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Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease syssubunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (NS5)]

 POLG_ZIKVF              Reviewed;        3423 AA.
A0A024B7W1;
31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
09-JUL-2014, sequence version 1.
18-JUL-2018, entry version 38.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Capsid protein C {ECO:0000250|UniProtKB:P17763};
AltName: Full=Capsid protein;
AltName: Full=Core protein;
Contains:
RecName: Full=Protein prM {ECO:0000250|UniProtKB:P17763};
AltName: Full=Precursor membrane protein;
Contains:
RecName: Full=Peptide pr {ECO:0000250|UniProtKB:P17763};
AltName: Full=Peptide precursor;
Contains:
RecName: Full=Small envelope protein M {ECO:0000250|UniProtKB:P17763};
AltName: Full=Matrix protein;
Contains:
RecName: Full=Envelope protein E {ECO:0000250|UniProtKB:P17763};
Contains:
RecName: Full=Non-structural protein 1 {ECO:0000250|UniProtKB:P17763};
Short=NS1;
Contains:
RecName: Full=Non-structural protein 2A {ECO:0000250|UniProtKB:P17763};
Short=NS2A;
Contains:
RecName: Full=Serine protease syssubunit NS2B {ECO:0000250|UniProtKB:P17763};
AltName: Full=Flavivirin protease NS2B regulatory subunit;
AltName: Full=Non-structural protein 2B;
Contains:
RecName: Full=Serine protease NS3 {ECO:0000250|UniProtKB:P17763};
EC=3.4.21.91;
EC=3.6.1.15;
EC=3.6.4.13;
AltName: Full=Flavivirin protease NS3 catalytic subunit;
AltName: Full=Non-structural protein 3;
Contains:
RecName: Full=Non-structural protein 4A {ECO:0000250|UniProtKB:P17763};
Short=NS4A;
Contains:
RecName: Full=Peptide 2k {ECO:0000250|UniProtKB:P17763};
Contains:
RecName: Full=Non-structural protein 4B {ECO:0000250|UniProtKB:P17763};
Short=NS4B;
Contains:
RecName: Full=RNA-directed RNA polymerase NS5 {ECO:0000250|UniProtKB:P17763};
EC=2.1.1.56;
EC=2.1.1.57;
EC=2.7.7.48;
AltName: Full=NS5;
Zika virus (isolate ZIKV/Human/French Polynesia/10087PF/2013) (ZIKV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus.
NCBI_TaxID=2043570;
NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=24903869; DOI=10.1128/genomeA.00500-14;
Baronti C., Piorkowski G., Charrel R.N., Boubis L., Leparc-Goffart I.,
de Lamballerie X.;
"Complete coding sequence of zika virus from a French polynesia
outbreak in 2013.";
Genome Announc. 2:0-0(2014).
[2]
INTERACTION WITH HOST TYRO3 (ENVELOPE PROTEIN E), INTERACTION WITH
HOST AXL (ENVELOPE PROTEIN E), AND INTERACTION WITH HOST DC SIGN
(ENVELOPE PROTEIN E).
PubMed=26085147; DOI=10.1128/JVI.00354-15;
Hamel R., Dejarnac O., Wichit S., Ekchariyawat P., Neyret A.,
Luplertlop N., Perera-Lecoin M., Surasombatpattana P., Talignani L.,
Thomas F., Cao-Lormeau V.M., Choumet V., Briant L., Despres P.,
Amara A., Yssel H., Misse D.;
"Biology of zika virus infection in human skin cells.";
J. Virol. 89:8880-8896(2015).
[3]
REVIEW (NON-STRUCTURAL PROTEIN 1).
STRAIN=Zika virus (strain Mr 766);
PubMed=27473856; DOI=10.1186/s12985-016-0590-7;
Rastogi M., Sharma N., Singh S.K.;
"Flavivirus NS1: a multifaceted enigmatic viral protein.";
Virol. J. 13:131-131(2016).
[4]
FUNCTION (NON-STRUCTURAL PROTEIN 4A), AND FUNCTION (NON-STRUCTURAL
PROTEIN 4B).
PubMed=27524440; DOI=10.1016/j.stem.2016.07.019;
Liang Q., Luo Z., Zeng J., Chen W., Foo S.S., Lee S.A., Ge J.,
Wang S., Goldman S.A., Zlokovic B.V., Zhao Z., Jung J.U.;
"Zika virus NS4A and NS4B proteins deregulate Akt-mTOR signaling in
human fetal neural stem cells to inhibit neurogenesis and induce
autophagy.";
Cell Stem Cell 19:663-671(2016).
[5]
SUBUNIT (NON-STRUCTURAL PROTEIN 1).
STRAIN=Zika virus (strain Mr 766);
PubMed=27455458; DOI=10.1038/nsmb.3268;
Brown W.C., Akey D.L., Konwerski J.R., Tarrasch J.T., Skiniotis G.,
Kuhn R.J., Smith J.L.;
"Extended surface for membrane association in Zika virus NS1
structure.";
Nat. Struct. Mol. Biol. 23:865-867(2016).
[6]
GLYCOSYLATION AT ASN-444, AND MUTAGENESIS OF ASN-444.
PubMed=29091758; DOI=10.1016/j.celrep.2017.10.016;
Fontes-Garfias C.R., Shan C., Luo H., Muruato A.E., Medeiros D.B.A.,
Mays E., Xie X., Zou J., Roundy C.M., Wakamiya M., Rossi S.L.,
Wang T., Weaver S.C., Shi P.Y.;
"Functional analysis of glycosylation of a Zika Virus envelope
protein.";
Cell Rep. 21:1180-1190(2017).
[7]
DOMAIN (SERINE PROTEASE SUBUNIT NS2B).
STRAIN=Zika virus (strain Mr 766);
PubMed=29080786; DOI=10.1016/j.jmb.2017.10.018;
Mishra P.M., Uversky V.N., Giri R.;
"Molecular recognition features in zika virus proteome.";
J. Mol. Biol. 0:0-0(2017).
[8]
FUNCTION (PROTEIN PRM).
