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 POLG_WNV                Reviewed;        3430 AA.
P06935;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
24-OCT-2003, sequence version 2.
25-OCT-2017, entry version 174.
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:0000250|UniProtKB:Q9Q6P4};
EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9Q6P4};
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;
West Nile virus (WNV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; Japanese encephalitis virus group.
NCBI_TaxID=11082;
NCBI_TaxID=7158; Aedes.
NCBI_TaxID=34610; Amblyomma variegatum (Tropical bont tick).
NCBI_TaxID=8782; Aves.
NCBI_TaxID=53527; Culex.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=34627; Hyalomma marginatum.
NCBI_TaxID=308735; Mansonia uniformis.
NCBI_TaxID=308737; Mimomyia.
NCBI_TaxID=34630; Rhipicephalus.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3753811; DOI=10.1016/0042-6822(86)90082-6;
Castle E., Leidner U., Nowak T., Wengler G., Wengler G.;
"Primary structure of the West Nile flavivirus genome region coding
for all nonstructural proteins.";
Virology 149:10-26(1986).
[2]
SEQUENCE REVISION TO 1908; 2018-2036; 2242 AND 2859-2860.
PubMed=11277701; DOI=10.1006/viro.2000.0795;
Yamshchikov V.F., Wengler G., Perelygin A.A., Brinton M.A.,
Compans R.W.;
"An infectious clone of the West Nile flavivirus.";
Virology 281:294-304(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-291.
PubMed=2992152; DOI=10.1016/0042-6822(85)90156-4;
Castle E., Nowak T., Leidner U., Wengler G., Wengler G.;
"Sequence analysis of the viral core protein and the membrane-
associated proteins V1 and NV2 of the flavivirus West Nile virus and
of the genome sequence for these proteins.";
Virology 145:227-236(1985).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 255-854.
PubMed=3855247; DOI=10.1016/0042-6822(85)90129-1;
Wengler G., Castle E., Leidner U., Nowak T., Wengler G.;
"Sequence analysis of the membrane protein V3 of the flavivirus West
Nile virus and of its gene.";
Virology 147:264-274(1985).
[5]
ABSENCE OF GLYCOSYLATION (ENVELOPE PROTEIN E).
PubMed=2441520;
Winkler G., Heinz F.X., Kunz C.;
"Studies on the glycosylation of flavivirus E proteins and the role of
carbohydrate in antigenic structure.";
Virology 159:237-243(1987).
[6]
DISULFIDE BONDS (ENVELOPE PROTEIN E).
PubMed=3811228; DOI=10.1016/0042-6822(87)90443-0;
Nowak T., Wengler G.;
"Analysis of disulfides present in the membrane proteins of the West
Nile flavivirus.";
Virology 156:127-137(1987).
[7]
FUNCTION (ENVELOPE PROTEIN E).
PubMed=15367621; DOI=10.1128/JVI.78.19.10543-10555.2004;
Chu J.J., Ng M.L.;
"Infectious entry of West Nile virus occurs through a clathrin-
mediated endocytic pathway.";
J. Virol. 78:10543-10555(2004).
[8]
SUBCELLULAR LOCATION (RNA-DIRECTED RNA POLYMERASE NS5).
STRAIN=E101;
PubMed=16699025; DOI=10.1128/JVI.01982-05;
Uchil P.D., Kumar A.V., Satchidanandam V.;
"Nuclear localization of flavivirus RNA synthesis in infected cells.";
J. Virol. 80:5451-5464(2006).
[9]
FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), AND MUTAGENESIS OF
LYS-2586; ASP-2671; LYS-2707 AND GLU-2743.
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).
[10]
PROTEOLYTIC PROCESSING (GENOME POLYPROTEIN).
PubMed=17067286; DOI=10.1042/BJ20061136;
Shiryaev S.A., Kozlov I.A., Ratnikov B.I., Smith J.W., Lebl M.,
Strongin A.Y.;
"Cleavage preference distinguishes the two-component NS2B-NS3 serine
proteinases of Dengue and West Nile viruses.";
Biochem. J. 401:743-752(2007).
