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Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit 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) (Non-structural protein 5)]

 POLG_DEN28              Reviewed;        3391 AA.
P14337; Q20II6;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 2.
29-SEP-2021, entry version 167.
RecName: Full=Genome polyprotein;
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=Peptide 2k;
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=Non-structural protein 5;
Dengue virus type 2 (isolate Thailand/0168/1979) (DENV-2).
Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
Amarillovirales; Flaviviridae; Flavivirus.
NCBI_TaxID=413041;
NCBI_TaxID=53540; Aedimorphus.
NCBI_TaxID=53539; Diceromyia.
NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=53541; Stegomyia.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 281-775.
STRAIN=Isolate Malaysia M1;
PubMed=2587234; DOI=10.1093/nar/17.21.8875;
Samuel S., Koh C.L., Blok J., Pang T., Lam S.K.;
"Nucleotide sequence of the envelope protein gene of a Malaysian dengue-2
virus isolated from a patient with dengue haemorrhagic fever.";
Nucleic Acids Res. 17:8875-8875(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16528037; DOI=10.1099/vir.0.81486-0;
Zhang C., Mammen M.P. Jr., Chinnawirotpisan P., Klungthong C.,
Rodpradit P., Nisalak A., Vaughn D.W., Nimmannitya S., Kalayanarooj S.,
Holmes E.C.;
"Structure and age of genetic diversity of dengue virus type 2 in
Thailand.";
J. Gen. Virol. 87:873-883(2006).
[3]
X-RAY CRYSTALLOGRAPHY (9.5 ANGSTROMS) OF 281-775, TOPOLOGY (ENVELOPE
PROTEIN E), AND TOPOLOGY (SMALL ENVELOPE PROTEIN M).
PubMed=14528291; DOI=10.1038/nsb990;
Zhang W., Chipman P.R., Corver J., Johnson P.R., Zhang Y., Mukhopadhyay S.,
Baker T.S., Strauss J.H., Rossmann M.G., Kuhn R.J.;
"Visualization of membrane protein domains by cryo-electron microscopy of
dengue virus.";
Nat. Struct. Biol. 10:907-912(2003).
[4]
X-RAY CRYSTALLOGRAPHY (12.5 ANGSTROMS) OF 115-195.
PubMed=18369147; DOI=10.1126/science.1153263;
Li L., Lok S.M., Yu I.M., Zhang Y., Kuhn R.J., Chen J., Rossmann M.G.;
"The flavivirus precursor membrane-envelope protein complex: structure and
maturation.";
Science 319:1830-1834(2008).
-!- 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 1]: Disrupts the host endothelial
glycocalyx layer of host pulmonary microvascular endothelial cells,
inducing degradation of sialic acid and shedding of heparan sulfate
proteoglycans. NS1 induces expression of sialidases, heparanase, and
activates cathepsin L, which activates heparanase via enzymatic
cleavage. These effects are probably linked to the endothelial
hyperpermeability observed in severe dengue disease.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: [Non-structural protein 2A]: Component of the viral RNA
replication complex that functions in virion assembly and antagonizes
the host immune response. {ECO:0000250|UniProtKB:P17763}.
-!- 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. Plays a role in the inhibition of the host innate
immune response. Interacts with host MAVS and thereby prevents the
interaction between DDX58 and MAVS. In turn, IFN-beta production is
impaired. Interacts with host AUP1 which mediates induction of
lipophagy in host cells and facilitates production of virus progeny
particles (By similarity). {ECO:0000250|UniProtKB:P17763,
ECO:0000250|UniProtKB:P29991, 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.
{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. 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 (By similarity). May reduce immune responses by
preventing the recruitment of the host PAF1 complex to interferon-
responsive genes (By similarity). {ECO:0000250|UniProtKB:P17763,
ECO:0000250|UniProtKB:P29990}.
-!- CATALYTIC ACTIVITY:
Reaction=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.;
EC=3.4.21.91;
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
-!- CATALYTIC ACTIVITY:
Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-
ProRule:PRU00924};
-!- CATALYTIC ACTIVITY:
Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
-!- SUBUNIT: [Capsid protein C]: Homodimer. Interacts (via N-terminus) with
host EXOC1 (via C-terminus); this interaction results in EXOC1
degradation through the proteasome degradation pathway.