PubMed=28971967; DOI=10.1126/science.aam7120;
Yuan L., Huang X.Y., Liu Z.Y., Zhang F., Zhu X.L., Yu J.Y., Ji X.,
Xu Y.P., Li G., Li C., Wang H.J., Deng Y.Q., Wu M., Cheng M.L., Ye Q.,
Xie D.Y., Li X.F., Wang X., Shi W., Hu B., Shi P.Y., Xu Z., Qin C.F.;
"A single mutation in the prM protein of Zika virus contributes to
fetal microcephaly.";
Science 358:933-936(2017).
[9]
FUNCTION (NON-STRUCTURAL PROTEIN 2A).
STRAIN=Zika virus (strain Mr 766);
PubMed=28826723; DOI=10.1016/j.stem.2017.07.014;
Yoon K.J., Song G., Qian X., Pan J., Xu D., Rho H.S., Kim N.S.,
Habela C., Zheng L., Jacob F., Zhang F., Lee E.M., Huang W.K.,
Ringeling F.R., Vissers C., Li C., Yuan L., Kang K., Kim S., Yeo J.,
Cheng Y., Liu S., Wen Z., Qin C.F., Wu Q., Christian K.M., Tang H.,
Jin P., Xu Z., Qian J., Zhu H., Song H., Ming G.L.;
"Zika-Virus-encoded NS2A disrupts mammalian cortical neurogenesis by
degrading adherens junction proteins.";
Cell Stem Cell 21:349-358(2017).
[10]
FUNCTION (SERINE PROTEASE NS3), AND FUNCTION (NON-STRUCTURAL PROTEIN
4A).
STRAIN=ZIKV/Homo sapiens/THA/PLCal_ZV/2013;
PubMed=28592527; DOI=10.1128/JVI.00474-17;
Hou S., Kumar A., Xu Z., Airo A.M., Stryapunina I., Wong C.P.,
Branton W., Tchesnokov E., Goette M., Power C., Hobman T.C.;
"Zika virus hijacks stress granule proteins and modulates the host
stress response.";
J. Virol. 0:0-0(2017).
[11]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2524-2785 IN COMPLEX WITH
GTP; S-ADENOSYL-L-METHIONINE.
PubMed=27866982; DOI=10.1016/j.bbrc.2016.11.098;
Zhang C., Feng T., Cheng J., Li Y., Yin X., Zeng W., Jin X., Li Y.,
Guo F., Jin T.;
"Structure of the NS5 methyltransferase from Zika virus and
implications in inhibitor design.";
Biochem. Biophys. Res. Commun. 492:624-630(2017).
[12]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 589-697, AND DISULFIDE
BONDS.
PubMed=27475895; DOI=10.1016/j.cell.2016.07.020;
Zhao H., Fernandez E., Dowd K.A., Speer S.D., Platt D.J., Gorman M.J.,
Govero J., Nelson C.A., Pierson T.C., Diamond M.S., Fremont D.H.;
"Structural basis of Zika Virus-specific antibody protection.";
Cell 166:1016-1027(2016).
[13]
X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 2521-2786 IN COMPLEX WITH
S-ADENOSYL-L-METHIONINE.
PubMed=27633330; DOI=10.1016/j.celrep.2016.08.091;
Coloma J., Jain R., Rajashankar K.R., Garcia-Sastre A., Aggarwal A.K.;
"Structures of NS5 Methyltransferase from Zika Virus.";
Cell Rep. 16:3097-3102(2016).
[14]
STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS) OF 216-794, AND
DISULFIDE BONDS.
PubMed=27882950; DOI=10.1038/ncomms13679;
Zhang S., Kostyuchenko V.A., Ng T.S., Lim X.N., Ooi J.S., Lambert S.,
Tan T.Y., Widman D.G., Shi J., Baric R.S., Lok S.M.;
"Neutralization mechanism of a highly potent antibody against Zika
virus.";
Nat. Commun. 7:13679-13679(2016).
[15]
STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS) OF 216-794, AND
DISULFIDE BONDS.
PubMed=27093288; DOI=10.1038/nature17994;
Kostyuchenko V.A., Lim E.X., Zhang S., Fibriansah G., Ng T.S.,
Ooi J.S., Shi J., Lok S.M.;
"Structure of the thermally stable Zika virus.";
Nature 533:425-428(2016).
[16]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 291-698, AND DISULFIDE
BONDS.
PubMed=27338953; DOI=10.1038/nature18938;
Barba-Spaeth G., Dejnirattisai W., Rouvinski A., Vaney M.C.,
Medits I., Sharma A., Simon-Loriere E., Sakuntabhai A.,
Cao-Lormeau V.M., Haouz A., England P., Stiasny K., Mongkolsapaya J.,
Heinz F.X., Screaton G.R., Rey F.A.;
"Structural basis of potent Zika-dengue virus antibody cross-
neutralization.";
Nature 536:48-53(2016).
[17]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1674-2119.
PubMed=27172988; DOI=10.1007/s13238-016-0275-4;
Tian H., Ji X., Yang X., Xie W., Yang K., Chen C., Wu C., Chi H.,
Mu Z., Wang Z., Yang H.;
"The crystal structure of Zika virus helicase: basis for antiviral
drug design.";
Protein Cell 7:450-454(2016).
[18]
STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 291-794 AND
216-290, AND DISULFIDE BONDS.
PubMed=27033547; DOI=10.1126/science.aaf5316;
Sirohi D., Chen Z., Sun L., Klose T., Pierson T.C., Rossmann M.G.,
Kuhn R.J.;
"The 3.8 A resolution cryo-EM structure of Zika virus.";
Science 352:467-470(2016).
[19]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2521-2784, AND DISULFIDE
BONDS.
