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 POLG_KUNJM              Reviewed;        3433 AA.
P14335; Q7T4P4; Q7T4P5; Q82983;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
22-NOV-2017, entry version 165.
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;
EC=3.6.4.13 {ECO:0000269|PubMed:17658551};
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};
EC=2.1.1.57 {ECO:0000255|PROSITE-ProRule:PRU00924};
EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
AltName: Full=NS5;
Kunjin virus (strain MRM61C).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; Japanese encephalitis virus group.
NCBI_TaxID=11078;
NCBI_TaxID=8920; Ciconiiformes.
NCBI_TaxID=162997; Culex annulirostris (Common banded mosquito).
NCBI_TaxID=9796; Equus caballus (Horse).
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2826659; DOI=10.1099/0022-1317-69-1-1;
Coia G., Parker M.D., Speight G., Byrne M.E., Westaway E.G.;
"Nucleotide and complete amino acid sequences of Kunjin virus:
definitive gene order and characteristics of the virus-specified
proteins.";
J. Gen. Virol. 69:1-21(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Infectious clone FLSDX, and Infectious clone pAKUN;
PubMed=12829820; DOI=10.1128/JVI.77.14.7804-7813.2003;
Liu W.J., Chen H.B., Khromykh A.A.;
"Molecular and functional analyses of Kunjin virus infectious cDNA
clones demonstrate the essential role for NS2A in virus assembly and
for a nonconservative residue in NS3 in RNA replication.";
J. Virol. 77:7804-7813(2003).
[3]
SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 2A), AND SUBCELLULAR
LOCATION (NON-STRUCTURAL PROTEIN 4A).
PubMed=9636360; DOI=10.1006/viro.1998.9156;
Mackenzie J.M., Khromykh A.A., Jones M.K., Westaway E.G.;
"Subcellular localization and some biochemical properties of the
flavivirus Kunjin nonstructural proteins NS2A and NS4A.";
Virology 245:203-215(1998).
[4]
FUNCTION (NON-STRUCTURAL PROTEIN 2A), AND MUTAGENESIS OF ALA-1173;
ASN-1244 AND PRO-2798.
PubMed=15507609; DOI=10.1128/JVI.78.22.12225-12235.2004;
Liu W.J., Chen H.B., Wang X.J., Huang H., Khromykh A.A.;
"Analysis of adaptive mutations in Kunjin virus replicon RNA reveals a
novel role for the flavivirus nonstructural protein NS2A in inhibition
of beta interferon promoter-driven transcription.";
J. Virol. 78:12225-12235(2004).
[5]
FUNCTION (NON-STRUCTURAL PROTEIN 2A), FUNCTION (NON-STRUCTURAL PROTEIN
2B), FUNCTION (NON-STRUCTURAL PROTEIN 3), FUNCTION (NON-STRUCTURAL
PROTEIN 4A), AND FUNCTION (NON-STRUCTURAL PROTEIN 4B).
PubMed=15650219; DOI=10.1128/JVI.79.3.1934-1942.2005;
Liu W.J., Wang X.J., Mokhonov V.V., Shi P.Y., Randall R.,
Khromykh A.A.;
"Inhibition of interferon signaling by the New York 99 strain and
Kunjin subtype of West Nile virus involves blockage of STAT1 and STAT2
activation by nonstructural proteins.";
J. Virol. 79:1934-1942(2005).
[6]
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).
[7]
MUTAGENESIS OF ALA-1173.
PubMed=16474146; DOI=10.1128/JVI.80.5.2396-2404.2006;
Liu W.J., Wang X.J., Clark D.C., Lobigs M., Hall R.A., Khromykh A.A.;
"A single amino acid substitution in the West Nile virus nonstructural
protein NS2A disables its ability to inhibit alpha/beta interferon
induction and attenuates virus virulence in mice.";
J. Virol. 80:2396-2404(2006).
[8]
FUNCTION (NON-STRUCTURAL PROTEIN 4A).
PubMed=16611922; DOI=10.1128/JVI.80.9.4623-4632.2006;
Roosendaal J., Westaway E.G., Khromykh A., Mackenzie J.M.;
"Regulated cleavages at the West Nile virus NS4A-2K-NS4B junctions
play a major role in rearranging cytoplasmic membranes and Golgi
trafficking of the NS4A protein.";
J. Virol. 80:4623-4632(2006).
[9]
FUNCTION (NON-STRUCTURAL PROTEIN 2A), MUTAGENESIS OF THR-1292, AND
CHARACTERIZATION OF VARIANT ASN-1202.
