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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_DEN4D              Reviewed;        3387 AA.
P09866; Q88661; Q88662; Q88663; Q88664; Q88665; Q88666; Q88667;
Q88668; Q88669; Q88670; Q88671; Q99BK4; Q9DKQ5; Q9DKQ6; Q9DKQ7;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
16-JAN-2004, sequence version 2.
20-JUN-2018, entry version 178.
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 4 (strain Dominica/814669/1981) (DENV-4).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus.
NCBI_TaxID=408871;
NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
NCBI_TaxID=188700; Aedes polynesiensis (Polynesian tiger mosquito).
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND SEQUENCE REVISION.
Yamashiro T., Shameem G., Lai C.-J.;
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Durbin A.P., Karron R.A., Sun W., Vaughn D.W., Reynolds M.J.,
Perreault J.R., Men R.H., Lai C.-J., Elkins W.R., Chanock R.M.,
Murphy B.R., Whitehead S.S.;
"A live attenuated dengue virus type 4 vaccine candidate with a 30
nucleotide deletion in the 3' untranslated region is highly attenuated
and immunogenic in humans.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-777.
PubMed=3022479; DOI=10.1016/0042-6822(86)90169-8;
Zhao B., Mackow E., Buckler-White A., Markoff L., Chancock R.M.,
Lai C.-J., Makino Y.;
"Cloning full-length dengue type 4 viral DNA sequences: analysis of
genes coding for structural proteins.";
Virology 155:77-88(1986).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 775-3387.
PubMed=3039728; DOI=10.1016/0042-6822(87)90458-2;
Mackow E., Makino Y., Zhao B., Zhang Y.M., Markoff L.,
Buckler-White A., Guiler M., Chanock R., Lai C.-J.;
"The nucleotide sequence of dengue type 4 virus: analysis of genes
coding for nonstructural proteins.";
Virology 159:217-228(1987).
[5]
PROTEIN SEQUENCE OF 114-143, AND PROTEOLYTIC PROCESSING (SMALL
ENVELOPE PROTEIN M).
STRAIN=814669;
PubMed=2501515;
Markoff L.;
"In vitro processing of dengue virus structural proteins: cleavage of
the pre-membrane protein.";
J. Virol. 63:3345-3352(1989).
[6]
STRUCTURE BY NMR OF 568-679.
PubMed=17395234; DOI=10.1016/j.virol.2007.02.023;
Volk D.E., Lee Y.C., Li X., Thiviyanathan V., Gromowski G.D., Li L.,
Lamb A.R., Beasley D.W., Barrett A.D., Gorenstein D.G.;
"Solution structure of the envelope protein domain III of dengue-4
virus.";
Virology 364:147-154(2007).
-!- FUNCTION: Capsid protein C: Plays a role in virus budding by
binding to the cell membrane and gathering the viral RNA into a
nucleocapsid that forms the core of a mature virus particle.
During virus entry, may induce genome penetration into the host
cytoplasm after hemifusion induced by the surface proteins. Can
migrate to the cell nucleus where it modulates host functions.
Overcomes the anti-viral effects of host EXOC1 by sequestering and
degrading the latter through the proteasome degradation pathway.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: 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. {ECO:0000250|UniProtKB:P17763,
ECO:0000250|UniProtKB:Q9Q6P4}.
-!- 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: 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.
{ECO:0000250|UniProtKB:P17763}.
-!- CATALYTIC ACTIVITY: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds
in which each of the Xaa can be either Arg or Lys and Yaa can be
either Ser or Ala.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl
5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-
adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-
triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].
{ECO:0000255|PROSITE-ProRule:PRU00924}.
-!- SUBUNIT: Capsid protein C: Homodimer. Interacts (via N-terminus)
with host EXOC1 (via C-terminus); this interaction results in
EXOC1 degradation through the proteasome degradation pathway.
Protein prM: Forms heterodimers with envelope protein E in the
endoplasmic reticulum and Golgi. Envelope protein E: Homodimer; in
the endoplasmic reticulum and Golgi. Interacts with protein prM.
Interacts with non-structural protein 1. Non-structural protein 1:
Homodimer; Homohexamer when secreted. Interacts with envelope
protein E. Non-structural protein 2A: Interacts (via N-terminus)
with serine protease NS3. Non-structural protein 2B: Forms a
heterodimer with serine protease NS3. May form homooligomers.