{ECO:0000250|UniProtKB:P17763}.
-!- SUBUNIT: [Protein prM]: Forms heterodimers with envelope protein E in
the endoplasmic reticulum and Golgi. {ECO:0000250|UniProtKB:P17763}.
-!- SUBUNIT: [Envelope protein E]: Homodimer; in the endoplasmic reticulum
and Golgi. Interacts with protein prM. Interacts with non-structural
protein 1. {ECO:0000250|UniProtKB:P17763}.
-!- SUBUNIT: [Non-structural protein 1]: Homodimer; Homohexamer when
secreted. Interacts with envelope protein E.
{ECO:0000250|UniProtKB:P17763}.
-!- SUBUNIT: [Non-structural protein 2A]: Interacts (via N-terminus) with
serine protease NS3. {ECO:0000250|UniProtKB:P17763}.
-!- SUBUNIT: [Serine protease subunit NS2B]: Forms a heterodimer with
serine protease NS3. May form homooligomers.
{ECO:0000250|UniProtKB:P17763}.
-!- SUBUNIT: [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. Interacts with host SHFL.
{ECO:0000250|UniProtKB:P17763}.
-!- SUBUNIT: [Non-structural protein 4A]: Interacts with host MAVS; this
interaction inhibits the synthesis of IFN-beta. Interacts with host
SHFL (By similarity). Interacts with host AUP1; the interaction occurs
in the presence of Dengue virus NS4B and induces lipophagy which
facilitates production of virus progeny particles (By similarity). May
interact with host SRPRA and SEC61G (By similarity).
{ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29990,
ECO:0000250|UniProtKB:P29991}.
-!- SUBUNIT: [Non-structural protein 4B]: Interacts with serine protease
NS3. {ECO:0000250|UniProtKB:P17763}.
-!- SUBUNIT: [RNA-directed RNA polymerase NS5]: Homodimer. Interacts with
host STAT2; this interaction inhibits the phosphorylation of the
latter, and, when all viral proteins are present (polyprotein), targets
STAT2 for degradation. Interacts with serine protease NS3 (By
similarity). Interacts with host PAF1 complex; the interaction may
prevent the recruitment of the PAF1 complex to interferon-responsive
genes, and thus reduces the immune response (By similarity).
{ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29990}.
-!- SUBCELLULAR LOCATION: [Capsid protein C]: Virion
{ECO:0000250|UniProtKB:P17763}. Host nucleus
{ECO:0000250|UniProtKB:P17763}. Host cytoplasm
{ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region
{ECO:0000250|UniProtKB:P17763}.
-!- 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;
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:P17763}; 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:P17763}; Multi-pass membrane
protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion
{ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles
hosting the replication complex. Interacts with host MAVS in the
mitochondrion-associated endoplasmic reticulum membranes.
{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:P17763}.
Note=Located in RE-associated vesicles hosting the replication complex.
NS5 protein is mainly localized in the nucleus rather than in ER
vesicles, especially in the DENV 2, 3, 4 serotypes.
{ECO:0000250|UniProtKB:P17763}.
-!- DOMAIN: The transmembrane domains of the small envelope protein M and
envelope protein E contain an endoplasmic reticulum retention signal.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield
mature proteins. Cleavages in the lumen of endoplasmic reticulum are
performed by host signal peptidase, whereas cleavages in the
cytoplasmic side are performed by serine protease NS3. Signal cleavage
at the 2K-4B site requires a prior NS3 protease-mediated cleavage at
the 4A-2K site. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin,
releasing the mature small envelope protein M, and peptide pr. This
cleavage is incomplete as up to 30% of viral particles still carry
uncleaved prM. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: [Envelope protein E]: N-glycosylated.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: [Non-structural protein 1]: N-glycosylated. 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}.
-!- PTM: [RNA-directed RNA polymerase NS5]: Sumoylation of RNA-directed RNA
polymerase NS5 increases NS5 protein stability allowing proper viral
RNA replication. {ECO:0000250|UniProtKB:P29990}.
-!- 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=Virus Pathogen Resource;
URL="https://www.viprbrc.org/brc/home.spg?decorator=flavi_dengue";
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EMBL; X15434; CAA33475.1; -; Genomic_RNA.
