2173 Regulates the ATPase activity of NS3
helicase. {ECO:0000269|PubMed:19474250}.
REGION 2614 2615 S-adenosyl-L-homocysteine binding.
{ECO:0000244|PDB:2OY0}.
REGION 2659 2660 S-adenosyl-L-homocysteine binding.
{ECO:0000244|PDB:2OY0}.
MOTIF 1790 1793 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
COMPBIAS 281 284 Poly-Leu. {ECO:0000255}.
ACT_SITE 1556 1556 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1580 1580 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1640 1640 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 2589 2589 For 2'-O-MTase activity.
{ECO:0000269|PubMed:17267492}.
ACT_SITE 2674 2674 For 2'-O-MTase activity.
{ECO:0000269|PubMed:17267492}.
ACT_SITE 2710 2710 For 2'-O-MTase activity.
{ECO:0000269|PubMed:17267492}.
ACT_SITE 2746 2746 For 2'-O-MTase activity.
{ECO:0000269|PubMed:17267492}.
METAL 2968 2968 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 2972 2972 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:P14335}.
METAL 2977 2977 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 2980 2980 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 3245 3245 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:P14335}.
METAL 3261 3261 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
METAL 3380 3380 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
BINDING 2541 2541 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2544 2544 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2545 2545 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2547 2547 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2556 2556 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2584 2584 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924,
ECO:0000269|PubMed:17267492}.
BINDING 2614 2614 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2615 2615 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2632 2632 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2633 2633 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2639 2639 S-adenosyl-L-homocysteine.
{ECO:0000269|PubMed:17267492}.
BINDING 2659 2659 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2660 2660 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2674 2674 S-adenosyl-L-homocysteine.
{ECO:0000269|PubMed:17267492}.
BINDING 2678 2678 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2741 2741 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2743 2743 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2748 2748 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 105 106 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P06935}.
SITE 123 124 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P06935}.
SITE 215 216 Cleavage; by host furin.
{ECO:0000250|UniProtKB:P06935}.
SITE 290 291 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P06935}.
SITE 791 792 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P06935}.
SITE 1143 1144 Cleavage; by host.
{ECO:0000250|UniProtKB:P06935}.
SITE 1374 1375 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P06935}.
SITE 1505 1506 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P06935}.
SITE 1963 1963 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 1966 1966 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 2124 2125 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P06935}.
SITE 2250 2251 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P06935}.
SITE 2273 2274 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P06935}.
SITE 2528 2529 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P06935}.
SITE 2552 2552 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00924,
ECO:0000269|PubMed:17267492}.
SITE 2589 2589 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2674 2674 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2675 2675 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2710 2710 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2746 2746 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
MOD_RES 2584 2584 Phosphoserine.
{ECO:0000250|UniProtKB:P03314}.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:P14335}.
CARBOHYD 921 921 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000269|PubMed:24505133}.
CARBOHYD 966 966 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000269|PubMed:24505133}.
CARBOHYD 998 998 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000269|PubMed:24505133}.
DISULFID 293 320 {ECO:0000269|PubMed:20956322}.
DISULFID 350 411 {ECO:0000269|PubMed:19713934,
ECO:0000269|PubMed:20956322}.
DISULFID 350 406 {ECO:0000250|UniProtKB:P06935}.
DISULFID 364 395 {ECO:0000269|PubMed:19713934,
ECO:0000269|PubMed:20956322}.
DISULFID 382 411 {ECO:0000250|UniProtKB:P06935}.
DISULFID 382 406 {ECO:0000269|PubMed:19713934,
ECO:0000269|PubMed:20956322}.
DISULFID 480 578 {ECO:0000269|PubMed:19713934,
ECO:0000269|PubMed:20956322}.
DISULFID 595 626 {ECO:0000269|PubMed:20956322}.
DISULFID 795 806 {ECO:0000269|PubMed:24505133}.
DISULFID 846 934 {ECO:0000269|PubMed:24505133}.
DISULFID 970 1014 {ECO:0000269|PubMed:24505133,
ECO:0000269|PubMed:24594604}.
DISULFID 1071 1120 {ECO:0000269|PubMed:24505133,
ECO:0000269|PubMed:24594604}.
DISULFID 1082 1103 {ECO:0000269|PubMed:24505133,
ECO:0000269|PubMed:24594604}.
DISULFID 1104 1107 {ECO:0000269|PubMed:24505133,
ECO:0000269|PubMed:24594604}.
MUTAGEN 968 968 T->N: No effect on TL3 signaling
inhibition by NS1.