[11]
INTERACTION WITH HUMAN EXOC1 (CAPSID PROTEIN C), AND SUBCELLULAR
LOCATION (CAPSID PROTEIN C).
PubMed=19889084; DOI=10.1111/j.1462-5822.2009.01407.x;
Bhuvanakantham R., Li J., Tan T.T., Ng M.L.;
"Human Sec3 protein is a novel transcriptional and translational
repressor of flavivirus.";
Cell. Microbiol. 12:453-472(2010).
[12]
INTERACTION WITH HUMAN EXOC1 (CAPSID PROTEIN C), FUNCTION (CAPSID
PROTEIN C), AND MUTAGENESIS OF VAL-14.
PubMed=23522008; DOI=10.1111/cmi.12143;
Bhuvanakantham R., Ng M.L.;
"West Nile virus and dengue virus capsid protein negates the antiviral
activity of human Sec3 protein through the proteasome pathway.";
Cell. Microbiol. 15:1688-1706(2013).
[13]
X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 1420-1688.
PubMed=16532006; DOI=10.1038/nsmb1073;
Erbel P., Schiering N., D'Arcy A., Renatus M., Kroemer M., Lim S.P.,
Yin Z., Keller T.H., Vasudevan S.G., Hommel U.;
"Structural basis for the activation of flaviviral NS3 proteases from
dengue and West Nile virus.";
Nat. Struct. Mol. Biol. 13:372-373(2006).
[14]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1419-1679.
PubMed=17400917; DOI=10.1110/ps.072753207;
Aleshin A.E., Shiryaev S.A., Strongin A.Y., Liddington R.C.;
"Structural evidence for regulation and specificity of flaviviral
proteases and evolution of the Flaviviridae fold.";
Protein Sci. 16:795-806(2007).
[15]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 291-688.
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).
-!- 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 (By
similarity). During virus entry, may induce genome penetration
into the host cytoplasm after hemifusion induced by the surface
proteins (By similarity). Can migrate to the cell nucleus where it
modulates host functions (By similarity). Overcomes the anti-viral
effects of host EXOC1 by sequestering and degrading the latter
through the proteasome degradation pathway (PubMed:23522008).
{ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:23522008}.
-!- 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
(PubMed:15367621). Envelope protein is synthesized in the
endoplasmic reticulum in the form of heterodimer with protein prM
(By similarity). They play a role in virion budding in the ER, and
the newly formed immature particule is covered with 60 spikes
composed of heterodimer between precursor prM and envelope protein
E (By similarity). The virion is transported to the Golgi
apparatus where the low pH causes dissociation of PrM-E
heterodimers and formation of E homodimers (By similarity). prM-E
cleavage is inefficient, and many virions are only partially
matured (By similarity). These uncleaved prM would play a role in
immune evasion (By similarity). {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.
{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}.
-!- FUNCTION: Non-structural protein 4A: Regulates the ATPase activity
of the NS3 helicase activity. NS4A allows NS3 helicase to conserve
energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}.
-!- 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.
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.
Inhibits STAT2 translocation in the nucleus after IFN-alpha
treatment. {ECO:0000250|UniProtKB:Q9Q6P4}.
-!- FUNCTION: RNA-directed RNA polymerase NS5: Replicates the viral
(+) and (-) RNA genome, and performs the capping of genomes in the
cytoplasm (PubMed:17267492). NS5 methylates viral RNA cap at
guanine N-7 and ribose 2'-O positions (PubMed:17267492). Besides
its role in RNA genome replication, also prevents the
establishment of cellular antiviral state by blocking the
interferon-alpha/beta (IFN-alpha/beta) signaling pathway (By
similarity). Inhibits host TYK2 and STAT2 phosphorylation, thereby
preventing activation of JAK-STAT signaling pathway (By
similarity). {ECO:0000250|UniProtKB:Q9Q6P4,
ECO:0000269|PubMed:17267492}.
-!- 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:0000250|UniProtKB:Q9Q6P4}.