PubMed=28357511; DOI=10.1007/s00705-017-3345-x;
Hercik K., Brynda J., Nencka R., Boura E.;
"Structural basis of Zika virus methyltransferase inhibition by
sinefungin.";
Arch. Virol. 162:2091-2096(2017).
[20]
X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 2525-2786 IN COMPLEX WITH
S-ADENOSYL-L-METHIONINE.
PubMed=28031359; DOI=10.1128/JVI.02202-16;
Coutard B., Barral K., Lichiere J., Selisko B., Martin B., Aouadi W.,
Lombardia M.O., Debart F., Vasseur J.J., Guillemot J.C., Canard B.,
Decroly E.;
"Zika Virus methyltransferase: structure and functions for drug design
perspectives.";
J. Virol. 91:0-0(2017).
[21]
STRUCTURE BY ELECTRON MICROSCOPY (6.20 ANGSTROMS) OF 291-686, AND
DISULFIDE BONDS.
PubMed=28300075; DOI=10.1038/ncomms14722;
Hasan S.S., Miller A., Sapparapu G., Fernandez E., Klose T., Long F.,
Fokine A., Porta J.C., Jiang W., Diamond M.S., Crowe J.E., Kuhn R.J.,
Rossmann M.G.;
"A human antibody against Zika virus crosslinks the E protein to
prevent infection.";
Nat. Commun. 8:14722-14722(2017).
[22]
STRUCTURE BY ELECTRON MICROSCOPY (9.10 ANGSTROMS) OF 726-791 AND
238-290.
PubMed=28067914; DOI=10.1038/nsmb.3352;
Prasad V.M., Miller A.S., Klose T., Sirohi D., Buda G., Jiang W.,
Kuhn R.J., Rossmann M.G.;
"Structure of the immature Zika virus at 9 A resolution.";
Nat. Struct. Mol. Biol. 24:184-186(2017).
[23]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2521-2788, AND DISULFIDE
BONDS.
PubMed=28487506; DOI=10.1038/s41598-017-01756-7;
Jain R., Butler K.V., Coloma J., Jin J., Aggarwal A.K.;
"Development of a S-adenosylmethionine analog that intrudes the RNA-
cap binding site of Zika methyltransferase.";
Sci. Rep. 7:1632-1632(2017).
-!- 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.
{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: Plays a role in host immune defense
modulation and protection of envelope protein E during virion
synthesis. PrM-E cleavage is ineficient, and immature prM-E
proteins could have an activity against host immune response. The
sequence of PrM contributes to fetal microcephaly in Humans. 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 could play a role
in immune evasion. {ECO:0000250|UniProtKB:P17763,
ECO:0000269|PubMed:28971967}.
-!- 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 particule 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 could 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 (By
similarity). Disrupts adherens junction formation and thereby
impairs proliferation of radial cells in both embryonic mouse
cortex and human forebrain organoids (PubMed:28826723).
{ECO:0000250|UniProtKB:P14335, ECO:0000269|PubMed:28826723}.
-!- FUNCTION: Non-structural protein 2B: Required cofactor for the
serine protease function of NS3. {ECO:0000250|UniProtKB:Q32ZE1}.
-!- 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 (By
similarity). Leads to translation arrest when expressed ex vivo
(PubMed:28592527). {ECO:0000250|UniProtKB:Q32ZE1,
ECO:0000269|PubMed:28592527}.
-!- FUNCTION: Non-structural protein 4A: Regulates the ATPase activity
of the NS3 helicase activity. NS4A allows NS3 helicase to conserve
energy during unwinding (By similarity). Cooperatively with NS4B
suppress the Akt-mTOR pathway and lead to cellular dysregulation
(PubMed:27524440). Leads to translation arrest when expressed ex
vivo (PubMed:28592527). {ECO:0000250|UniProtKB:Q9Q6P4,
ECO:0000269|PubMed:27524440, ECO:0000269|PubMed:28592527}.
-!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and
is required for the interferon antagonism activity of the latter.
{ECO:0000250}.
-!- 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 (By similarity). Cooperatively with NS4A suppress the
Akt-mTOR pathway and lead to cellular dysregulation
(PubMed:27524440). {ECO:0000250|UniProtKB:Q9Q6P4,
ECO:0000269|PubMed:27524440}.
-!- FUNCTION: RNA-directed RNA polymerase NS5: Replicates the viral
(+) and (-) RNA genome, and performs the capping of genomes in the
cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose
2'-O positions. 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.
Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing
activation of JAK-STAT signaling pathway.
{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}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- 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. {ECO:0000250|UniProtKB:Q32ZE1}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
{ECO:0000250|UniProtKB:Q32ZE1}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- SUBUNIT: Capsid protein C: Homodimer. 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). Interacts with
host Tyro3, AXL and DC-SIGN proteins (PubMed:26085147). Non-
structural protein 1: Homodimer; Homohexamer when secreted
(PubMed:27455458). Interacts with envelope protein E (By
similarity). Non-structural protein 2B: Forms a heterodimer with
serine protease NS3. May form homooligomers (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:26085147,
ECO:0000269|PubMed:27455458}.
-!- 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:P17763}; Multi-pass membrane protein
{ECO:0000255}. Host endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000255}. Host endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted
{ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:Q32ZE1}; Peripheral membrane
protein {ECO:0000250|UniProtKB:Q32ZE1}; 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:P17763}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:Q32ZE1}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P17763}; 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 {ECO:0000250|UniProtKB:Q32ZE1};
Peripheral membrane protein {ECO:0000250|UniProtKB:Q32ZE1};
Cytoplasmic side {ECO:0000250|UniProtKB:Q32ZE1}. Host nucleus
{ECO:0000250|UniProtKB:P17763}. 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: Small envelope protein M: The transmembrane domain
contains an endoplasmic reticulum retention signal.
{ECO:0000250|UniProtKB:P17763}.
-!- DOMAIN: Envelope protein E: The transmembrane domain contains an
endoplasmic reticulum retention signal.
{ECO:0000250|UniProtKB:P17763}.