{ECO:0000269|PubMed:24889229}.
MUTAGEN 982 982 N->I: No effect on TL3 signaling
inhibition by NS1.
{ECO:0000269|PubMed:24889229}.
MUTAGEN 1029 1029 E->V: No effect on TL3 signaling
inhibition by NS1.
{ECO:0000269|PubMed:24889229}.
MUTAGEN 1046 1046 N->D: Complete loss of TL3 signaling
inhibition by NS1.
{ECO:0000269|PubMed:24889229}.
MUTAGEN 1086 1086 G->R: Almost no effect on TL3 signaling
inhibition by NS1.
{ECO:0000269|PubMed:24889229}.
MUTAGEN 1108 1108 T->I: Complete loss of TL3 signaling
inhibition by NS1.
{ECO:0000269|PubMed:24889229}.
MUTAGEN 1111 1111 P->S: About 50% loss of TL3 signaling
inhibition by NS1.
{ECO:0000269|PubMed:24889229}.
MUTAGEN 1124 1124 M->V: About 50% loss of TL3 signaling
inhibition by NS1.
{ECO:0000269|PubMed:24889229}.
MUTAGEN 2169 2173 EELPD->KKLPK: Complete loss of regulation
of the ATPase activity of NS3 helicase by
NS4A. {ECO:0000269|PubMed:19474250}.
MUTAGEN 2557 2557 K->A: 85% loss of NS5-GMP formation.
{ECO:0000269|PubMed:19850911}.
MUTAGEN 2589 2589 K->A,E,R: Complete loss of 2'-O-
methyltranferase activity.
{ECO:0000269|PubMed:17267492}.
MUTAGEN 2674 2674 D->A,N,K: Complete loss of 2'-O-
methyltranferase activity.
{ECO:0000269|PubMed:17267492}.
MUTAGEN 2676 2676 G->A: 86% loss of N7 guanine
methyltransferase activity; 60% loss of
2'-O-methyltranferase activity.
{ECO:0000269|PubMed:20685660}.
MUTAGEN 2688 2688 R->A: 78% loss of N7 guanine
methyltransferase activity; no effect 2'-
O-methyltranferase activity.
{ECO:0000269|PubMed:20685660}.
MUTAGEN 2691 2691 R->A: 50% loss of N7 guanine
methyltransferase activity; no effect 2'-
O-methyltranferase activity.
{ECO:0000269|PubMed:20685660}.
MUTAGEN 2692 2692 V->A: 10% loss of N7 guanine
methyltransferase activity; 50% loss of
2'-O-methyltranferase activity.
{ECO:0000269|PubMed:20685660}.
MUTAGEN 2710 2710 K->A,E,N: Complete loss of 2'-O-
methyltranferase activity.
{ECO:0000269|PubMed:17267492}.
MUTAGEN 2712 2712 L->A: 20% loss of N7 guanine
methyltransferase activity7; 74% loss of
2'-O-methyltranferase activity.
{ECO:0000269|PubMed:20685660}.
MUTAGEN 2746 2746 E->A,D,K: Complete loss of 2'-O-
methyltranferase activity.
{ECO:0000269|PubMed:17267492}.
STRAND 299 303 {ECO:0000244|PDB:3I50}.
STRAND 312 314 {ECO:0000244|PDB:3I50}.
STRAND 320 324 {ECO:0000244|PDB:3I50}.
STRAND 326 328 {ECO:0000244|PDB:3I50}.
STRAND 331 342 {ECO:0000244|PDB:3I50}.
STRAND 344 363 {ECO:0000244|PDB:3I50}.
STRAND 365 367 {ECO:0000244|PDB:3I50}.
HELIX 373 376 {ECO:0000244|PDB:3I50}.
STRAND 380 389 {ECO:0000244|PDB:3I50}.
HELIX 391 393 {ECO:0000244|PDB:3I50}.
STRAND 399 412 {ECO:0000244|PDB:3I50}.
STRAND 414 419 {ECO:0000244|PDB:3I50}.
HELIX 422 424 {ECO:0000244|PDB:3I50}.
STRAND 425 431 {ECO:0000244|PDB:3I50}.
STRAND 461 463 {ECO:0000244|PDB:3I50}.
HELIX 471 473 {ECO:0000244|PDB:3I50}.
STRAND 474 479 {ECO:0000244|PDB:3I50}.
STRAND 484 486 {ECO:0000244|PDB:3I50}.
STRAND 490 495 {ECO:0000244|PDB:3I50}.
STRAND 500 504 {ECO:0000244|PDB:3I50}.