PubMed=18337583; DOI=10.1128/JVI.00002-08;
Leung J.Y., Pijlman G.P., Kondratieva N., Hyde J., Mackenzie J.M.,
Khromykh A.A.;
"Role of nonstructural protein NS2A in flavivirus assembly.";
J. Virol. 82:4731-4741(2008).
[10]
FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), AND MUTAGENESIS OF
SER-3181.
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).
[11]
MUTAGENESIS OF PRO-2244; GLU-2245; PRO-2246 AND GLU-2247.
PubMed=21880777; DOI=10.1128/JVI.05864-11;
Ambrose R.L., Mackenzie J.M.;
"A conserved peptide in West Nile virus NS4A protein contributes to
proteolytic processing and is essential for replication.";
J. Virol. 85:11274-11282(2011).
[12]
FUNCTION (NON-STRUCTURAL PROTEIN 4A), AND MUTAGENESIS OF PRO-2137;
PRO-2172; ASP-2173 AND GLY-2190.
PubMed=25771497; DOI=10.1016/j.virol.2015.02.045;
Ambrose R.L., Mackenzie J.M.;
"Conserved amino acids within the N-terminus of the West Nile virus
NS4A protein contribute to virus replication, protein stability and
membrane proliferation.";
Virology 481:95-106(2015).
[13]
X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 23-98 IN COMPLEX WITH
CALCIUM, AND SUBUNIT (CAPSID PROTEIN C).
PubMed=15242592; DOI=10.1016/j.str.2004.04.024;
Dokland T., Walsh M., Mackenzie J.M., Khromykh A.A., Ee K.H., Wang S.;
"West Nile virus core protein; tetramer structure and ribbon
formation.";
Structure 12:1157-1163(2004).
[14] {ECO:0000244|PDB:2HCN, ECO:0000244|PDB:2HCS, ECO:0000244|PDB:2HFZ}
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 2846-3433 IN COMPLEX WITH
ZINC.
PubMed=17287213; DOI=10.1074/jbc.M607273200;
Malet H., Egloff M.P., Selisko B., Butcher R.E., Wright P.J.,
Roberts M., Gruez A., Sulzenbacher G., Vonrhein C., Bricogne G.,
Mackenzie J.M., Khromykh A.A., Davidson A.D., Canard B.;
"Crystal structure of the RNA polymerase domain of the West Nile virus
non-structural protein 5.";
J. Biol. Chem. 282:10678-10689(2007).
[15] {ECO:0000244|PDB:2QEQ}
X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1691-2124, AND CATALYTIC
ACTIVITY (SERINE PROTEASE NS3).
PubMed=17658551; DOI=10.1016/j.jmb.2007.06.055;
Mastrangelo E., Milani M., Bollati M., Selisko B., Peyrane F.,
Pandini V., Sorrentino G., Canard B., Konarev P.V., Svergun D.I.,
de Lamballerie X., Coutard B., Khromykh A.A., Bolognesi M.;
"Crystal structure and activity of Kunjin virus NS3 helicase; protease
and helicase domain assembly in the full length NS3 protein.";
J. Mol. Biol. 372:444-455(2007).
[16] {ECO:0000244|PDB:2OF6}
STRUCTURE BY ELECTRON MICROSCOPY (24.00 ANGSTROMS) OF 291-690,
SUBCELLULAR LOCATION (ENVELOPE PROTEIN E), AND GLYCOSYLATION AT
ASN-138.
PubMed=17376919; DOI=10.1128/JVI.00037-07;
Zhang Y., Kaufmann B., Chipman P.R., Kuhn R.J., Rossmann M.G.;
"Structure of immature West Nile virus.";
J. Virol. 81:6141-6145(2007).
-!- 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:0000250|UniProtKB:Q9Q6P4}.
-!- 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
(PubMed:15507609, PubMed:18337583). Inhibits STAT2 translocation
in the nucleus after IFN-alpha treatment (PubMed:15650219).
{ECO:0000269|PubMed:15507609, ECO:0000269|PubMed:15650219,
ECO:0000269|PubMed:18337583}.
-!- FUNCTION: Serine protease subunit NS2B: Required cofactor for the
serine protease function of NS3. May have membrane-destabilizing
activity and form viroporins (By similarity). Inhibits STAT2
translocation in the nucleus after IFN-alpha treatment
(PubMed:15650219). {ECO:0000250|UniProtKB:P17763,
ECO:0000255|PROSITE-ProRule:PRU00859,
ECO:0000269|PubMed:15650219}.
-!- 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.
NS3 supports the separation of RNA daughter and template strands
during viral replication. In addition, NS3 assists the initiation
of replication by unwinding the RNA secondary structure in the 3'
non-translated region (NTR). Inhibits STAT2 translocation in the
nucleus after IFN-alpha treatment (PubMed:15650219).