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. Non-structural protein 4A: Interacts
with host MAVS; this interaction inhibits the synthesis of IFN-
beta. Non-structural protein 4B: Interacts with serine protease
NS3. 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.
{ECO:0000250|UniProtKB:P17763}.
-!- 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,
ECO:0000269|PubMed:2501515}.
-!- 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: Sumoylation of RNA-directed
RNA polymerase NS5 increases NS5 protein stability allowing proper
viral RNA replication. {ECO:0000250|UniProtKB:P29990}.
-!- 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=Virus Pathogen Resource;
URL="http://www.viprbrc.org/brc/home.do?decorator=flavi_dengue";
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EMBL; M14931; AAA42964.2; -; Genomic_RNA.
EMBL; AF326825; AAG45435.1; -; Genomic_RNA.
EMBL; AF326826; AAG45436.1; -; Genomic_RNA.
EMBL; AF326827; AAG45437.1; -; Genomic_RNA.
EMBL; AF326573; AAK01233.1; -; Genomic_RNA.
RefSeq; NP_073286.1; NC_002640.1.
PDB; 2H0P; NMR; -; A=568-679.
PDB; 3UAJ; X-ray; 3.23 A; A/B=280-674.
PDB; 3UC0; X-ray; 2.71 A; A/B=280-329, A/B=414-469, A/B=560-577.
PDB; 3WE1; X-ray; 2.28 A; A/B=575-679.
PDB; 4X42; X-ray; 2.78 A; A/B/C/D/E/F=575-679.
PDB; 5B1C; X-ray; 2.00 A; A/B/C=575-679.
PDBsum; 2H0P; -.
PDBsum; 3UAJ; -.
PDBsum; 3UC0; -.
PDBsum; 3WE1; -.
PDBsum; 4X42; -.
PDBsum; 5B1C; -.
ProteinModelPortal; P09866; -.
SMR; P09866; -.
MINT; P09866; -.
PRIDE; P09866; -.
GeneID; 5075729; -.
KEGG; vg:5075729; -.
OrthoDB; VOG0900007N; -.
EvolutionaryTrace; P09866; -.
PRO; PR:P09866; -.
Proteomes; UP000000274; Genome.
Proteomes; UP000108177; Genome.
Proteomes; UP000115480; Genome.
Proteomes; UP000137425; Genome.
Proteomes; UP000156481; 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:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
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: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: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:0006355; P:regulation of transcription, DNA-templated; 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:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd12149; Flavi_E_C; 1.
Gene3D; 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; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus; ATP-binding;
Capsid protein; Clathrin-mediated endocytosis of virus by host;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; 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 3386 Genome polyprotein.
/FTId=PRO_0000405226.
CHAIN 1 99 Capsid protein C.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000038000.
PROPEP 100 113 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000038001.
CHAIN 114 279 Protein prM.
{ECO:0000269|PubMed:2501515}.
/FTId=PRO_0000308297.
CHAIN 114 204 Peptide pr.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000308298.
CHAIN 205 279 Small envelope protein M.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000038002.
CHAIN 280 774 Envelope protein E.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000038003.
CHAIN 775 1126 Non-structural protein 1.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000038004.
CHAIN 1127 1344 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000038005.
CHAIN 1345 1474 Serine protease subunit NS2B.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000038006.
CHAIN 1475 2092 Serine protease NS3.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000038007.
CHAIN 2093 2219 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000038008.
PEPTIDE 2220 2242 Peptide 2k.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000308300.
CHAIN 2243 2487 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000038009.
CHAIN 2488 3387 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000038010.
TOPO_DOM 1 100 Cytoplasmic. {ECO:0000255}.
TRANSMEM 101 117 Helical. {ECO:0000255}.
TOPO_DOM 118 237 Extracellular. {ECO:0000255}.
TRANSMEM 238 258 Helical. {ECO:0000255}.
TOPO_DOM 259 265 Cytoplasmic. {ECO:0000255}.
TRANSMEM 266 279 Helical. {ECO:0000255}.
TOPO_DOM 280 725 Extracellular. {ECO:0000255}.
TRANSMEM 726 746 Helical. {ECO:0000255}.
TOPO_DOM 747 751 Cytoplasmic. {ECO:0000255}.
TRANSMEM 752 772 Helical. {ECO:0000255}.
TOPO_DOM 773 1194 Extracellular. {ECO:0000255}.
TRANSMEM 1195 1218 Helical. {ECO:0000255}.