EMBL; DQ181805; ABA61184.1; -; Genomic_RNA.
PIR; S06747; S06747.
PDB; 1P58; EM; 9.50 A; A/B/C=281-775.
PDB; 2M9P; NMR; -; A=1391-1654.
PDB; 2M9Q; NMR; -; A=1391-1654.
PDB; 3C6D; EM; 12.50 A; D/E/F=115-195.
PDBsum; 1P58; -.
PDBsum; 2M9P; -.
PDBsum; 2M9Q; -.
PDBsum; 3C6D; -.
BMRB; P14337; -.
SMR; P14337; -.
MEROPS; S07.001; -.
ABCD; P14337; 1 sequenced antibody.
EvolutionaryTrace; P14337; -.
PRO; PR:P14337; -.
Proteomes; UP000007195; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0033650; C:host cell mitochondrion; 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:0044385; C:integral to membrane of host cell; 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:0140603; F:ATP hydrolysis activity; IEA:RHEA.
GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; 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:UniProtKB-EC.
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; ISS:UniProtKB.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
GO; GO:0039545; P:suppression by virus of host MAVS 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:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd20761; capping_2-OMTase_Flaviviridae; 1.
CDD; cd12149; Flavi_E_C; 1.
Gene3D; 1.10.10.930; -; 1.
Gene3D; 1.10.8.970; -; 1.
Gene3D; 1.20.1280.260; -; 1.
Gene3D; 2.40.10.10; -; 1.
Gene3D; 2.60.260.50; -; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 2.60.98.10; -; 1.
Gene3D; 3.30.387.10; -; 1.
Gene3D; 3.30.67.10; -; 1.
Gene3D; 3.40.50.300; -; 2.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR043502; DNA/RNA_pol_sf.
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; IPR043504; Peptidase_S1_PA_chymotrypsin.
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; SSF56672; SSF56672; 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; 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 mitochondrion; 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 MAVS by virus; Inhibition of host RLR pathway by virus;
Inhibition of host STAT2 by virus; Inhibition of host TYK2 by virus;
Ion channel; Ion transport; 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;
Transport; Ubl conjugation; Viral attachment to host cell;
Viral envelope protein; Viral immunoevasion; Viral ion channel;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus endocytosis by host; Virus entry into host cell; Zinc.
CHAIN 1..3391
/note="Genome polyprotein"
/id="PRO_0000405210"
CHAIN 1..100
/note="Capsid protein C"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000267992"
PROPEP 101..114
/note="ER anchor for the capsid protein C, removed in
mature form by serine protease NS3"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000267993"
CHAIN 115..280
/note="Protein prM"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000267994"
CHAIN 115..205
/note="Peptide pr"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000267995"
CHAIN 206..280
/note="Small envelope protein M"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000267996"
CHAIN 281..775
/note="Envelope protein E"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000037914"
CHAIN 776..1127
/note="Non-structural protein 1"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000267997"
CHAIN 1128..1345
/note="Non-structural protein 2A"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000267999"
CHAIN 1346..1475
/note="Serine protease subunit NS2B"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000268000"
CHAIN 1476..2093
/note="Serine protease NS3"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000268001"
CHAIN 2094..2220
/note="Non-structural protein 4A"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000268002"
PEPTIDE 2221..2243
/note="Peptide 2k"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000268003"
CHAIN 2244..2491
/note="Non-structural protein 4B"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000268004"
CHAIN 2492..3391
/note="RNA-directed RNA polymerase NS5"
/evidence="ECO:0000250|UniProtKB:P29990"
/id="PRO_0000268005"
TOPO_DOM 1..101
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 102..122
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 123..238