{ECO:0000255|PROSITE-ProRule:PRU00860,
ECO:0000269|PubMed:15650219}.
-!- FUNCTION: Non-structural protein 4A: Regulates the ATPase activity
of the NS3 helicase activity (By similarity). NS4A allows NS3
helicase to conserve energy during unwinding (By similarity).
Induces host ER membrane rearrangements to provide a compartment
where viral replication can take part (PubMed:16611922,
PubMed:25771497). Inhibits STAT2 translocation in the nucleus
after IFN-alpha treatment (PubMed:15650219).
{ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:15650219,
ECO:0000269|PubMed:16611922, ECO:0000269|PubMed:25771497}.
-!- 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
(By similarity). 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:15650219). Inhibits STAT2 translocation
in the nucleus after IFN-alpha treatment (PubMed:15650219).
{ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:15650219}.
-!- FUNCTION: RNA-directed RNA polymerase NS5: Replicates the viral
(+) and (-) genome, and performs the capping of genomes in the
cytoplasm (By similarity). NS5 methylates viral RNA cap at guanine
N-7 and ribose 2'-O positions (By similarity). 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:15650160, PubMed:20106931).
Inhibits host JAK1 and TYK2 phosphorylation, thereby preventing
activation of JAK-STAT signaling pathway (PubMed:15650160).
{ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:15650160,
ECO:0000269|PubMed:20106931}.
-!- 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:17658551}.
-!- 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}.
-!- 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}.
-!- SUBUNIT: Capsid protein C: Homodimer; further assembles as a
homotetramer (PubMed:15242592). 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 (By
similarity). Non-structural protein 1: Homodimer; Homohexamer when
secreted (By similarity). NS1 interacts with NS4B (By similarity).
Interacts with host complement protein CFH; this interaction leads
to the degradation of C3 (By similarity). Non-structural protein
2A: Interacts (via N-terminus) with serine protease NS3 (By
similarity). Non-structural protein 2B: Forms a heterodimer with
serine protease NS3 (By similarity). May form homooligomers (By
similarity). Serine protease NS3: Forms a heterodimer with NS2B
(By similarity). Interacts with NS4B (By similarity). Interacts
with unphosphorylated RNA-directed RNA polymerase NS5; this
interaction stimulates RNA-directed RNA polymerase NS5
guanylyltransferase activity (By similarity). Serine protease NS3:
Forms a heterodimer with NS2B (By similarity). Interacts with NS4B
(By similarity). 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 (By similarity). 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:15242592}.
-!- 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:0000269|PubMed:17376919}; 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:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
membrane; Peripheral membrane protein; Lumenal side
{ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived
vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic
reticulum membrane {ECO:0000269|PubMed:9636360}; 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:9636360}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in
RE-associated vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in
RE-derived vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- 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:0000269|PubMed:17376919}.
-!- PTM: Non-structural protein 1: N-glycosylated. The excreted form
is glycosylated and this is required for efficient secretion of
the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.
-!- 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; D00246; BAA00176.1; -; Genomic_RNA.
EMBL; AY274504; AAP78941.1; -; Genomic_RNA.
EMBL; AY274505; AAP78942.1; -; Genomic_RNA.
PIR; A28697; GNWVKV.
PDB; 1SFK; X-ray; 3.20 A; A/B/C/D/E/F/G/H=23-98.
PDB; 2HCN; X-ray; 2.35 A; A=2846-3433.
PDB; 2HCS; X-ray; 2.50 A; A=2846-3433.
PDB; 2HFZ; X-ray; 3.00 A; A=2802-3433.
PDB; 2OF6; EM; 24.00 A; A/B/C=291-690.
PDB; 2QEQ; X-ray; 3.10 A; A/B=1691-2124.
PDBsum; 1SFK; -.
PDBsum; 2HCN; -.
PDBsum; 2HCS; -.
PDBsum; 2HFZ; -.
PDBsum; 2OF6; -.
PDBsum; 2QEQ; -.
ProteinModelPortal; P14335; -.
SMR; P14335; -.
IntAct; P14335; 37.
MEROPS; S07.003; -.
PeptideAtlas; P14335; -.
OrthoDB; VOG090001DL; -.
EvolutionaryTrace; P14335; -.
Proteomes; UP000008379; Genome.
Proteomes; UP000099558; Genome.
Proteomes; UP000138183; 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:UniProtKB-KW.
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; IEA:UniProtKB-EC.
GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
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:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
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:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0039576; P:suppression by virus of host JAK1 activity; IEA:UniProtKB-KW.
GO; GO:0039563; P:suppression by virus of host STAT1 activity; IDA:UniProtKB.
GO; GO:0039564; P:suppression by virus of host STAT2 activity; IDA:UniProtKB.