TOPO_DOM 1219 1224 Lumenal. {ECO:0000255}.
TRANSMEM 1225 1243 Helical. {ECO:0000255}.
TOPO_DOM 1244 1267 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1268 1288 Helical. {ECO:0000255}.
TOPO_DOM 1289 1289 Lumenal. {ECO:0000255}.
TRANSMEM 1290 1308 Helical. {ECO:0000255}.
TOPO_DOM 1309 1316 Lumenal. {ECO:0000255}.
TRANSMEM 1317 1337 Helical. {ECO:0000255}.
TOPO_DOM 1338 1345 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1346 1366 Helical. {ECO:0000255}.
TOPO_DOM 1367 1369 Lumenal. {ECO:0000255}.
TRANSMEM 1370 1390 Helical. {ECO:0000255}.
TOPO_DOM 1391 1437 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1438 1458 Helical. {ECO:0000255}.
TOPO_DOM 1459 2143 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2144 2164 Helical. {ECO:0000255}.
TOPO_DOM 2165 2169 Lumenal. {ECO:0000255}.
INTRAMEM 2170 2190 Helical. {ECO:0000255}.
TOPO_DOM 2191 2191 Lumenal. {ECO:0000255}.
TRANSMEM 2192 2212 Helical. {ECO:0000255}.
TOPO_DOM 2213 2225 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2226 2246 Helical; Note=Signal for NS4B.
{ECO:0000255}.
TOPO_DOM 2247 2270 Lumenal. {ECO:0000255}.
INTRAMEM 2271 2291 Helical. {ECO:0000255}.
TOPO_DOM 2292 2301 Lumenal. {ECO:0000255}.
INTRAMEM 2302 2322 Helical. {ECO:0000255}.
TOPO_DOM 2323 2343 Lumenal. {ECO:0000255}.
TRANSMEM 2344 2364 Helical. {ECO:0000255}.
TOPO_DOM 2365 2409 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2410 2430 Helical. {ECO:0000255}.
TOPO_DOM 2431 2455 Lumenal. {ECO:0000255}.
TRANSMEM 2456 2476 Helical. {ECO:0000255}.
TOPO_DOM 2477 3387 Cytoplasmic. {ECO:0000255}.
DOMAIN 1475 1652 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1654 1810 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1820 1987 Helicase C-terminal.
DOMAIN 2489 2751 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3016 3166 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1667 1674 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 36 71 Hydrophobic; homodimerization of capsid
protein C.
{ECO:0000250|UniProtKB:P29990}.
REGION 377 390 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
REGION 1397 1436 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
REGION 1658 1661 Important for RNA-binding.
{ECO:0000250|UniProtKB:P14340}.
MOTIF 1758 1761 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 2564 2567 SUMO-interacting motif.
{ECO:0000250|UniProtKB:P29990}.
ACT_SITE 1525 1525 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1549 1549 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1609 1609 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 2548 2548 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2633 2633 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2668 2668 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2704 2704 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2925 2925 Zinc 1. {ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2929 2929 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2934 2934 Zinc 1. {ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2937 2937 Zinc 1. {ECO:0000250|UniProtKB:Q6YMS4}.
METAL 3200 3200 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 3216 3216 Zinc 2. {ECO:0000250|UniProtKB:Q6YMS4}.
METAL 3335 3335 Zinc 2. {ECO:0000250|UniProtKB:Q6YMS4}.
BINDING 2504 2504 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2505 2505 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2507 2507 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2516 2516 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2543 2543 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2573 2573 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2574 2574 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2591 2591 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2592 2592 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2618 2618 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2619 2619 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2637 2637 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2699 2699 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2701 2701 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2706 2706 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 99 100 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P29990}.
SITE 113 114 Cleavage; by host signal peptidase.
{ECO:0000269|PubMed:2501515}.
SITE 204 205 Cleavage; by host furin.
{ECO:0000250|UniProtKB:P29990,
ECO:0000255}.
SITE 279 280 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 774 775 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 1126 1127 Cleavage; by host.
{ECO:0000250|UniProtKB:P29990}.
SITE 1344 1345 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P29990}.
SITE 1474 1475 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P29990}.
SITE 1931 1931 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 1934 1934 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 2092 2093 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P29990}.
SITE 2219 2220 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P29990}.
SITE 2242 2243 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 2487 2488 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P29990}.
SITE 2512 2512 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2548 2548 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2633 2633 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2634 2634 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2668 2668 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2704 2704 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
MOD_RES 2543 2543 Phosphoserine.