-!- DOMAIN: Capsid protein C: The disordered region at the N-terminus
may be involved in lipid-droplet binding.
{ECO:0000250|UniProtKB:P12823}.
-!- DOMAIN: Serine protease subunit NS2B: The central disordered
region transitions to ordered by binding to NS3.
{ECO:0000269|PubMed:29080786}.
-!- 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-glycosylation plays a role in virulence
in mammal?ian and mosquito hosts, but may have no effect on
neurovirulence. {ECO:0000269|PubMed:29091758}.
-!- 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}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Side effects - Issue
200 of February 2018;
URL="https://web.expasy.org/spotlight/back_issues/200/";
-----------------------------------------------------------------------
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EMBL; KJ776791; AHZ13508.1; -; Genomic_RNA.
EMBL; KX447509; ANO46301.1; -; Genomic_RNA.
EMBL; KX447510; ANO46302.1; -; Genomic_RNA.
EMBL; KX447512; ANO46304.1; -; Genomic_RNA.
PDB; 5GOZ; X-ray; 2.05 A; A/B/C=2524-2785.
PDB; 5GP1; X-ray; 2.44 A; A/B/C=2524-2785.
PDB; 5H30; EM; 4.40 A; A/B/C=291-794, D/E/F=216-290.
PDB; 5H32; EM; 12.00 A; A/B/C=291-693.
PDB; 5H37; EM; 4.00 A; A/B/C=291-794, D/E/F=216-290.
PDB; 5IRE; EM; 3.80 A; A/C/E=291-794, B/D/F=216-290.
PDB; 5IZ7; EM; 3.70 A; A/B/C=291-794, D/E/F=216-290.
PDB; 5JMT; X-ray; 1.80 A; A=1674-2119.
PDB; 5KQR; X-ray; 1.33 A; A=2521-2786.
PDB; 5KQS; X-ray; 1.50 A; A=2521-2786.
PDB; 5KVE; X-ray; 1.70 A; E=588-697.
PDB; 5LBS; X-ray; 2.41 A; A/B=291-698.
PDB; 5LBV; X-ray; 2.20 A; A/B=291-698.
PDB; 5LCV; X-ray; 2.64 A; A/B=291-698.
PDB; 5M5B; X-ray; 2.01 A; A/B=2525-2786.
PDB; 5MRK; X-ray; 1.90 A; A/B=2521-2784.
PDB; 5NJU; X-ray; 2.10 A; A/B=2525-2784.
PDB; 5NJV; X-ray; 2.00 A; A/B/C/D=2524-2785.
PDB; 5U4W; EM; 9.10 A; G/I/K=726-791, H/J/L=238-290.
PDB; 5UHY; EM; 6.20 A; A/C/E=291-686.
PDB; 5ULP; X-ray; 1.55 A; A/B=2521-2788.
PDB; 5Y0A; EM; 22.00 A; A/B/C=291-693.
PDBsum; 5GOZ; -.
PDBsum; 5GP1; -.
PDBsum; 5H30; -.
PDBsum; 5H32; -.
PDBsum; 5H37; -.
PDBsum; 5IRE; -.
PDBsum; 5IZ7; -.
PDBsum; 5JMT; -.
PDBsum; 5KQR; -.
PDBsum; 5KQS; -.
PDBsum; 5KVE; -.
PDBsum; 5LBS; -.
PDBsum; 5LBV; -.
PDBsum; 5LCV; -.
PDBsum; 5M5B; -.
PDBsum; 5MRK; -.
PDBsum; 5NJU; -.
PDBsum; 5NJV; -.
PDBsum; 5U4W; -.
PDBsum; 5UHY; -.
PDBsum; 5ULP; -.
PDBsum; 5Y0A; -.
SMR; A0A024B7W1; -.
Proteomes; UP000112691; Genome.
Proteomes; UP000137079; Genome.
Proteomes; UP000151151; Genome.
Proteomes; UP000168269; 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:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0005525; F:GTP binding; IEA:UniProtKB-KW.
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: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: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.
CDD; cd00079; HELICc; 1.
Gene3D; 1.10.10.930; -; 1.
Gene3D; 1.10.8.970; -; 1.
Gene3D; 1.20.1280.260; -; 1.
Gene3D; 2.60.260.50; -; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 2.60.98.10; -; 3.
Gene3D; 3.30.387.10; -; 2.
Gene3D; 3.30.67.10; -; 4.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR000069; Env_glycoprot_M_flavivir.
InterPro; IPR038302; Env_glycoprot_M_sf_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; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
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; IPR038688; Flavi_propep_sf.
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; IPR038055; Glycoprot_E_dimer_dom.
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; 4Fe-4S; 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;
GTP-binding; 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;
Inhibition of host TYK2 by virus; Iron; Iron-sulfur; Membrane;
Metal-binding; Methyltransferase; mRNA capping; mRNA processing;
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 3423 Genome polyprotein.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000443018.
CHAIN 1 104 Capsid protein C.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000443019.
PROPEP 105 122 ER anchor for capsid protein C, removed
in mature form by serine protease NS3.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000443020.
CHAIN 123 290 Protein prM.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000443021.
CHAIN 123 215 Peptide pr.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000443022.
CHAIN 216 290 Small envelope protein M.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000443023.
CHAIN 291 794 Envelope protein E.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000443024.
CHAIN 795 1146 Non-structural protein 1.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000443025.
CHAIN 1147 1372 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000443026.
CHAIN 1373 1502 Serine protease syssubunit NS2B.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000443027.
CHAIN 1503 2119 Serine protease NS3.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000443028.
CHAIN 2120 2246 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000443029.
PEPTIDE 2247 2269 Peptide 2k.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000443030.
CHAIN 2270 2520 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000443031.
CHAIN 2521 3423 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000443032.
TOPO_DOM 1 104 Cytoplasmic. {ECO:0000305}.
TRANSMEM 105 125 Helical. {ECO:0000255}.
TOPO_DOM 126 249 Extracellular. {ECO:0000305}.