GO; GO:0039574; P:suppression by virus of host TYK2 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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; Clathrin-mediated endocytosis of virus by host;
Cleavage on pair of basic residues; 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 JAK1 by virus; Inhibition of host STAT1 by virus;
Inhibition of host STAT2 by virus; Inhibition of host TYK2 by virus;
Membrane; Metal-binding; Methyltransferase; mRNA capping;
mRNA processing; Multifunctional enzyme; Nucleotide-binding;
Nucleotidyltransferase; Phosphoprotein; Protease; RNA-binding;
RNA-directed RNA polymerase; S-adenosyl-L-methionine; Secreted;
Serine protease; Suppressor of RNA silencing; Transcription;
Transcription regulation; Transferase; Transmembrane;
Transmembrane helix; Viral attachment to host cell;
Viral envelope protein; Viral immunoevasion;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus endocytosis by host; Virus entry into host cell; Zinc.
CHAIN 1 3433 Genome polyprotein.
/FTId=PRO_0000405136.
CHAIN 1 105 Capsid protein C.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037703.
PROPEP 106 123 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000405137.
CHAIN 124 290 Protein prM.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000405138.
CHAIN 124 215 Peptide pr.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037704.
CHAIN 216 290 Small envelope protein M.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037705.
CHAIN 291 791 Envelope protein E.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037706.
CHAIN 792 1143 Non-structural protein 1.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037707.
CHAIN 1144 1374 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037708.
CHAIN 1375 1505 Serine protease subunit NS2B.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037709.
CHAIN 1506 2124 Serine protease NS3.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037710.
CHAIN 2125 2250 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037711.
PEPTIDE 2251 2273 Peptide 2k.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000405139.
CHAIN 2274 2528 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037712.
CHAIN 2529 3433 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037713.
TOPO_DOM 2 105 Cytoplasmic. {ECO:0000255}.
TRANSMEM 106 126 Helical. {ECO:0000255}.
TOPO_DOM 127 248 Extracellular. {ECO:0000255}.
TRANSMEM 249 269 Helical. {ECO:0000255}.
TOPO_DOM 270 273 Cytoplasmic. {ECO:0000255}.
TRANSMEM 274 290 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 1247 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1248 1268 Helical. {ECO:0000255}.
TOPO_DOM 1269 1288 Lumenal. {ECO:0000255}.
TRANSMEM 1289 1309 Helical. {ECO:0000255}.
TOPO_DOM 1310 1316 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1317 1335 Helical. {ECO:0000255}.
TOPO_DOM 1336 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 2273 Helical; Note=Signal for NS4B.
{ECO:0000305}.
TOPO_DOM 2274 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:0000250|UniProtKB:Q9Q6P4}.
MOTIF 1790 1793 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
COMPBIAS 281 284 Poly-Leu.
COMPBIAS 2678 2681 Poly-Ser.
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:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2674 2674 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2710 2710 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2746 2746 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2968 2968 Zinc 1. {ECO:0000269|PubMed:17287213}.
METAL 2972 2972 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:17287213}.
METAL 2977 2977 Zinc 1. {ECO:0000269|PubMed:17287213}.
METAL 2980 2980 Zinc 1. {ECO:0000269|PubMed:17287213}.
METAL 3245 3245 Zinc 2; via tele nitrogen.
{ECO:0000269|PubMed:17287213}.
METAL 3261 3261 Zinc 2. {ECO:0000269|PubMed:17287213}.
METAL 3380 3380 Zinc 2. {ECO:0000269|PubMed:17287213}.
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}.
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 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 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,
ECO:0000255}.
SITE 1505 1506 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P06935}.
SITE 1963 1963 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000269|PubMed:17658551}.
SITE 1966 1966 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000269|PubMed:17658551}.
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:0000255}.
SITE 2552 2552 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
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:0000269|PubMed:17376919}.
CARBOHYD 921 921 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:Q9Q6P4}.
CARBOHYD 966 966 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:Q9Q6P4}.
CARBOHYD 998 998 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 293 320 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 350 411 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 350 406 {ECO:0000250|UniProtKB:P06935}.
DISULFID 364 395 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 382 411 {ECO:0000250|UniProtKB:P06935}.
DISULFID 382 406 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 480 578 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 595 626 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 795 806 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 846 934 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 970 1014 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 1071 1120 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 1082 1103 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 1104 1107 {ECO:0000250|UniProtKB:Q9Q6P4}.
VARIANT 150 150 P -> T (in strain: Infectious clone pAKUN
and Infectious clone FLSDX).
VARIANT 820 820 I -> M (in strain: Infectious clone
pAKUNa and Infectious clone FLSDX).