{ECO:0000250|UniProtKB:P03314}.
CARBOHYD 182 182 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 346 346 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 432 432 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 904 904 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 981 981 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2297 2297 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2301 2301 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2453 2453 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 282 309 {ECO:0000250|UniProtKB:P17763}.
DISULFID 339 400 {ECO:0000250|UniProtKB:P17763}.
DISULFID 353 384 {ECO:0000250|UniProtKB:P17763}.
DISULFID 371 395 {ECO:0000250|UniProtKB:P17763}.
DISULFID 464 564 {ECO:0000250|UniProtKB:P17763}.
DISULFID 581 612 {ECO:0000250|UniProtKB:P17763}.
DISULFID 778 789 {ECO:0000250|UniProtKB:P17763}.
DISULFID 829 917 {ECO:0000250|UniProtKB:P17763}.
DISULFID 953 997 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1054 1103 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1065 1087 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1086 1090 {ECO:0000250|UniProtKB:P17763}.
CONFLICT 780 780 A -> V (in Ref. 2; AAG45436/AAK01233).
{ECO:0000305}.
CONFLICT 1418 1418 I -> V (in Ref. 2; AAG45435).
{ECO:0000305}.
CONFLICT 1909 1909 P -> T (in Ref. 2; AAK01233).
{ECO:0000305}.
CONFLICT 2032 2032 K -> E (in Ref. 2; AAG45435).
{ECO:0000305}.
CONFLICT 2351 2351 V -> A (in Ref. 2; AAG45436).
{ECO:0000305}.
CONFLICT 2354 2354 L -> F (in Ref. 2; AAG45437).
{ECO:0000305}.
CONFLICT 2510 2510 K -> R (in Ref. 2; AAK01233).
{ECO:0000305}.
CONFLICT 2736 2736 K -> R (in Ref. 2; AAG45436).
{ECO:0000305}.
STRAND 286 292 {ECO:0000244|PDB:3UAJ}.
STRAND 298 304 {ECO:0000244|PDB:3UAJ}.
STRAND 309 314 {ECO:0000244|PDB:3UAJ}.
STRAND 317 328 {ECO:0000244|PDB:3UAJ}.
STRAND 333 351 {ECO:0000244|PDB:3UAJ}.
HELIX 362 364 {ECO:0000244|PDB:3UAJ}.
STRAND 369 379 {ECO:0000244|PDB:3UAJ}.
TURN 380 383 {ECO:0000244|PDB:3UAJ}.
STRAND 388 408 {ECO:0000244|PDB:3UAJ}.
STRAND 411 413 {ECO:0000244|PDB:3UAJ}.
STRAND 415 422 {ECO:0000244|PDB:3UAJ}.
STRAND 439 444 {ECO:0000244|PDB:3UAJ}.
STRAND 449 454 {ECO:0000244|PDB:3UAJ}.
TURN 455 457 {ECO:0000244|PDB:3UAJ}.
STRAND 458 467 {ECO:0000244|PDB:3UAJ}.
HELIX 472 474 {ECO:0000244|PDB:3UAJ}.
STRAND 475 480 {ECO:0000244|PDB:3UAJ}.
STRAND 483 488 {ECO:0000244|PDB:3UAJ}.
HELIX 489 493 {ECO:0000244|PDB:3UAJ}.
HELIX 513 515 {ECO:0000244|PDB:3UAJ}.
STRAND 517 519 {ECO:0000244|PDB:3UAJ}.
STRAND 529 531 {ECO:0000244|PDB:3UAJ}.
HELIX 536 542 {ECO:0000244|PDB:3UAJ}.
STRAND 544 546 {ECO:0000244|PDB:3UAJ}.
STRAND 548 550 {ECO:0000244|PDB:3UAJ}.
STRAND 552 554 {ECO:0000244|PDB:3UAJ}.
STRAND 561 567 {ECO:0000244|PDB:3UAJ}.
STRAND 570 572 {ECO:0000244|PDB:2H0P}.
TURN 574 577 {ECO:0000244|PDB:3UAJ}.
STRAND 585 593 {ECO:0000244|PDB:5B1C}.
STRAND 595 597 {ECO:0000244|PDB:3WE1}.
STRAND 599 605 {ECO:0000244|PDB:5B1C}.
STRAND 607 609 {ECO:0000244|PDB:5B1C}.