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 239..259
/note="Helical"
/evidence="ECO:0000305|PubMed:14528291"
TOPO_DOM 260..265
/note="Cytoplasmic"
/evidence="ECO:0000305|PubMed:14528291"
TRANSMEM 266..280
/note="Helical"
/evidence="ECO:0000305|PubMed:14528291"
TOPO_DOM 281..725
/note="Extracellular"
/evidence="ECO:0000305|PubMed:14528291"
TRANSMEM 726..746
/note="Helical"
/evidence="ECO:0000305|PubMed:14528291"
TOPO_DOM 747..752
/note="Cytoplasmic"
/evidence="ECO:0000305|PubMed:14528291"
TRANSMEM 753..773
/note="Helical"
/evidence="ECO:0000305|PubMed:14528291"
TOPO_DOM 774..1195
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 1196..1220
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1221..1226
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 1227..1245
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1246..1269
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 1270..1290
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1291
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 1292..1310
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1311..1317
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 1318..1338
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1339..1346
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 1347..1367
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1368..1370
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 1371..1391
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1392..1447
/note="Cytoplasmic"
/evidence="ECO:0000255"
INTRAMEM 1448..1468
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1469..2147
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 2148..2168
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 2169..2170
/note="Lumenal"
/evidence="ECO:0000255"
INTRAMEM 2171..2191
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 2192
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 2193..2213
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 2214..2228
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 2229..2249
/note="Helical; Note=Signal for NS4B"
/evidence="ECO:0000255"
TOPO_DOM 2250..2274
/note="Lumenal"
/evidence="ECO:0000255"
INTRAMEM 2275..2295
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 2296..2316
/note="Lumenal"
/evidence="ECO:0000255"
INTRAMEM 2317..2337
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 2338..2347
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 2348..2368
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 2369..2413
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 2414..2434
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 2435..2459
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 2460..2480
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 2481..3391
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 1476..1653
/note="Peptidase S7"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
DOMAIN 1655..1811
/note="Helicase ATP-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
DOMAIN 1821..1988
/note="Helicase C-terminal"
DOMAIN 2493..2755
/note="mRNA cap 0-1 NS5-type MT"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
DOMAIN 3020..3169
/note="RdRp catalytic"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
NP_BIND 1668..1675
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
REGION 1..15
/note="Interaction with host EXOC1"
/evidence="ECO:0000250|UniProtKB:P17763"
REGION 37..72
/note="Hydrophobic; homodimerization of capsid protein C"
/evidence="ECO:0000250|UniProtKB:P29990"
REGION 378..391
/note="Fusion peptide"
/evidence="ECO:0000250|UniProtKB:P14336"
REGION 1398..1437
/note="Interacts with and activates NS3 protease"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00859"
REGION 1659..1662
/note="Important for RNA-binding"
/evidence="ECO:0000250|UniProtKB:P14340"
MOTIF 1759..1762
/note="DEAH box"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
MOTIF 2568..2571
/note="SUMO-interacting motif"
/evidence="ECO:0000250|UniProtKB:P29990"
ACT_SITE 1526
/note="Charge relay system; for serine protease NS3
activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
ACT_SITE 1550
/note="Charge relay system; for serine protease NS3
activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
ACT_SITE 1610
/note="Charge relay system; for serine protease NS3
activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
ACT_SITE 2552
/note="For 2'-O-MTase activity"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
ACT_SITE 2637
/note="For 2'-O-MTase activity"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
ACT_SITE 2672
/note="For 2'-O-MTase activity"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
ACT_SITE 2708
/note="For 2'-O-MTase activity"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
METAL 2929
/note="Zinc 1"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
METAL 2933
/note="Zinc 1; via tele nitrogen"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
METAL 2938
/note="Zinc 1"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
METAL 2941
/note="Zinc 1"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
METAL 3203
/note="Zinc 2; via tele nitrogen"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
METAL 3219
/note="Zinc 2"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
METAL 3338
/note="Zinc 2"
/evidence="ECO:0000250|UniProtKB:Q6YMS4"
BINDING 2547
/note="S-adenosyl-L-methionine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
BINDING 2577
/note="S-adenosyl-L-methionine; via carbonyl oxygen"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
BINDING 2578
/note="S-adenosyl-L-methionine; via carbonyl oxygen"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
BINDING 2595
/note="S-adenosyl-L-methionine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
BINDING 2596
/note="S-adenosyl-L-methionine; via carbonyl oxygen"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
BINDING 2622
/note="S-adenosyl-L-methionine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
BINDING 2623
/note="S-adenosyl-L-methionine; via carbonyl oxygen"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
BINDING 2638
/note="S-adenosyl-L-methionine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
BINDING 2710
/note="S-adenosyl-L-methionine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 100..101
/note="Cleavage; by viral protease NS3"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 114..115
/note="Cleavage; by host signal peptidase"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 205..206
/note="Cleavage; by host furin"
/evidence="ECO:0000250|UniProtKB:P29990, ECO:0000255"
SITE 280..281
/note="Cleavage; by host signal peptidase"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 775..776
/note="Cleavage; by host signal peptidase"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 1127..1128
/note="Cleavage; by host"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 1345..1346
/note="Cleavage; by viral protease NS3"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 1475..1476
/note="Cleavage; by autolysis"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 1932
/note="Involved in NS3 ATPase and RTPase activities"
/evidence="ECO:0000250|UniProtKB:P14335"
SITE 1935
/note="Involved in NS3 ATPase and RTPase activities"
/evidence="ECO:0000250|UniProtKB:P14335"
SITE 2093..2094
/note="Cleavage; by autolysis"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 2220..2221
/note="Cleavage; by viral protease NS3"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 2243..2244
/note="Cleavage; by host signal peptidase"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 2491..2492
/note="Cleavage; by viral protease NS3"
/evidence="ECO:0000250|UniProtKB:P29990"
SITE 2505
/note="mRNA cap binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2508
/note="mRNA cap binding; via carbonyl oxygen"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2509
/note="mRNA cap binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2511
/note="mRNA cap binding; via carbonyl oxygen"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2516
/note="mRNA cap binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2520