-!- 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 (By similarity). Interacts
(via N-terminus) with host EXOC1 (via C-terminus)
(PubMed:19889084, PubMed:23522008); this interaction results in
EXOC1 degradation through the proteasome degradation pathway
(PubMed:23522008). 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. 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.
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:19889084, ECO:0000269|PubMed:23522008}.
-!- INTERACTION:
Q17NZ6:CTLMA15 (xeno); NbExp=5; IntAct=EBI-2912469, EBI-2912457;
P05106:ITGB3 (xeno); NbExp=4; IntAct=EBI-981051, EBI-702847;
-!- SUBCELLULAR LOCATION: Capsid protein C: Virion
{ECO:0000250|UniProtKB:P17763}. Host nucleus
{ECO:0000250|UniProtKB:P17763}. Host cytoplasm
{ECO:0000269|PubMed:19889084}. Host cytoplasm, host perinuclear
region {ECO:0000269|PubMed:19889084}.
-!- 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: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: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:0000250|UniProtKB:P14335}; 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 {ECO:0000250|UniProtKB:P17763}. Host nucleus
{ECO:0000269|PubMed:16699025}. 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, ECO:0000269|PubMed:17067286}.
-!- 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: Not N-glycosylated.
{ECO:0000269|PubMed:2441520}.
-!- 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; M12294; AAA48498.2; -; Genomic_RNA.
PIR; A25256; GNWVWV.
RefSeq; NP_041724.2; NC_001563.2.
PDB; 2FP7; X-ray; 1.68 A; A=1420-1466, B=1517-1688.
PDB; 2G05; Model; -; D=1675-2120.
PDB; 2G2G; Model; -; D=1675-2120.
PDB; 2GGV; X-ray; 1.80 A; A=1419-1525, B=1503-1679.
PDB; 2IJO; X-ray; 2.30 A; A=1419-1482, B=1502-1685.
PDB; 2P5P; X-ray; 2.80 A; A/B/C=585-701.
PDB; 2YOL; X-ray; 3.20 A; A=1420-1465, A=1502-1671.
PDB; 3E90; X-ray; 2.45 A; A/C=1420-1463, B/D=1502-1685.
PDB; 3I50; X-ray; 3.00 A; E=291-688.
PDB; 5IDK; X-ray; 1.50 A; A/B/C=1420-1465.
PDBsum; 2FP7; -.
PDBsum; 2G05; -.
PDBsum; 2G2G; -.
PDBsum; 2GGV; -.
PDBsum; 2IJO; -.
PDBsum; 2P5P; -.
PDBsum; 2YOL; -.
PDBsum; 3E90; -.
PDBsum; 3I50; -.
PDBsum; 5IDK; -.
DisProt; DP00673; -.
ProteinModelPortal; P06935; -.
SMR; P06935; -.
IntAct; P06935; 4.
BindingDB; P06935; -.
ChEMBL; CHEMBL5419; -.
MEROPS; S07.003; -.
GeneID; 912267; -.
KEGG; vg:912267; -.
OrthoDB; VOG09000016; -.
BRENDA; 2.7.7.48; 6687.
BRENDA; 3.4.21.91; 6687.
EvolutionaryTrace; P06935; -.
PRO; PR:P06935; -.
Proteomes; UP000008600; Genome.
GO; GO:0039714; C:cytoplasmic viral factory; IDA:UniProtKB.
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:0032993; C:protein-DNA complex; IMP:CAFA.
GO; GO:1990904; C:ribonucleoprotein complex; IMP:CAFA.
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:0003677; F:DNA binding; IMP:CAFA.
GO; GO:1990814; F:DNA/DNA annealing activity; IMP:CAFA.
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; IDA:UniProtKB.
GO; GO:0008233; F:peptidase activity; IDA:CACAO.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IMP:CAFA.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0033592; F:RNA strand annealing activity; IMP:CAFA.
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; IDA:UniProtKB.
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:0045070; P:positive regulation of viral genome replication; IMP:CACAO.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0106005; P:RNA 5'-cap (guanine-N7)-methylation; IDA:UniProtKB.