VARIANT 943 943 N -> S (in strain: Infectious clone pAKUN
and Infectious clone FLSDX).
VARIANT 1041 1041 P -> L (in strain: Infectious clone pAKUN
and Infectious clone FLSDX).
VARIANT 1202 1202 I -> N (in strain: Infectious clone
pAKUN; blocks induction of virus-specific
membrane structures).
{ECO:0000269|PubMed:18337583}.
VARIANT 1318 1318 R -> K (in strain: Infectious clone
pAKUN).
VARIANT 1967 1967 T -> I (in strain: Infectious clone pAKUN
and Infectious clone FLSDX).
VARIANT 1974 1974 A -> V (in strain: Infectious clone pAKUN
and Infectious clone FLSDX).
VARIANT 2023 2023 Y -> H (in strain: Infectious clone
pAKUN).
VARIANT 2062 2062 S -> P (in strain: Infectious clone
pAKUN).
VARIANT 2339 2339 T -> N (in strain: Infectious clone pAKUN
and Infectious clone FLSDX).
MUTAGEN 1173 1173 A->P: No effect on viral RNA replication
and packaging; drastic increase in IFN-
alpha and IFN-beta host cell response.
{ECO:0000269|PubMed:15507609,
ECO:0000269|PubMed:16474146}.
MUTAGEN 1244 1244 N->D: 28% decrease in viral RNA
replication; decreased packaging
efficiency.
{ECO:0000269|PubMed:15507609}.
MUTAGEN 1292 1292 T->P: Restores induction of virus-
specific membrane structures; when
associated with N-1202.
{ECO:0000269|PubMed:18337583}.
MUTAGEN 2137 2137 P->A: Complete loss of viral replication.
{ECO:0000269|PubMed:25771497}.
MUTAGEN 2172 2172 P->A: Reduced membrane proliferation and
efficiency of replication; no effect on
replication complex formation.
{ECO:0000269|PubMed:25771497}.
MUTAGEN 2173 2173 D->A: Slightly reduced membrane
proliferation and efficiency of
replication at early time of infection;
no effect on replication complex
formation. {ECO:0000269|PubMed:25771497}.
MUTAGEN 2190 2190 G->A: Reduced membrane proliferation and
efficiency of replication; no effect on
replication complex formation.
{ECO:0000269|PubMed:25771497}.
MUTAGEN 2244 2244 P->A: Complete loss of viral replication.
{ECO:0000269|PubMed:21880777}.
MUTAGEN 2245 2245 E->A: Complete loss of viral replication.
{ECO:0000269|PubMed:21880777}.
MUTAGEN 2246 2246 P->A: 20% decrease in viral replication.
{ECO:0000269|PubMed:21880777}.
MUTAGEN 2247 2247 E->A: Complete loss of viral replication.
{ECO:0000269|PubMed:21880777}.
MUTAGEN 2798 2798 P->S: 88% decrease in viral RNA
replication; decreased packaging
efficiency.
{ECO:0000269|PubMed:15507609}.
MUTAGEN 3181 3181 S->F: Increases STAT1 inhibitory function
of NS5. {ECO:0000269|PubMed:20106931}.
HELIX 26 38 {ECO:0000244|PDB:1SFK}.
HELIX 44 56 {ECO:0000244|PDB:1SFK}.
HELIX 63 69 {ECO:0000244|PDB:1SFK}.
HELIX 74 95 {ECO:0000244|PDB:1SFK}.
STRAND 1694 1697 {ECO:0000244|PDB:2QEQ}.
TURN 1703 1708 {ECO:0000244|PDB:2QEQ}.
HELIX 1709 1719 {ECO:0000244|PDB:2QEQ}.
STRAND 1724 1730 {ECO:0000244|PDB:2QEQ}.
HELIX 1731 1740 {ECO:0000244|PDB:2QEQ}.
STRAND 1763 1767 {ECO:0000244|PDB:2QEQ}.
HELIX 1768 1776 {ECO:0000244|PDB:2QEQ}.
STRAND 1777 1779 {ECO:0000244|PDB:2QEQ}.
STRAND 1785 1791 {ECO:0000244|PDB:2QEQ}.
HELIX 1797 1811 {ECO:0000244|PDB:2QEQ}.
STRAND 1816 1820 {ECO:0000244|PDB:2QEQ}.
STRAND 1839 1842 {ECO:0000244|PDB:2QEQ}.
STRAND 1851 1853 {ECO:0000244|PDB:2QEQ}.
HELIX 1855 1859 {ECO:0000244|PDB:2QEQ}.
STRAND 1864 1867 {ECO:0000244|PDB:2QEQ}.
HELIX 1871 1883 {ECO:0000244|PDB:2QEQ}.