/note="mRNA cap binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2552
/note="Essential for 2'-O-methyltransferase activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2637
/note="Essential for 2'-O-methyltransferase and N-7
methyltransferase activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2641
/note="mRNA cap binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2672
/note="Essential for 2'-O-methyltransferase activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2703
/note="mRNA cap binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2705
/note="mRNA cap binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
SITE 2708
/note="Essential for 2'-O-methyltransferase activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
MOD_RES 2547
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P03314"
CARBOHYD 183
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 347
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 433
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 905
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 982
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 1134
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 2301
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 2305
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
CARBOHYD 2457
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
DISULFID 283..310
/evidence="ECO:0000250|UniProtKB:P17763"
DISULFID 340..401
/evidence="ECO:0000250|UniProtKB:P17763"
DISULFID 354..385
/evidence="ECO:0000250|UniProtKB:P17763"
DISULFID 372..396
/evidence="ECO:0000250|UniProtKB:P17763"
DISULFID 465..565
/evidence="ECO:0000250|UniProtKB:P17763"
DISULFID 582..613
/evidence="ECO:0000250|UniProtKB:P17763"
DISULFID 779..790
/evidence="ECO:0000250|UniProtKB:P17763"
DISULFID 830..918
/evidence="ECO:0000250|UniProtKB:P17763"
DISULFID 954..998
/evidence="ECO:0000250|UniProtKB:P17763"
DISULFID 1055..1104
/evidence="ECO:0000250|UniProtKB:P17763"
DISULFID 1066..1088
/evidence="ECO:0000250|UniProtKB:P17763"
DISULFID 1087..1091
/evidence="ECO:0000250|UniProtKB:P17763"
VARIANT 291
/note="F -> L (in strain: Isolate Malaysia M1)"
VARIANT 357
/note="Q -> L (in strain: Isolate Malaysia M1)"
VARIANT 370
/note="F -> L (in strain: Isolate Malaysia M1)"
VARIANT 444
/note="V -> I (in strain: Isolate Malaysia M1)"
VARIANT 540
/note="M -> I (in strain: Isolate Malaysia M1)"
VARIANT 590
/note="K -> E (in strain: Isolate Malaysia M1)"
VARIANT 647
/note="I -> V (in strain: Isolate Malaysia M1)"
VARIANT 687
/note="R -> I (in strain: Isolate Malaysia M1)"
VARIANT 696
/note="G -> R (in strain: Isolate Malaysia M1)"
VARIANT 773
/note="V -> C (in strain: Isolate Malaysia M1)"
STRAND 1396..1402
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1411..1414
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1418..1420
/evidence="ECO:0007829|PDB:2M9Q"
STRAND 1422..1424
/evidence="ECO:0007829|PDB:2M9P"
TURN 1425..1427
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1428..1433
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1453..1455
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1483..1485
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1486..1488
/evidence="ECO:0007829|PDB:2M9Q"
STRAND 1496..1504
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1507..1517
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1520..1525
/evidence="ECO:0007829|PDB:2M9P"
TURN 1526..1529
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1533..1535
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1538..1540
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1543..1546
/evidence="ECO:0007829|PDB:2M9P"
TURN 1547..1550
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1551..1558
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1570..1575
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1581..1587
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1589..1592
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1597..1602
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1612..1616
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1623..1631
/evidence="ECO:0007829|PDB:2M9P"