GO; GO:0043489; P:RNA stabilization; IMP:CAFA.
GO; GO:0019050; P:suppression by virus of host apoptotic process; IDA:CACAO.
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; IEA:UniProtKB-KW.
GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
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.
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 3430 Genome polyprotein.
/FTId=PRO_0000441418.
CHAIN 1 105 Capsid protein C.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037743.
PROPEP 106 123 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037744.
CHAIN 124 290 Protein prM.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000405150.
CHAIN 124 215 Peptide pr.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000405151.
CHAIN 216 290 Small envelope protein M.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037745.
CHAIN 291 787 Envelope protein E.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037746.
CHAIN 788 1139 Non-structural protein 1.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037747.
CHAIN 1140 1370 Non-structural protein 2A.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037748.
CHAIN 1371 1501 Serine protease subunit NS2B.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037749.
CHAIN 1502 2120 Serine protease NS3.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037750.
CHAIN 2121 2246 Non-structural protein 4A.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037751.
PEPTIDE 2247 2269 Peptide 2k.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000405152.
CHAIN 2270 2525 Non-structural protein 4B.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037752.
CHAIN 2526 3430 RNA-directed RNA polymerase NS5.
{ECO:0000269|PubMed:17067286}.
/FTId=PRO_0000037753.
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 270 275 Cytoplasmic. {ECO:0000255}.
TRANSMEM 276 290 Helical. {ECO:0000305}.
TOPO_DOM 291 739 Extracellular. {ECO:0000255}.
TRANSMEM 740 760 Helical. {ECO:0000255}.
TOPO_DOM 761 766 Cytoplasmic. {ECO:0000255}.
TRANSMEM 767 787 Helical. {ECO:0000255}.
TOPO_DOM 788 1212 Extracellular. {ECO:0000255}.
TRANSMEM 1213 1233 Helical. {ECO:0000255}.
TOPO_DOM 1234 1243 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1244 1264 Helical. {ECO:0000255}.
TOPO_DOM 1265 1278 Lumenal. {ECO:0000255}.
TRANSMEM 1279 1299 Helical. {ECO:0000255}.
TOPO_DOM 1300 1307 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1308 1328 Helical. {ECO:0000255}.
TOPO_DOM 1329 1340 Lumenal. {ECO:0000255}.
TRANSMEM 1341 1361 Helical. {ECO:0000255}.
TOPO_DOM 1362 1371 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1372 1392 Helical. {ECO:0000255}.
TOPO_DOM 1393 1395 Lumenal. {ECO:0000255}.
TRANSMEM 1396 1416 Helical. {ECO:0000255}.
TOPO_DOM 1417 1473 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1474 1494 Helical. {ECO:0000255}.
TOPO_DOM 1495 2170 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2171 2191 Helical. {ECO:0000255}.
TOPO_DOM 2192 2196 Lumenal. {ECO:0000255}.
INTRAMEM 2197 2217 Helical. {ECO:0000255}.
TOPO_DOM 2218 2218 Lumenal. {ECO:0000255}.
TRANSMEM 2219 2239 Helical. {ECO:0000255}.
TOPO_DOM 2240 2254 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2255 2275 Helical; Note=Signal for NS4B.
{ECO:0000255}.
TOPO_DOM 2276 2309 Lumenal. {ECO:0000255}.
INTRAMEM 2310 2330 Helical. {ECO:0000255}.
TOPO_DOM 2331 2377 Lumenal. {ECO:0000255}.
TRANSMEM 2378 2398 Helical. {ECO:0000255}.
TOPO_DOM 2399 2441 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2442 2462 Helical. {ECO:0000255}.
TOPO_DOM 2463 2467 Lumenal. {ECO:0000255}.
TRANSMEM 2468 2488 Helical. {ECO:0000255}.
TOPO_DOM 2489 3430 Cytoplasmic. {ECO:0000255}.
DOMAIN 1502 1679 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1682 1838 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1849 2014 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2526 2791 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3055 3207 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1695 1702 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 2 15 Interaction with host EXOC1.