STRAND 1888 1891 {ECO:0000244|PDB:2QEQ}.
STRAND 1909 1914 {ECO:0000244|PDB:2QEQ}.
STRAND 1926 1930 {ECO:0000244|PDB:2QEQ}.
STRAND 1937 1944 {ECO:0000244|PDB:2QEQ}.
STRAND 1946 1949 {ECO:0000244|PDB:2QEQ}.
HELIX 1957 1964 {ECO:0000244|PDB:2QEQ}.
STRAND 1977 1980 {ECO:0000244|PDB:2QEQ}.
HELIX 1992 2002 {ECO:0000244|PDB:2QEQ}.
HELIX 2007 2009 {ECO:0000244|PDB:2QEQ}.
HELIX 2016 2021 {ECO:0000244|PDB:2QEQ}.
TURN 2026 2029 {ECO:0000244|PDB:2QEQ}.
HELIX 2034 2044 {ECO:0000244|PDB:2QEQ}.
HELIX 2050 2058 {ECO:0000244|PDB:2QEQ}.
HELIX 2066 2069 {ECO:0000244|PDB:2QEQ}.
HELIX 2074 2076 {ECO:0000244|PDB:2QEQ}.
STRAND 2079 2084 {ECO:0000244|PDB:2QEQ}.
STRAND 2086 2088 {ECO:0000244|PDB:2QEQ}.
STRAND 2094 2096 {ECO:0000244|PDB:2QEQ}.
STRAND 2100 2103 {ECO:0000244|PDB:2QEQ}.
HELIX 2104 2106 {ECO:0000244|PDB:2QEQ}.
HELIX 2110 2121 {ECO:0000244|PDB:2QEQ}.
HELIX 2808 2815 {ECO:0000244|PDB:2HFZ}.
TURN 2819 2821 {ECO:0000244|PDB:2HFZ}.
STRAND 2831 2840 {ECO:0000244|PDB:2HFZ}.
HELIX 2853 2857 {ECO:0000244|PDB:2HCN}.
HELIX 2860 2862 {ECO:0000244|PDB:2HCN}.
TURN 2870 2872 {ECO:0000244|PDB:2HFZ}.
HELIX 2878 2885 {ECO:0000244|PDB:2HFZ}.
HELIX 2898 2915 {ECO:0000244|PDB:2HCN}.
TURN 2916 2918 {ECO:0000244|PDB:2HCN}.
HELIX 2926 2934 {ECO:0000244|PDB:2HCN}.
HELIX 2951 2957 {ECO:0000244|PDB:2HCN}.
HELIX 2959 2974 {ECO:0000244|PDB:2HCN}.
HELIX 3004 3019 {ECO:0000244|PDB:2HCN}.
HELIX 3021 3024 {ECO:0000244|PDB:2HCN}.
TURN 3025 3028 {ECO:0000244|PDB:2HCN}.
HELIX 3030 3033 {ECO:0000244|PDB:2HCN}.
STRAND 3034 3036 {ECO:0000244|PDB:2HCN}.
HELIX 3042 3052 {ECO:0000244|PDB:2HCN}.
STRAND 3055 3058 {ECO:0000244|PDB:2HCN}.
STRAND 3065 3067 {ECO:0000244|PDB:2HCS}.
HELIX 3068 3070 {ECO:0000244|PDB:2HCN}.
HELIX 3074 3080 {ECO:0000244|PDB:2HCN}.
HELIX 3081 3086 {ECO:0000244|PDB:2HCN}.
HELIX 3089 3099 {ECO:0000244|PDB:2HCN}.
TURN 3100 3103 {ECO:0000244|PDB:2HCN}.
STRAND 3104 3113 {ECO:0000244|PDB:2HFZ}.
HELIX 3115 3117 {ECO:0000244|PDB:2HFZ}.
STRAND 3119 3128 {ECO:0000244|PDB:2HFZ}.
HELIX 3134 3156 {ECO:0000244|PDB:2HCN}.
STRAND 3164 3167 {ECO:0000244|PDB:2HCN}.
HELIX 3172 3188 {ECO:0000244|PDB:2HCN}.
STRAND 3191 3194 {ECO:0000244|PDB:2HCN}.
STRAND 3197 3200 {ECO:0000244|PDB:2HCN}.
HELIX 3205 3209 {ECO:0000244|PDB:2HCN}.
HELIX 3212 3216 {ECO:0000244|PDB:2HCN}.
TURN 3236 3238 {ECO:0000244|PDB:2HCN}.
STRAND 3244 3250 {ECO:0000244|PDB:2HCN}.
STRAND 3256 3261 {ECO:0000244|PDB:2HCN}.