HELIX 505 508 {ECO:0000244|PDB:3I50}.
HELIX 527 529 {ECO:0000244|PDB:3I50}.
STRAND 530 532 {ECO:0000244|PDB:3I50}.
STRAND 542 544 {ECO:0000244|PDB:3I50}.
HELIX 549 553 {ECO:0000244|PDB:3I50}.
STRAND 557 559 {ECO:0000244|PDB:3I50}.
STRAND 567 570 {ECO:0000244|PDB:3I50}.
STRAND 577 581 {ECO:0000244|PDB:3I50}.
HELIX 582 584 {ECO:0000244|PDB:3I50}.
STRAND 792 798 {ECO:0000244|PDB:4O6D}.
HELIX 799 801 {ECO:0000244|PDB:4O6D}.
STRAND 803 813 {ECO:0000244|PDB:4O6D}.
TURN 816 818 {ECO:0000244|PDB:4O6D}.
HELIX 819 822 {ECO:0000244|PDB:4O6D}.
STRAND 823 828 {ECO:0000244|PDB:4O6D}.
HELIX 830 841 {ECO:0000244|PDB:4O6D}.
TURN 842 844 {ECO:0000244|PDB:4O6D}.
HELIX 853 872 {ECO:0000244|PDB:4O6D}.
STRAND 878 881 {ECO:0000244|PDB:4O6D}.
STRAND 922 927 {ECO:0000244|PDB:4O6D}.
STRAND 932 934 {ECO:0000244|PDB:4O6D}.
HELIX 936 938 {ECO:0000244|PDB:4O6D}.
STRAND 944 950 {ECO:0000244|PDB:4O6D}.
STRAND 956 962 {ECO:0000244|PDB:4O6D}.
HELIX 972 974 {ECO:0000244|PDB:4O6D}.
STRAND 975 980 {ECO:0000244|PDB:4OIE}.
STRAND 983 1010 {ECO:0000244|PDB:4OIE}.
HELIX 1018 1020 {ECO:0000244|PDB:4OIE}.
HELIX 1029 1031 {ECO:0000244|PDB:4OIE}.
HELIX 1036 1038 {ECO:0000244|PDB:4OIE}.
STRAND 1061 1069 {ECO:0000244|PDB:4OIE}.
STRAND 1075 1078 {ECO:0000244|PDB:4OIE}.
STRAND 1080 1082 {ECO:0000244|PDB:4O6C}.
STRAND 1089 1092 {ECO:0000244|PDB:4OIE}.
STRAND 1094 1096 {ECO:0000244|PDB:4O6D}.
STRAND 1101 1106 {ECO:0000244|PDB:4OIE}.
STRAND 1112 1116 {ECO:0000244|PDB:4OIE}.
STRAND 1119 1122 {ECO:0000244|PDB:4OIE}.
STRAND 1126 1129 {ECO:0000244|PDB:4OIE}.
HELIX 2536 2544 {ECO:0000244|PDB:3LKZ}.
HELIX 2549 2555 {ECO:0000244|PDB:3LKZ}.
TURN 2556 2559 {ECO:0000244|PDB:3LKZ}.
STRAND 2561 2563 {ECO:0000244|PDB:3LKZ}.
HELIX 2566 2574 {ECO:0000244|PDB:3LKZ}.
STRAND 2583 2585 {ECO:0000244|PDB:2OY0}.
HELIX 2586 2595 {ECO:0000244|PDB:3LKZ}.
STRAND 2603 2608 {ECO:0000244|PDB:3LKZ}.
HELIX 2614 2619 {ECO:0000244|PDB:3LKZ}.
STRAND 2625 2631 {ECO:0000244|PDB:3LKZ}.
HELIX 2649 2651 {ECO:0000244|PDB:3LKZ}.
STRAND 2652 2655 {ECO:0000244|PDB:3LKZ}.
TURN 2660 2662 {ECO:0000244|PDB:2OY0}.
STRAND 2669 2673 {ECO:0000244|PDB:3LKZ}.
HELIX 2682 2700 {ECO:0000244|PDB:3LKZ}.
STRAND 2706 2712 {ECO:0000244|PDB:3LKZ}.
HELIX 2717 2730 {ECO:0000244|PDB:3LKZ}.
STRAND 2733 2735 {ECO:0000244|PDB:3LKZ}.
STRAND 2747 2750 {ECO:0000244|PDB:3LKZ}.
HELIX 2757 2770 {ECO:0000244|PDB:3LKZ}.
STRAND 2781 2783 {ECO:0000244|PDB:3LKZ}.
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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