{ECO:0000269|PubMed:19889084}.
REGION 37 72 Hydrophobic; homodimerization of capsid
protein C.
{ECO:0000250|UniProtKB:P29990}.
REGION 388 401 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
REGION 1424 1463 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
REGION 1686 1689 Important for RNA-binding.
{ECO:0000250|UniProtKB:P14340}.
REGION 2165 2169 Regulates the ATPase activity of NS3
helicase. {ECO:0000250|UniProtKB:Q9Q6P4}.
MOTIF 1786 1789 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
COMPBIAS 281 284 Poly-Leu.
COMPBIAS 2675 2678 Poly-Ser.
ACT_SITE 1552 1552 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1576 1576 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1636 1636 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 2586 2586 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2671 2671 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2707 2707 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2743 2743 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2965 2965 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 2969 2969 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:P14335}.
METAL 2974 2974 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 2977 2977 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 3242 3242 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:P14335}.
METAL 3258 3258 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
METAL 3377 3377 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
BINDING 2538 2538 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2541 2541 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2542 2542 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2544 2544 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2553 2553 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2581 2581 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2611 2611 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2612 2612 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2629 2629 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2630 2630 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2656 2656 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2657 2657 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2675 2675 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2738 2738 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2740 2740 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2745 2745 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 105 106 Cleavage; by viral protease NS3.
{ECO:0000269|PubMed:17067286}.
SITE 123 124 Cleavage; by host signal peptidase.
{ECO:0000269|PubMed:17067286}.
SITE 215 216 Cleavage; by host furin.
{ECO:0000303|PubMed:17067286}.
SITE 290 291 Cleavage; by host signal peptidase.
{ECO:0000303|PubMed:17067286}.
SITE 787 788 Cleavage; by host signal peptidase.
{ECO:0000303|PubMed:17067286}.
SITE 1139 1140 Cleavage; by host.
{ECO:0000303|PubMed:17067286}.
SITE 1370 1371 Cleavage; by viral protease NS3.
{ECO:0000269|PubMed:17067286}.
SITE 1501 1502 Cleavage; by autolysis.
{ECO:0000269|PubMed:17067286}.
SITE 1959 1959 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 1962 1962 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 2120 2121 Cleavage; by autolysis.
{ECO:0000303|PubMed:17067286}.
SITE 2246 2247 Cleavage; by viral protease NS3.
{ECO:0000303|PubMed:17067286}.
SITE 2269 2270 Cleavage; by host signal peptidase.
{ECO:0000303|PubMed:17067286}.
SITE 2525 2526 Cleavage; by viral protease NS3.
{ECO:0000269|PubMed:17067286}.
SITE 2549 2549 mRNA cap binding.
{ECO:0000269|PubMed:17067286}.
SITE 2586 2586 Essential for 2'-O-methyltransferase
activity.
SITE 2671 2671 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
SITE 2672 2672 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2707 2707 Essential for 2'-O-methyltransferase
activity.
SITE 2743 2743 Essential for 2'-O-methyltransferase
activity.
MOD_RES 2581 2581 Phosphoserine.
{ECO:0000250|UniProtKB:P03314}.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:P14335}.
CARBOHYD 917 917 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:Q9Q6P4}.
CARBOHYD 962 962 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:Q9Q6P4}.
CARBOHYD 994 994 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 293 320 {ECO:0000269|PubMed:3811228}.
DISULFID 350 411 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 350 406 {ECO:0000269|PubMed:3811228}.
DISULFID 364 395 {ECO:0000269|PubMed:3811228}.
DISULFID 382 411 {ECO:0000269|PubMed:3811228}.
DISULFID 382 406 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 476 574 {ECO:0000269|PubMed:3811228}.
DISULFID 591 622 {ECO:0000269|PubMed:3811228}.
DISULFID 791 802 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 842 930 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 966 1010 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 1067 1116 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 1078 1099 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 1100 1103 {ECO:0000250|UniProtKB:Q9Q6P4}.
MUTAGEN 14 14 V->A: Loss of interaction between capsid
protein C and host EXOC1.