STRAND 611 613 {ECO:0000244|PDB:5B1C}.
STRAND 616 619 {ECO:0000244|PDB:5B1C}.
STRAND 621 623 {ECO:0000244|PDB:3WE1}.
STRAND 632 634 {ECO:0000244|PDB:5B1C}.
STRAND 636 639 {ECO:0000244|PDB:2H0P}.
STRAND 643 648 {ECO:0000244|PDB:5B1C}.
STRAND 652 661 {ECO:0000244|PDB:5B1C}.
HELIX 662 664 {ECO:0000244|PDB:5B1C}.
STRAND 666 672 {ECO:0000244|PDB:5B1C}.
SEQUENCE 3387 AA; 378385 MW; 0CE81B6E7DEFDB5E CRC64;
MNQRKKVVRP PFNMLKRERN RVSTPQGLVK RFSTGLFSGK GPLRMVLAFI TFLRVLSIPP
TAGILKRWGQ LKKNKAIKIL IGFRKEIGRM LNILNGRKRS TITLLCLIPT VMAFSLSTRD
GEPLMIVAKH ERGRPLLFKT TEGINKCTLI AMDLGEMCED TVTYKCPLLV NTEPEDIDCW
CNLTSTWVMY GTCTQSGERR REKRSVALTP HSGMGLETRA ETWMSSEGAW KHAQRVESWI
LRNPGFALLA GFMAYMIGQT GIQRTVFFVL MMLVAPSYGM RCVGVGNRDF VEGVSGGAWV
DLVLEHGGCV TTMAQGKPTL DFELTKTTAK EVALLRTYCI EASISNITTA TRCPTQGEPY
LKEEQDQQYI CRRDVVDRGW GNGCGLFGKG GVVTCAKFSC SGKITGNLVQ IENLEYTVVV
TVHNGDTHAV GNDTSNHGVT AMITPRSPSV EVKLPDYGEL TLDCEPRSGI DFNEMILMKM
KKKTWLVHKQ WFLDLPLPWT AGADTSEVHW NYKERMVTFK VPHAKRQDVT VLGSQEGAMH
SALAGATEVD SGDGNHMFAG HLKCKVRMEK LRIKGMSYTM CSGKFSIDKE MAETQHGTTV
VKVKYEGAGA PCKVPIEIRD VNKEKVVGRI ISSTPLAENT NSVTNIELEP PFGDSYIVIG
VGNSALTLHW FRKGSSIGKM FESTYRGAKR MAILGETAWD FGSVGGLFTS LGKAVHQVFG
SVYTTMFGGV SWMIRILIGF LVLWIGTNSR NTSMAMTCIA VGGITLFLGF TVQADMGCVA
SWSGKELKCG SGIFVVDNVH TWTEQYKFQP ESPARLASAI LNAHKDGVCG IRSTTRLENV
MWKQITNELN YVLWEGGHDL TVVAGDVKGV LTKGKRALTP PVSDLKYSWK TWGKAKIFTP
EARNSTFLID GPDTSECPNE RRAWNSLEVE DYGFGMFTTN IWMKFREGSS EVCDHRLMSA
AIKDQKAVHA DMGYWIESSK NQTWQIEKAS LIEVKTCLWP KTHTLWSNGV LESQMLIPKS
YAGPFSQHNY RQGYATQTVG PWHLGKLEID FGECPGTTVT IQEDCDHRGP SLRTTTASGK
LVTQWCCRSC TMPPLRFLGE DGCWYGMEIR PLSEKEENMV KSQVTAGQGT SETFSMGLLC
LTLFVEECLR RRVTRKHMIL VVVITLCAII LGGLTWMDLL RALIMLGDTM SGRIGGQIHL
AIMAVFKMSP GYVLGVFLRK LTSRETALMV IGMAMTTVLS IPHDLMELID GISLGLILLK
IVTQFDNTQV GTLALSLTFI RSTMPLVMAW RTIMAVLFVV TLIPLCRTSC LQKQSHWVEI
TALILGAQAL PVYLMTLMKG ASRRSWPLNE GIMAVGLVSL LGSALLKNDV PLAGPMVAGG
LLLAAYVMSG SSADLSLEKA ANVQWDEMAD ITGSSPIIEV KQDEDGSFSI RDVEETNMIT
LLVKLALITV SGLYPLAIPV TMTLWYMWQV KTQRSGALWD VPSPAATKKA ALSEGVYRIM