TRANSMEM 250 269 Helical. {ECO:0000255}.
TOPO_DOM 270 274 Cytoplasmic. {ECO:0000305}.
TRANSMEM 275 290 Helical. {ECO:0000305}.
TOPO_DOM 291 745 Extracellular. {ECO:0000305}.
TRANSMEM 746 767 Helical. {ECO:0000255}.
TOPO_DOM 768 773 Cytoplasmic. {ECO:0000305}.
TRANSMEM 774 794 Helical. {ECO:0000255}.
TOPO_DOM 795 1177 Lumenal. {ECO:0000305}.
TRANSMEM 1178 1198 Helical. {ECO:0000255}.
TOPO_DOM 1199 1220 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1221 1241 Helical. {ECO:0000255}.
TOPO_DOM 1242 1270 Lumenal. {ECO:0000305}.
TRANSMEM 1271 1291 Helical. {ECO:0000255}.
TOPO_DOM 1292 1295 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1296 1316 Helical. {ECO:0000255}.
TOPO_DOM 1317 1345 Lumenal. {ECO:0000305}.
TRANSMEM 1346 1366 Helical. {ECO:0000255}.
TOPO_DOM 1367 1373 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1374 1394 Helical. {ECO:0000255}.
TOPO_DOM 1395 1397 Lumenal. {ECO:0000305}.
TRANSMEM 1398 1418 Helical. {ECO:0000255}.
TOPO_DOM 1419 1472 Cytoplasmic. {ECO:0000305}.
INTRAMEM 1473 1493 Helical. {ECO:0000255}.
TOPO_DOM 1494 2170 Lumenal. {ECO:0000305}.
TRANSMEM 2171 2191 Helical. {ECO:0000255}.
TOPO_DOM 2192 2195 Lumenal. {ECO:0000305}.
INTRAMEM 2196 2216 Helical. {ECO:0000255}.
TOPO_DOM 2217 2218 Cytoplasmic. {ECO:0000305}.
TRANSMEM 2219 2239 Helical. {ECO:0000255}.
TOPO_DOM 2240 2254 Lumenal. {ECO:0000305}.
INTRAMEM 2255 2269 Helical; Note=Signal for NS4B.
{ECO:0000305}.
TOPO_DOM 2268 2307 Lumenal. {ECO:0000305}.
INTRAMEM 2308 2328 Helical. {ECO:0000255}.
TOPO_DOM 2329 2344 Lumenal. {ECO:0000305}.
TRANSMEM 2345 2365 Helical. {ECO:0000255}.
TOPO_DOM 2366 2375 Cytoplasmic. {ECO:0000305}.
TRANSMEM 2376 2396 Helical. {ECO:0000255}.
TOPO_DOM 2397 2441 Lumenal. {ECO:0000305}.
TRANSMEM 2442 2462 Helical. {ECO:0000255}.
TOPO_DOM 2463 3423 Cytoplasmic. {ECO:0000305}.
DOMAIN 1503 1680 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1683 1839 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1834 2013 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2521 2785 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3049 3199 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1696 1703 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
NP_BIND 2533 2539 GTP. {ECO:0000244|PDB:5GOZ}.
NP_BIND 2669 2675 GTP. {ECO:0000244|PDB:5GOZ}.
NP_BIND 2733 2735 GTP. {ECO:0000244|PDB:5GOZ}.
REGION 1 25 Disordered.
{ECO:0000250|UniProtKB:Q32ZE1}.
REGION 37 72 Hydrophobic; homodimerization of capsid
protein C.
{ECO:0000250|UniProtKB:P29990}.
REGION 388 401 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
REGION 1425 1464 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
REGION 1429 1451 Disordered.
{ECO:0000250|UniProtKB:Q32ZE1}.
REGION 1687 1690 Important for RNA-binding.
{ECO:0000250|UniProtKB:P14340}.
REGION 2601 2607 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:5GP1}.
REGION 2624 2625 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:5GP1}.
REGION 2630 2631 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:5GOZ,
ECO:0000244|PDB:5GP1}.
REGION 2651 2652 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:5GOZ,
ECO:0000244|PDB:5GP1}.
MOTIF 1787 1790 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
ACT_SITE 1553 1553 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1577 1577 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1637 1637 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 2581 2581 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2666 2666 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2702 2702 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2738 2738 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2959 2959 Zinc 1. {ECO:0000250|UniProtKB:Q32ZE1}.
METAL 2963 2963 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:Q32ZE1}.
METAL 2968 2968 Zinc 1. {ECO:0000250|UniProtKB:Q32ZE1}.
METAL 2971 2971 Zinc 1. {ECO:0000250|UniProtKB:Q32ZE1}.
METAL 3234 3234 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:Q32ZE1}.
METAL 3250 3250 Zinc 2. {ECO:0000250|UniProtKB:Q32ZE1}.
METAL 3369 3369 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
BINDING 2533 2533 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2536 2536 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2537 2537 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2539 2539 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2544 2544 mRNA cap. {ECO:0000244|PDB:5GOZ}.
BINDING 2548 2548 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2576 2576 S-adenosyl-L-methionine.
{ECO:0000244|PDB:5GOZ}.
BINDING 2651 2651 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2652 2652 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2670 2670 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2733 2733 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2735 2735 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2740 2740 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 104 105 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:Q32ZE1}.
SITE 122 123 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:Q32ZE1}.
SITE 139 139 Fetal microcephaly.
SITE 215 216 Cleavage; by host furin.
{ECO:0000250|UniProtKB:Q32ZE1}.
SITE 290 291 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P09732}.
SITE 794 795 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P09732}.
SITE 1146 1147 Cleavage; by host.
{ECO:0000250|UniProtKB:P09732}.
SITE 1372 1373 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P09732}.
SITE 1502 1503 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P09732}.
SITE 1958 1958 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 1961 1961 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 2119 2120 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P09732}.
SITE 2246 2247 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P09732}.
SITE 2269 2270 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P09732}.