TURN 1632..1634
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1635..1641
/evidence="ECO:0007829|PDB:2M9P"
STRAND 1647..1650
/evidence="ECO:0007829|PDB:2M9P"
SEQUENCE 3391 AA; 379394 MW; 5325B9EEB03F40F9 CRC64;
MNNQRKKAKN TPFNMLKRER NRVSTVQQLT KRFSLGMLQG RGPLKLFMAL VAFLRFLTIP
PTAGILKRWG TIKKSKAINV LRGFRKEIGR MLNILNRRRR SAGMIIMLIP TVMAFHLTTR
NGEPHMIVSR QEKGKSLLFK TEDGVNMCTL MAMDLGELCE DTITYKCPLL RQNEPEDIDC
WCNSTSTWVT YGTCTTTGEH RREKRSVALV PHVGMGLETR TETWMSSEGA WKHAQRIETW
ILRHPGFTIM AAILAYTIGT THFQRALIFI LLTAVAPSMT MRCIGISNRD FVEGVSGGSW
VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC IEAKLTNTTT ESRCPTQGEP
SLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFT CKKNMEGKIV QPENLEYTIV
VTPHSGEEHA VGNDTGKHGK EIKVTPQSSI TEAELTGYGT VTMECSPRTG LDFNEMVLLQ
MENKAWLVHR QWFLDLPLPW LPGADTQGSN WIQKETLVTF KNPHAKKQDV VVLGSQEGAM
HTALTGATEI QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS MCTGKFKVVK EIAETQHGTI
VIRVQYEGDG SPCKIPFEIM DLEKRHVLGR LITVNPIVTE KDSPVNIEAE PPFGDSYIII
GVEPGQLKLN WFKKGSSIGQ MFETTMRGAK RMAILGDTAW DFGSLGGVFT SIGKALHQVF
GAIYGAAFSG VSWTMKILIG VIITWIGMNS RSTSLSVSLV LVGIVTLYLG VMVQADSGCV
VSWKNKELKC GSGIFITDNV HTWTEQYKFQ PESPSKLASA IQKAQEEGIC GIRSVTRLEN
LMWKQITPEL NHILAENEVK LTIMTGDIKG IMQAGKRSLR PQPTELKYSW KTWGKAKMLS
TESHNQTFLI DGPETAECPN TNRAWNSLEV EDYGFGVFTT NIWLKLKEKQ DAFCDSKLMS
AAIKDNRAVH ADMGYWIESA LNDTWKIEKA SFIEVKNCHW PKSHTLWSNG VLESEMIIPK
NLAGPVSQHN YRPGYHTQIA GPWHLGKLEM DFDFCDGTTV VVTEDCGNRG PSLRTTTASG
KLITEWCCRS CTLPPLRYRG EDGCWYGMEI RPLKEKEENL VNSLVTAGHG QVDNFSLGVL
GMALFLEEML RTRVGTKHAI LLVAVSFVTL ITGNMSFKDL GRVVVMVGAT MTDDIGMGVT
YLALLAAFKV RPTFAAGLLL RKLTSKELMM TTIGIVLLSQ STIPETILEL TDALALGMMV
LKMVRNMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTILA VVSVSPLLLT SSQQKTDWIP
LALTIKGLNP TAIFLTTLSR TSKKRSWPLN EAIMAVGMVS ILASSLLKND IPMTGPLVAG
GLLTVCYVLT GRSADLELER AADVKWEDQA EISGSSPILS ITISEDGSMS IKNEEEEQTL
TILIRTGLLV ISGLFPVSIP ITAAAWYLWE VKKQRAGVLW DVPSPPPMGK AELEDGAYRI
KQKGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHKGKRI EPSWADVKKD LISYGGGWKL
EGEWKEGEEV QVLALEPGKN PRAVQTKPGL FKTNAGTIGA VSLDFSPGTS GSPIIDKKGK
VVGLYGNGVV TRSGAYVSAI AQTEKSIEDN PEIEDDIFRK RRLTIMDLHP GAGKTKRYLP
AIVREAIKRG LRTLILAPTR VVAAEMEEAL RGLPIRYQTP AIRAEHTGRE IVDLMCHATF
TMRLLSPVRV PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT ATPPGSRDPF
PQSNAPIIDE EREIPERSWN SGHEWVTDFK GKTVWFVPSI KAGNDIAACL RKNGKKVIQL
SRKTFDSEYV KTRTNDWDFV VTTDISEMGA NFKAERVIDP RRCMKPVILT DGEERVILAG
PMPVTHSSAA QRRGRIGRNP KNENDQYIYM GEPLENDEDC AHWKEAKMLL DNINTPEGII
PSMFEPEREK VDAIDGEYRL RGEARKTFVD LMRRGDLPVW LAYKVAAEGI NYADRRWCFD
GIKNNQILEE NVEVEIWTKE GERKKLKPRW LDARIYSDPL ALKEFKEFAA GRKSLTLNLI
TEMGRLPTFM TQKTRDALDN LAVLHTAEAG GRAYNHALSE LPETLETLLL LTLLATVTGG
IFLFLMSGRG IGKMTLGMCC IITASVLLWY AQIQPHWIAA SIILEFFLIV LLIPEPEKQR
TPQDNQLTYV VIAILTVVAA TMANEMGFLE KTKKDLGLGS IATQQPESNI LDIDLRPASA
WTLYAVATTF VTPMLRHSIE NSSVNVSLTA IANQATVLMG LGKGWPLSKM DIGVPLLAIG
CYSQVNPITL TAALLLLVAH YAIIGPGLQA KATREAQKRA AAGIMKNPTV DGITVIDLDP
IPYDPKFEKQ LGQVMLLVLC VTQVLMMRTT WALCEALTLA TGPISTLWEG NPGRFWNTTI
AVSMANIFRG SYLAGAGLLF SIMKNTTNTR RGTGNIGETL GEKWKSRLNA LGKSEFQIYK
KSGIQEVDRT LAKEGIKRGE TDHHAVSRGS AKLRWFVERN MVTPEGKVVD LGCGRGGWSY
YCGGLKNVRE VKGLTKGGPG HEEPIPMSTY GWNLVRLQSG VDVFFIPPEK CDTLLCDIGE
SSPSPTVEAG RTLRVLNLVE NWLNNNTQFC IKVLNPYMPS VIEKMETLQR KYGGALVRNP
LSRNSTHEMY WVSNASGNIV SSVNMISRML INRFTMRHKK ATYEPDVDLG SGTRNIGIES
EIPNLDIIGK RIEKIKQEHE TSWHYDQDHP YKTWAYHGSY ETKQTGSASS MVNGVVRLLT
KPWDVLPTVT QMAMTDTTPF GQQRVFKEKV DTRTQEPKEG TKKLMKITAE WLWKELGKKK
TPRMCTREEF TRKVRSNAAL GAIFTDENKW KSAREAVEDS RFWELVDKER NLHLEGKCET
CVYNMMGKRE KKLGEFGKAK GSRAIWYMWL GARFLEFEAL GFLNEDHWFS RENSLSGVEG
EGLHKLGYIL RDVSKKEGGA MYADDTAGWD TRITLEDLKN EEMVTNHMEG EHKKLAEAIF
KLTYQNKVVR VQRPTPRGTV MDIISRRDQR GSGQVGTYGL NTFTNMEAQL IRQMEGEGVF
KNIQHLTVTE EIAVQNWLAR VGRERLSRMA ISGDDCVVKP LDDRFASALT ALNDMGKIRK
DIQQWEPSRG WNDWTQVPFC SHHFHELIMK DGRVLVVPCR NQDELIGRAR ISQGAGWSLR
ETACLGKSYA QMWSLMYFHR RDLRLAANAI CSAVPSHWVP TSRTTWSIHA KHEWMTTEDM
LTVWNRVWIQ ENPWMEDKTP VESWEEIPYL GKREDQWCGS LIGLTSRATW AKNIQAAINQ
VRSLIGNEEY TDYMPSMKRF RREEEEAGVL W


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