{ECO:0000269|PubMed:23522008}.
MUTAGEN 2586 2586 K->A: Complete loss of 2'-O-
methyltransferase activity. No effect on
N-7 methyltransferase activity.
{ECO:0000269|PubMed:17267492}.
MUTAGEN 2671 2671 D->A: Lethal for the virus. Complete loss
of 2'-O and N-7 methyltransferase
activies. {ECO:0000269|PubMed:17267492}.
MUTAGEN 2707 2707 K->A: Complete loss of 2'-O-
methyltransferase activity. No effect on
N-7 methyltransferase activity.
{ECO:0000269|PubMed:17267492}.
MUTAGEN 2743 2743 E->A: Complete loss of 2'-O-
methyltransferase activity. No effect on
N-7 methyltransferase activity.
{ECO:0000269|PubMed:17267492}.
STRAND 595 603 {ECO:0000244|PDB:2P5P}.
STRAND 605 607 {ECO:0000244|PDB:2P5P}.
STRAND 609 615 {ECO:0000244|PDB:2P5P}.
STRAND 621 623 {ECO:0000244|PDB:2P5P}.
STRAND 626 631 {ECO:0000244|PDB:2P5P}.
STRAND 634 637 {ECO:0000244|PDB:2P5P}.
STRAND 639 643 {ECO:0000244|PDB:2P5P}.
STRAND 657 662 {ECO:0000244|PDB:2P5P}.
STRAND 665 673 {ECO:0000244|PDB:2P5P}.
STRAND 679 685 {ECO:0000244|PDB:2P5P}.
STRAND 1422 1428 {ECO:0000244|PDB:5IDK}.
HELIX 1434 1439 {ECO:0000244|PDB:2GGV}.
STRAND 1440 1443 {ECO:0000244|PDB:2GGV}.
STRAND 1444 1449 {ECO:0000244|PDB:5IDK}.
STRAND 1451 1453 {ECO:0000244|PDB:2YOL}.
STRAND 1455 1457 {ECO:0000244|PDB:5IDK}.
STRAND 1503 1505 {ECO:0000244|PDB:5IDK}.
STRAND 1521 1532 {ECO:0000244|PDB:5IDK}.
STRAND 1534 1543 {ECO:0000244|PDB:5IDK}.
STRAND 1546 1549 {ECO:0000244|PDB:5IDK}.
HELIX 1551 1554 {ECO:0000244|PDB:5IDK}.
STRAND 1559 1561 {ECO:0000244|PDB:5IDK}.
STRAND 1564 1566 {ECO:0000244|PDB:5IDK}.
STRAND 1568 1572 {ECO:0000244|PDB:5IDK}.
TURN 1573 1576 {ECO:0000244|PDB:5IDK}.
STRAND 1577 1583 {ECO:0000244|PDB:5IDK}.
STRAND 1592 1594 {ECO:0000244|PDB:5IDK}.
STRAND 1596 1600 {ECO:0000244|PDB:5IDK}.
STRAND 1608 1612 {ECO:0000244|PDB:5IDK}.
STRAND 1615 1618 {ECO:0000244|PDB:5IDK}.
STRAND 1623 1627 {ECO:0000244|PDB:5IDK}.
HELIX 1633 1635 {ECO:0000244|PDB:2FP7}.
STRAND 1639 1641 {ECO:0000244|PDB:5IDK}.
STRAND 1647 1650 {ECO:0000244|PDB:5IDK}.
STRAND 1654 1656 {ECO:0000244|PDB:5IDK}.
STRAND 1662 1665 {ECO:0000244|PDB:5IDK}.
STRAND 1672 1674 {ECO:0000244|PDB:2IJO}.