SITE 2520 2521 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P09732}.
SITE 2667 2667 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
MOD_RES 2576 2576 Phosphoserine.
{ECO:0000250|UniProtKB:P03314}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 444 444 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000244|PDB:5H37,
ECO:0000244|PDB:5IZ7,
ECO:0000244|PDB:5LBV,
ECO:0000244|PDB:5LCV,
ECO:0000269|PubMed:29091758}.
CARBOHYD 924 924 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:Q9Q6P4}.
CARBOHYD 1001 1001 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 350 406 {ECO:0000250|UniProtKB:P17763}.
DISULFID 382 411 {ECO:0000250|UniProtKB:P17763}.
DISULFID 798 809 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 849 937 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 973 1017 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 1074 1123 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 1085 1106 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 1107 1110 {ECO:0000250|UniProtKB:Q9Q6P4}.
MUTAGEN 444 444 N->Q: Improves attachment, assembly and
infectivity in cell culture. Attenuates
the virus in mouse and mosquitoes.
{ECO:0000269|PubMed:29091758}.
TURN 292 295 {ECO:0000244|PDB:5LBV}.
STRAND 297 303 {ECO:0000244|PDB:5LBV}.
STRAND 305 307 {ECO:0000244|PDB:5LBV}.
STRAND 310 316 {ECO:0000244|PDB:5LBV}.
STRAND 320 324 {ECO:0000244|PDB:5LBV}.
STRAND 331 340 {ECO:0000244|PDB:5LBV}.
STRAND 345 362 {ECO:0000244|PDB:5LBV}.
HELIX 373 376 {ECO:0000244|PDB:5LBV}.
STRAND 380 390 {ECO:0000244|PDB:5LBV}.
TURN 391 394 {ECO:0000244|PDB:5LBV}.
STRAND 399 418 {ECO:0000244|PDB:5LBV}.
HELIX 422 424 {ECO:0000244|PDB:5LBV}.
STRAND 425 433 {ECO:0000244|PDB:5LBV}.
HELIX 439 441 {ECO:0000244|PDB:5LBV}.
TURN 448 450 {ECO:0000244|PDB:5LCV}.
STRAND 454 460 {ECO:0000244|PDB:5LBV}.
STRAND 461 463 {ECO:0000244|PDB:5LBS}.
STRAND 465 469 {ECO:0000244|PDB:5LBV}.
HELIX 471 473 {ECO:0000244|PDB:5LBV}.
STRAND 474 481 {ECO:0000244|PDB:5LBV}.
HELIX 488 490 {ECO:0000244|PDB:5LCV}.
STRAND 491 496 {ECO:0000244|PDB:5LBV}.
STRAND 499 504 {ECO:0000244|PDB:5LBV}.
HELIX 505 509 {ECO:0000244|PDB:5LBV}.
STRAND 515 517 {ECO:0000244|PDB:5LBV}.
HELIX 529 532 {ECO:0000244|PDB:5LBV}.
STRAND 533 537 {ECO:0000244|PDB:5LBV}.
TURN 539 541 {ECO:0000244|PDB:5LBS}.
STRAND 543 547 {ECO:0000244|PDB:5LBV}.
HELIX 552 558 {ECO:0000244|PDB:5LBV}.
TURN 559 561 {ECO:0000244|PDB:5LBV}.
STRAND 562 568 {ECO:0000244|PDB:5LBV}.
STRAND 571 573 {ECO:0000244|PDB:5LBV}.
STRAND 578 584 {ECO:0000244|PDB:5LBV}.
HELIX 585 587 {ECO:0000244|PDB:5LBS}.
TURN 591 594 {ECO:0000244|PDB:5LCV}.
STRAND 602 606 {ECO:0000244|PDB:5KVE}.
STRAND 616 622 {ECO:0000244|PDB:5KVE}.
STRAND 628 630 {ECO:0000244|PDB:5KVE}.
STRAND 633 637 {ECO:0000244|PDB:5KVE}.
TURN 639 641 {ECO:0000244|PDB:5KVE}.
STRAND 644 648 {ECO:0000244|PDB:5KVE}.
STRAND 650 652 {ECO:0000244|PDB:5KVE}.
STRAND 662 669 {ECO:0000244|PDB:5KVE}.
STRAND 672 682 {ECO:0000244|PDB:5KVE}.
STRAND 686 692 {ECO:0000244|PDB:5KVE}.
STRAND 1678 1680 {ECO:0000244|PDB:5JMT}.
HELIX 1683 1686 {ECO:0000244|PDB:5JMT}.
STRAND 1691 1694 {ECO:0000244|PDB:5JMT}.
TURN 1702 1705 {ECO:0000244|PDB:5JMT}.
HELIX 1706 1716 {ECO:0000244|PDB:5JMT}.
STRAND 1721 1727 {ECO:0000244|PDB:5JMT}.
HELIX 1728 1737 {ECO:0000244|PDB:5JMT}.
TURN 1738 1740 {ECO:0000244|PDB:5JMT}.
STRAND 1759 1764 {ECO:0000244|PDB:5JMT}.
HELIX 1765 1773 {ECO:0000244|PDB:5JMT}.
STRAND 1774 1776 {ECO:0000244|PDB:5JMT}.
STRAND 1782 1788 {ECO:0000244|PDB:5JMT}.
HELIX 1794 1808 {ECO:0000244|PDB:5JMT}.
STRAND 1813 1817 {ECO:0000244|PDB:5JMT}.
STRAND 1835 1839 {ECO:0000244|PDB:5JMT}.
STRAND 1848 1850 {ECO:0000244|PDB:5JMT}.
HELIX 1852 1855 {ECO:0000244|PDB:5JMT}.
STRAND 1861 1864 {ECO:0000244|PDB:5JMT}.
HELIX 1868 1880 {ECO:0000244|PDB:5JMT}.
STRAND 1885 1888 {ECO:0000244|PDB:5JMT}.
TURN 1890 1892 {ECO:0000244|PDB:5JMT}.