HELIX 3264 3271 {ECO:0000244|PDB:2HCN}.
STRAND 3275 3278 {ECO:0000244|PDB:2HFZ}.
HELIX 3282 3298 {ECO:0000244|PDB:2HCN}.
HELIX 3303 3315 {ECO:0000244|PDB:2HCN}.
STRAND 3338 3340 {ECO:0000244|PDB:2HCN}.
HELIX 3342 3350 {ECO:0000244|PDB:2HCN}.
TURN 3351 3353 {ECO:0000244|PDB:2HCN}.
HELIX 3366 3368 {ECO:0000244|PDB:2HCN}.
HELIX 3374 3379 {ECO:0000244|PDB:2HCN}.
HELIX 3387 3394 {ECO:0000244|PDB:2HCN}.
HELIX 3396 3407 {ECO:0000244|PDB:2HCN}.
HELIX 3416 3418 {ECO:0000244|PDB:2HCN}.
SEQUENCE 3433 AA; 381369 MW; EE4B888A7D040B99 CRC64;
MSKKPGGPGK SRAVNMLKRG MPRVLSLTGL KRAMLSLIDG RGPTRFVLAL LAFFRFTAIA
PTRAVLDRWR SVNKQTAMKH LLSFKKELGT LTSAINRRSS KQKKRGGKTG IAFMIGLIAG
VGAVTLSNFQ GKVMMTVNAT DVTDIITIPP AAGKNLCIVR AMDVGHMCDD TITYECPVLS
AGNDPEDIDC WCTKLAVYVR YGRCTKTRHS RRSRRSLTVQ THGESTLSNK KGAWMDSTKA
TRYLVKTESW ILRNPGYALV AAVIGWMLGS NTMQRVVFAV LLLLVAPAYS FNCLGMSNRD
FLEGVSGATW VDLVLEGDSC VTIMSKDKPT IDVKMMNMEA ANLAEVRSYC YLATVSELST
KAACPTMGEA HNDKRADPSF VCKQGVVDRG WGNGCGLFGK GSIDTCAKFA CSTKATGRTI
LKENIKYEVA IFVHGPTTVE SHGNYFTQTG AAQAGRFSIT PAAPSYTLKL GEYGEVTVDC
EPRSGIDTSA YYVMTVGTKT FLVHREWFMD LNLPWSSAES NVWRNRETLM EFEEPHATKQ
SVIALGSQEG ALHQALAGAI PVEFSSNTVK LTSGHLKCRV KMEKLQLKGT TYGVCSKAFR
FLGTPADTGH GTVVLELQYT GTDGPCKIPI SSVASLNDLT PVGRLVTVNP FVSVSTANAK
VLIELEPPFG DSYIVVGRGE QQINHHWHKS GSSIGKAFTA TLKGAQRLAA LGDTAWDFGS
VGGVFTSVGK AVHQVFGGAF RSLFGGMSWI TQGLLGALLL WMGINARDRS IALTFLAVGG
VLLFLSVNVH ADTGCAIDIS RQELRCGSGV FIHNDVEAWI DRYKYYPETP QGLAKIIQKA
HKEGVCGLRS VSRLEHQMWE AVKDELNTLL KENGVDLSIV VEKQEGMYKS APRRLTATTE
KLEIGWKAWG KSILFAPELA NNTFVIDGPE TKECPTQNRA WNNLEVEDFG FGLTSTRMFL
RVRESNTTEC DSKIIGTAVK NNLAIHSDLS YWIESRFNDT WKLERAVLGE VKSCTWPETH
TLWGDGVLES DLIIPITLAG PRSNHNRRPG YKTQSQGPWD EGRVEIDFDY CPGTTVTLSE
SCGHRGPATR TTTESGKLIT DWCCRSCTLP PLRYQTDNGC WYGMEIRPQR HDEKTLVQSQ
VNAYNADMID PFQLGLLVVF LATQEVLRKR WTAKISMPAI LIALLVLVFG GITYTDVLRY
VILVGAAFAE SNSGGDVVHL ALMATFKIQP VFMVASFLKA RWTNQENILL MLAAAFFQMA
YYDARQILLW EMPDVLNSLA VAWMILRAIT FTTTSNVVVP LLALLTPGLR CLNLDVYRIL
LLMVGIGSLI REKRSAAAKK KGASLLCLAL ASTGFFNPMI LAAGLVACDP NRKRGWPATE
VMTAVGLMFA IVGGLAELDI DSMAIPMTIA GLMFAAFVIS GKSTDMWIER TADISWEGDA
EITGSSERVD VRLDDDGNFQ LMNDPGAPWK IWMLRMACLA ISAYTPWAIL PSVVGFWITL