SEQUENCE 3430 AA; 380110 MW; 42D71B7CB12DC45B CRC64;
MSKKPGGPGK NRAVNMLKRG MPRGLSLIGL KRAMLSLIDG KGPIRFVLAL LAFFRFTAIA
PTRAVLDRWR GVNKQTAMKH LLSFKKELGT LTSAINRRST KQKKRGGTAG FTILLGLIAC
AGAVTLSNFQ GKVMMTVNAT DVTDVITIPT AAGKNLCIVR AMDVGYLCED TITYECPVLA
AGNDPEDIDC WCTKSSVYVR YGRCTKTRHS RRSRRSLTVQ THGESTLANK KGAWLDSTKA
TRYLVKTESW ILRNPGYALV AAVIGWMLGS NTMQRVVFAI LLLLVAPAYS FNCLGMSNRD
FLEGVSGATW VDLVLEGDSC VTIMSKDKPT IDVKMMNMEA ANLADVRSYC YLASVSDLST
RAACPTMGEA HNEKRADPAF VCKQGVVDRG WGNGCGLFGK GSIDTCAKFA CTTKATGWII
QKENIKYEVA IFVHGPTTVE SHGKIGATQA GRFSITPSAP SYTLKLGEYG EVTVDCEPRS
GIDTSAYYVM SVGEKSFLVH REWFMDLNLP WSSAGSTTWR NRETLMEFEE PHATKQSVVA
LGSQEGALHQ ALAGAIPVEF SSNTVKLTSG HLKCRVKMEK LQLKGTTYGV CSKAFKFART
PADTGHGTVV LELQYTGTDG PCKVPISSVA SLNDLTPVGR LVTVNPFVSV ATANSKVLIE
LEPPFGDSYI VVGRGEQQIN HHWHKSGSSI GKAFTTTLRG AQRLAALGDT AWDFGSVGGV
FTSVGKAIHQ VFGGAFRSLF GGMSWITQGL LGALLLWMGI NARDRSIAMT FLAVGGVLLF
LSVNVHADTG CAIDIGRQEL RCGSGVFIHN DVEAWMDRYK FYPETPQGLA KIIQKAHAEG
VCGLRSVSRL EHQMWEAIKD ELNTLLKENG VDLSVVVEKQ NGMYKAAPKR LAATTEKLEM
GWKAWGKSII FAPELANNTF VIDGPETEEC PTANRAWNSM EVEDFGFGLT STRMFLRIRE
TNTTECDSKI IGTAVKNNMA VHSDLSYWIE SGLNDTWKLE RAVLGEVKSC TWPETHTLWG
DGVLESDLII PITLAGPRSN HNRRPGYKTQ NQGPWDEGRV EIDFDYCPGT TVTISDSCEH
RGPAARTTTE SGKLITDWCC RSCTLPPLRF QTENGCWYGM EIRPTRHDEK TLVQSRVNAY
NADMIDPFQL GLMVVFLATQ EVLRKRWTAK ISIPAIMLAL LVLVFGGITY TDVLRYVILV
GAAFAEANSG GDVVHLALMA TFKIQPVFLV ASFLKARWTN QESILLMLAA AFFQMAYYDA
KNVLSWEVPD VLNSLSVAWM ILRAISFTNT SNVVVPLLAL LTPGLKCLNL DVYRILLLMV
GVGSLIKEKR SSAAKKKGAC LICLALASTG VFNPMILAAG LMACDPNRKR GWPATEVMTA
VGLMFAIVGG LAELDIDSMA IPMTIAGLMF AAFVISGKST DMWIERTADI TWESDAEITG
SSERVDVRLD DDGNFQLMND PGAPWKIWML RMACLAISAY TPWAILPSVI GFWITLQYTK
RGGVLWDTPS PKEYKKGDTT TGVYRIMTRG LLGSYQAGAG VMVEGVFHTL WHTTKGAALM
SGEGRLDPYW GSVKEDRLCY GGPWKLQHKW NGHDEVQMIV VEPGKNVKNV QTKPGVFKTP
EGEIGAVTLD YPTGTSGSPI VDKNGDVIGL YGNGVIMPNG SYISAIVQGE RMEEPAPAGF
EPEMLRKKQI TVLDLHPGAG KTRKILPQII KEAINKRLRT AVLAPTRVVA AEMSEALRGL