HELIX 1893 1896 {ECO:0000244|PDB:5JMT}.
HELIX 1899 1902 {ECO:0000244|PDB:5JMT}.
STRAND 1906 1912 {ECO:0000244|PDB:5JMT}.
TURN 1914 1917 {ECO:0000244|PDB:5JMT}.
STRAND 1923 1927 {ECO:0000244|PDB:5JMT}.
STRAND 1930 1937 {ECO:0000244|PDB:5JMT}.
TURN 1938 1940 {ECO:0000244|PDB:5JMT}.
STRAND 1941 1949 {ECO:0000244|PDB:5JMT}.
HELIX 1952 1959 {ECO:0000244|PDB:5JMT}.
STRAND 1971 1975 {ECO:0000244|PDB:5JMT}.
HELIX 1988 1996 {ECO:0000244|PDB:5JMT}.
HELIX 2011 2016 {ECO:0000244|PDB:5JMT}.
TURN 2021 2024 {ECO:0000244|PDB:5JMT}.
HELIX 2028 2038 {ECO:0000244|PDB:5JMT}.
HELIX 2045 2053 {ECO:0000244|PDB:5JMT}.
HELIX 2062 2064 {ECO:0000244|PDB:5JMT}.
HELIX 2069 2071 {ECO:0000244|PDB:5JMT}.
STRAND 2081 2083 {ECO:0000244|PDB:5JMT}.
STRAND 2089 2091 {ECO:0000244|PDB:5JMT}.
HELIX 2099 2101 {ECO:0000244|PDB:5JMT}.
STRAND 2102 2104 {ECO:0000244|PDB:5JMT}.
HELIX 2105 2115 {ECO:0000244|PDB:5JMT}.
HELIX 2528 2538 {ECO:0000244|PDB:5KQR}.
HELIX 2541 2547 {ECO:0000244|PDB:5KQR}.
TURN 2548 2551 {ECO:0000244|PDB:5KQR}.
STRAND 2553 2556 {ECO:0000244|PDB:5KQR}.
HELIX 2558 2565 {ECO:0000244|PDB:5KQR}.
STRAND 2569 2571 {ECO:0000244|PDB:5NJV}.
HELIX 2578 2587 {ECO:0000244|PDB:5KQR}.
STRAND 2595 2600 {ECO:0000244|PDB:5KQR}.
TURN 2603 2605 {ECO:0000244|PDB:5GP1}.
HELIX 2606 2612 {ECO:0000244|PDB:5KQR}.
STRAND 2617 2623 {ECO:0000244|PDB:5KQR}.
HELIX 2641 2643 {ECO:0000244|PDB:5KQR}.
STRAND 2644 2647 {ECO:0000244|PDB:5KQR}.
HELIX 2652 2654 {ECO:0000244|PDB:5KQR}.
STRAND 2661 2665 {ECO:0000244|PDB:5KQR}.
HELIX 2674 2692 {ECO:0000244|PDB:5KQR}.
STRAND 2697 2704 {ECO:0000244|PDB:5KQR}.
HELIX 2709 2722 {ECO:0000244|PDB:5KQR}.
STRAND 2725 2727 {ECO:0000244|PDB:5KQR}.
STRAND 2739 2742 {ECO:0000244|PDB:5KQR}.
HELIX 2749 2762 {ECO:0000244|PDB:5KQR}.
STRAND 2765 2767 {ECO:0000244|PDB:5KQR}.
STRAND 2772 2775 {ECO:0000244|PDB:5KQR}.
SEQUENCE 3423 AA; 379113 MW; 5F0E490EE43DE346 CRC64;
MKNPKKKSGG FRIVNMLKRG VARVSPFGGL KRLPAGLLLG HGPIRMVLAI LAFLRFTAIK
PSLGLINRWG SVGKKEAMEI IKKFKKDLAA MLRIINARKE KKRRGADTSV GIVGLLLTTA
MAAEVTRRGS AYYMYLDRND AGEAISFPTT LGMNKCYIQI MDLGHMCDAT MSYECPMLDE
GVEPDDVDCW CNTTSTWVVY GTCHHKKGEA RRSRRAVTLP SHSTRKLQTR SQTWLESREY
TKHLIRVENW IFRNPGFALA AAAIAWLLGS STSQKVIYLV MILLIAPAYS IRCIGVSNRD
FVEGMSGGTW VDVVLEHGGC VTVMAQDKPT VDIELVTTTV SNMAEVRSYC YEASISDMAS
DSRCPTQGEA YLDKQSDTQY VCKRTLVDRG WGNGCGLFGK GSLVTCAKFA CSKKMTGKSI
QPENLEYRIM LSVHGSQHSG MIVNDTGHET DENRAKVEIT PNSPRAEATL GGFGSLGLDC
EPRTGLDFSD LYYLTMNNKH WLVHKEWFHD IPLPWHAGAD TGTPHWNNKE ALVEFKDAHA
KRQTVVVLGS QEGAVHTALA GALEAEMDGA KGRLSSGHLK CRLKMDKLRL KGVSYSLCTA
AFTFTKIPAE TLHGTVTVEV QYAGTDGPCK VPAQMAVDMQ TLTPVGRLIT ANPVITESTE
NSKMMLELDP PFGDSYIVIG VGEKKITHHW HRSGSTIGKA FEATVRGAKR MAVLGDTAWD
FGSVGGALNS LGKGIHQIFG AAFKSLFGGM SWFSQILIGT LLMWLGLNTK NGSISLMCLA
LGGVLIFLST AVSADVGCSV DFSKKETRCG TGVFVYNDVE AWRDRYKYHP DSPRRLAAAV
KQAWEDGICG ISSVSRMENI MWRSVEGELN AILEENGVQL TVVVGSVKNP MWRGPQRLPV