QYTKRGGVLW DTPSPKEYKR GDTTTGVYRI MTRGLLGSYQ AGAGVMVEGV FHTLWHTTKG
AALMSGEGRL DPYWGSVKED RLCYGGPWKL QHKWNGQDEV QMIVVEPGKN VKNVQTKPGV
FKTPEGEIGA VTLDFPTGTS GSPIVDKNGD VIGLYGNGVI MPNGSYISAI VQGERMDEPV
PAGFEPEMLR KKQITVLDLH PGAGKTRRIL PQIIKEAINR RLRTAVLAPT RVVAAEMAEA
LRGLPIRYQT SAVAREHNGN EIVDVMCHAT LTHRLMSPHR VPNYNLFVMD EAHFTDPASI
AARGYISTRV ELGEAAAIFM TATPPGTSDP FPESNAPISD LQTEIPDRAW NSGYEWITEY
IGKTVWFVPS VKMGNEIALC LQRAGKKVIQ LNRKSYETEY PKCKNDDWDF VVTTDISEMG
ANFKASRVID SRKSVKPTII TEGEGRVILG EPSAVTAASA AQRRGRTGRN PSQAGDEYCY
GGHTNEDDSN CAHWTEARIM LDNINMPNGL IAQFYQPERE KVYTMDGEYR LRGEERKNFL
ELLRTADLPV WLAYKVAAAG VSYHDRRWCF DGPRTNTILE DNNEVEVITK LGERKILRPR
WIDARVYSDH QALKSFKDFA SGKRSQIGFI EVLGKMPEHF MGKTWEALDT MYVVATAEKG
GRAHRMALEE LPDALQTIAL IALLSVMTMG VFFLLMQRKG IGKIGLGGVV LGAATFFCWM
AEVPGTKIAG MLLLSLLLMI VLIPEPEKQR SQTDNQLAVF LICVLTLVGA VAANEMGWLD
KTKSDISGLF GQRIETKENF SIGEFLLDLR PATAWSLYAV TTAVLTPLLK HLITSDYITT
SLTSINVQAS ALFTLARGFP FVDVGVSALL LAAGCWGQVT LTVTVTSATL LFCHYAYMVP
GWQAEAMRSA QRRTAAGIMK NAVVDGIVAT DVPELERTTP IMQKKVGQVM LILVSLAALV
VNPSVKTVRE AGILITAAAV TLWENGASSV WNATTAIGLC HIMRGGWLSC LSITWTLVKN
MEKPGLKRGG AKGRTLGEVW KERLNQMTKE EFIRYRKEAI TEVDRSAAKH ARKERNITGG
HPVSRGTAKL RWLVERRFLE PVGKVIDLGC GRGGWCYYMA TQKRVQEVRG YTKGGPGHEE
PQLVQSYGWN IVTMKSGVDV FYRPSECCDT LLCDIGESSS SAEVEEHRTL RVLEMVEDWL
HRGPKEFCVK VLCPYMPKVI EKMELLQRRY GGGLVRNPLS RNSTHEMYWV SRASGNVVHS
VNMTSQVLLG RMEKKTWKGP QYEEDVNLGS GTRAVGKPLL NSDTSKIKNR IERLRREYSS
TWHHDENHPY RTWNYHGSYE VKPTGSASSL VNGVVRLLSK PWDTITNVTT MAMTDTTPFG
QQRVFKEKVD TKAPEPPEGV KYVLNETTNW LWAFLAREKR PRMCSREEFI RKVNSNAALG
AMFEEQNQWR SAREAVEDPK FWEMVDEERE AHLRGECHTC IYNMMGKREK KPGEFGKAKG
SRAIWFMWLG ARFLEFEALG FLNEDHWLGR KNSGGGVEGL GLQKLGYILR EVGTRPGGRI
YADDTAGWDT RITRADLENE AKVLELLDGE HRRLARAIIE LTYRHKVVKV MRPAADGRTV
MDVISREDQR GSGQVVTYAL NTFTNLAVQL VRMMEGEGVI GPDDVEKLTK GKGPKVRTWL
SENGEERLSR MAVSGDDCVV KPLDDRFATS LHFLNAMSKV RKDIQEWKPS TGWYDWQQVP
FCSNHFTELI MKDGRTLVTP CRGQDELVGR ARISPGAGWN VRDTACLAKS YAQMWLLLYF
HRRDLRLMAN AICSAVPVNW VPTGRTTWSI HAGGEWMTTE DMLEVWNRVW IEENEWMEDK
TPVEKWSDVP YSGKREDIWC GSLIGTRARA TWAENIQVAI NQVRSIIGDE KYVDYMSSLK
RYEDTTLVED TVL


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