PIRYQTSAVH REHSGNEIVD VMCHATLTHR LMSPHRVPNY NLFIMDEAHF TDPASIAARG
YIATKVELGE AAAIFMTATP PGTSDPFPES NAPISDMQTE IPDRAWNTGY EWITEYVGKT
VWFVPSVKMG NEIALCLQRA GKKVIQLNRK SYETEYPKCK NDDWDFVITT DISEMGANFK
ASRVIDSRKS VKPTIIEEGD GRVILGEPSA ITAASAAQRR GRIGRNPSQV GDEYCYGGHT
NEDDSNFAHW TEARIMLDNI NMPNGLVAQL YQPEREKVYT MDGEYRLRGE ERKNFLEFLR
TADLPVWLAY KVAAAGISYH DRKWCFDGPR TNTILEDNNE VEVITKLGER KILRPRWADA
RVYSDHQALK SFKDFASGKR SQIGLVEVLG RMPEHFMVKT WEALDTMYVV ATAEKGGRAH
RMALEELPDA LQTIVLIALL SVMSLGVFFL LMQRKGIGKI GLGGVILGAA TFFCWMAEVP
GTKIAGMLLL SLLLMIVLIP EPEKQRSQTD NQLAVFLICV LTLVGAVAAN EMGWLDKTKN
DIGSLLGHRP EARETTLGVE SFLLDLRPAT AWSLYAVTTA VLTPLLKHLI TSDYINTSLT
SINVQASALF TLARGFPFVD VGVSALLLAV GCWGQVTLTV TVTAAALLFC HYAYMVPGWQ
AEAMRSAQRR TAAGIMKNVV VDGIVATDVP ELERTTPVMQ KKVGQIILIL VSMAAVVVNP
SVRTVREAGI LTTAAAVTLW ENGASSVWNA TTAIGLCHIM RGGWLSCLSI MWTLIKNMEK
PGLKRGGAKG RTLGEVWKER LNHMTKEEFT RYRKEAITEV DRSAAKHARR EGNITGGHPV
SRGTAKLRWL VERRFLEPVG KVVDLGCGRG GWCYYMATQK RVQEVKGYTK GGPGHEEPQL
VQSYGWNIVT MKSGVDVFYR PSEASDTLLC DIGESSSSAE VEEHRTVRVL EMVEDWLHRG
PKEFCIKVLC PYMPKVIEKM ETLQRRYGGG LIRNPLSRNS THEMYWVSHA SGNIVHSVNM
TSQVLLGRME KKTWKGPQFE EDVNLGSGTR AVGKPLLNSD TSKIKNRIER LKKEYSSTWH
QDANHPYRTW NYHGSYEVKP TGSASSLVNG VVRLLSKPWD TITNVTTMAM TDTTPFGQQR
VFKEKVDTKA PEPPEGVKYV LNETTNWLWA FLARDKKPRM CSREEFIGKV NSNAALGAMF
EEQNQWKNAR EAVEDPKFWE MVDEEREAHL RGECNTCIYN MMGKREKKPG EFGKAKGSRA
IWFMWLGARF LEFEALGFLN EDHWLGRKNS GGGVEGLGLQ KLGYILKEVG TKPGGKVYAD
DTAGWDTRIT KADLENEAKV LELLDGEHRR LARSIIELTY RHKVVKVMRP AADGKTVMDV
ISREDQRGSG QVVTYALNTF TNLAVQLVRM MEGEGVIGPD DVEKLGKGKG PKVRTWLFEN
GEERLSRMAV SGDDCVVKPL DDRFATSLHF LNAMSKVRKD IQEWKPSTGW YDWQQVPFCS
NHFTELIMKD GRTLVVPCRG QDELIGRARI SPGAGWNVRD TACLAKSYAQ MWLLLYFHRR
DLRLMANAIC SAVPANWVPT GRTTWSIHAK GEWMTTEDML AVWNRVWIEE NEWMEDKTPV
ERWSDVPYSG KREDIWCGSL IGTRTRATWA ENIHVAINQV RSVIGEEKYV DYMSSLRRYE
DTIVVEDTVL


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