PVNELPHGWK AWGKSYFVRA AKTNNSFVVD GDTLKECPLK HRAWNSFLVE DHGFGVFHTS
VWLKVREDYS LECDPAVIGT AVKGKEAVHS DLGYWIESEK NDTWRLKRAH LIEMKTCEWP
KSHTLWTDGI EESDLIIPKS LAGPLSHHNT REGYRTQMKG PWHSEELEIR FEECPGTKVH
VEETCGTRGP SLRSTTASGR VIEEWCCREC TMPPLSFRAK DGCWYGMEIR PRKEPESNLV
RSMVTAGSTD HMDHFSLGVL VILLMVQEGL KKRMTTKIII STSMAVLVAM ILGGFSMSDL
AKLAILMGAT FAEMNTGGDV AHLALIAAFK VRPALLVSFI FRANWTPRES MLLALASCLL
QTAISALEGD LMVLINGFAL AWLAIRAMVV PRTDNITLAI LAALTPLARG TLLVAWRAGL
ATCGGFMLLS LKGKGSVKKN LPFVMALGLT AVRLVDPINV VGLLLLTRSG KRSWPPSEVL
TAVGLICALA GGFAKADIEM AGPMAAVGLL IVSYVVSGKS VDMYIERAGD ITWEKDAEVT
GNSPRLDVAL DESGDFSLVE DDGPPMREII LKVVLMTICG MNPIAIPFAA GAWYVYVKTG
KRSGALWDVP APKEVKKGET TDGVYRVMTR RLLGSTQVGV GVMQEGVFHT MWHVTKGSAL
RSGEGRLDPY WGDVKQDLVS YCGPWKLDAA WDGHSEVQLL AVPPGERARN IQTLPGIFKT
KDGDIGAVAL DYPAGTSGSP ILDKCGRVIG LYGNGVVIKN GSYVSAITQG RREEETPVEC
FEPSMLKKKQ LTVLDLHPGA GKTRRVLPEI VREAIKTRLR TVILAPTRVV AAEMEEALRG
LPVRYMTTAV NVTHSGTEIV DLMCHATFTS RLLQPIRVPN YNLYIMDEAH FTDPSSIAAR
GYISTRVEMG EAAAIFMTAT PPGTRDAFPD SNSPIMDTEV EVPERAWSSG FDWVTDHSGK
TVWFVPSVRN GNEIAACLTK AGKRVIQLSR KTFETEFQKT KHQEWDFVVT TDISEMGANF
KADRVIDSRR CLKPVILDGE RVILAGPMPV THASAAQRRG RIGRNPNKPG DEYLYGGGCA
ETDEDHAHWL EARMLLDNIY LQDGLIASLY RPEADKVAAI EGEFKLRTEQ RKTFVELMKR
GDLPVWLAYQ VASAGITYTD RRWCFDGTTN NTIMEDSVPA EVWTRHGEKR VLKPRWMDAR
VCSDHAALKS FKEFAAGKRG AAFGVMEALG TLPGHMTERF QEAIDNLAVL MRAETGSRPY
KAAAAQLPET LETIMLLGLL GTVSLGIFFV LMRNKGIGKM GFGMVTLGAS AWLMWLSEIE
PARIACVLIV VFLLLVVLIP EPEKQRSPQD NQMAIIIMVA VGLLGLITAN ELGWLERTKS
DLSHLMGRRE EGATIGFSMD IDLRPASAWA IYAALTTFIT PAVQHAVTTS YNNYSLMAMA
TQAGVLFGMG KGMPFYAWDF GVPLLMIGCY SQLTPLTLIV AIILLVAHYM YLIPGLQAAA
ARAAQKRTAA GIMKNPVVDG IVVTDIDTMT IDPQVEKKMG QVLLIAVAVS SAILSRTAWG
WGEAGALITA ATSTLWEGSP NKYWNSSTAT SLCNIFRGSY LAGASLIYTV TRNAGLVKRR
GGGTGETLGE KWKARLNQMS ALEFYSYKKS GITEVCREEA RRALKDGVAT GGHAVSRGSA
KLRWLVERGY LQPYGKVIDL GCGRGGWSYY AATIRKVQEV KGYTKGGPGH EEPMLVQSYG
WNIVRLKSGV DVFHMAAEPC DTLLCDIGES SSSPEVEEAR TLRVLSMVGD WLEKRPGAFC
IKVLCPYTST MMETLERLQR RYGGGLVRVP LSRNSTHEMY WVSGAKSNTI KSVSTTSQLL
LGRMDGPRRP VKYEEDVNLG SGTRAVVSCA EAPNMKIIGN RIERIRSEHA ETWFFDENHP
YRTWAYHGSY EAPTQGSASS LINGVVRLLS KPWDVVTGVT GIAMTDTTPY GQQRVFKEKV
DTRVPDPQEG TRQVMSMVSS WLWKELGKHK RPRVCTKEEF INKVRSNAAL GAIFEEEKEW
KTAVEAVNDP RFWALVDKER EHHLRGECQS CVYNMMGKRE KKQGEFGKAK GSRAIWYMWL
GARFLEFEAL GFLNEDHWMG RENSGGGVEG LGLQRLGYVL EEMSRIPGGR MYADDTAGWD
TRISRFDLEN EALITNQMEK GHRALALAII KYTYQNKVVK VLRPAEKGKT VMDIISRQDQ
RGSGQVVTYA LNTFTNLVVQ LIRNMEAEEV LEMQDLWLLR RSEKVTNWLQ SNGWDRLKRM
AVSGDDCVVK PIDDRFAHAL RFLNDMGKVR KDTQEWKPST GWDNWEEVPF CSHHFNKLHL
KDGRSIVVPC RHQDELIGRA RVSPGAGWSI RETACLAKSY AQMWQLLYFH RRDLRLMANA
ICSSVPVDWV PTGRTTWSIH GKGEWMTTED MLVVWNRVWI EENDHMEDKT PVTKWTDIPY
LGKREDLWCG SLIGHRPRTT WAENIKNTVN MVRRIIGDEE KYMDYLSTQV RYLGEEGSTP
GVL


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