QRGLFGKTQV GVGIHMEGVF HTMWHVTRGS VICHETGRLE PSWADVRNDM ISYGGGWRLG
DKWDKEEDVQ VLAIEPGKNP KHVQTKPGLF KTLTGEIGAV TLDFKPGTSG SPIINRKGKV
IGLYGNGVVT KSGDYVSAIT QAERIGEPDY EVDEDIFRKK RLTIMDLHPG AGKTKRILPS
IVREALKRRL RTLILAPTRV VAAEMEEALR GLPIRYQTPA VKSEHTGREI VDLMCHATFT
TRLLSSTRVP NYNLIVMDEA HFTDPSSVAA RGYISTRVEM GEAAAIFMTA TPPGATDPFP
QSNSPIEDIE REIPERSWNT GFDWITDYQG KTVWFVPSIK AGNDIANCLR KSGKKVIQLS
RKTFDTEYPK TKLTDWDFVV TTDISEMGAN FRAGRVIDPR RCLKPVILPD GPERVILAGP
IPVTPASAAQ RRGRIGRNPA QEDDQYVFSG DPLKNDEDHA HWTEAKMLLD NIYTPEGIIP
TLFGPEREKT QAIDGEFRLR GEQRKTFVEL MRRGDLPVWL SYKVASAGIS YKDREWCFTG
ERNNQILEEN MEVEIWTREG EKKKLRPRWL DARVYADPMA LKDFKEFASG RKSITLDILT
EIASLPTYLS SRAKLALDNI VMLHTTERGG RAYQHALNEL PESLETLMLV ALLGAMTAGI
FLFFMQGKGI GKLSMGLITI AVASGLLWVA EIQPQWIAAS IILEFFLMVL LIPEPEKQRT
PQDNQLIYVI LTILTIIGLI AANEMGLIEK TKTDFGFYQV KTETTILDVD LRPASAWTLY
AVATTILTPM LRHTIENTSA NLSLAAIANQ AAVLMGLGKG WPLHRMDLGV PLLAMGCYSQ
VNPTTLTASL VMLLVHYAII GPGLQAKATR EAQKRTAAGI MKNPTVDGIT VIDLEPISYD
PKFEKQLGQV MLLVLCAGQL LLMRTTWAFC EVLTLATGPI LTLWEGNPGR FWNTTIAVST
ANIFRGSYLA GAGLAFSLIK NAQTPRRGTG TTGETLGEKW KRQLNSLDRK EFEEYKRSGI
LEVDRTEAKS ALKDGSKIKH AVSRGSSKIR WIVERGMVKP KGKVVDLGCG RGGWSYYMAT
LKNVTEVKGY TKGGPGHEEP IPMATYGWNL VKLHSGVDVF YKPTEQVDTL LCDIGESSSN
PTIEEGRTLR VLKMVEPWLS SKPEFCIKVL NPYMPTVIEE LEKLQRKHGG NLVRCPLSRN
STHEMYWVSG ASGNIVSSVN TTSKMLLNRF TTRHRKPTYE KDVDLGAGTR SVSTETEKPD
MTIIGRRLQR LQEEHKETWH YDQENPYRTW AYHGSYEAPS TGSASSMVNG VVKLLTKPWD
VIPMVTQLAM TDTTPFGQQR VFKEKVDTRT PQPKPGTRMV MTTTANWLWA LLGKKKNPRL
CTREEFISKV RSNAAIGAVF QEEQGWTSAS EAVNDSRFWE LVDKERALHQ EGKCESCVYN
MMGKREKKLG EFGRAKGSRA IWYMWLGARF LEFEALGFLN EDHWFGRENS WSGVEGEGLH
RLGYILEEID KKDGDLMYAD DTAGWDTRIT EDDLQNEELI TEQMAPHHKI LAKAIFKLTY
QNKVVKVLRP TPRGAVMDII SRKDQRGSGQ VGTYGLNTFT NMEVQLIRQM EAEGVITQDD
MQNPKGLKER VEKWLKECGV DRLKRMAISG DDCVVKPLDE RFGTSLLFLN DMGKVRKDIP
QWEPSKGWKN WQEVPFCSHH FHKIFMKDGR SLVVPCRNQD ELIGRARISQ GAGWSLRETA
CLGKAYAQMW SLMYFHRRDL RLASMAICSA VPTEWFPTSR TTWSIHAHHQ WMTTEDMLKV
WNRVWIEDNP NMTDKTPVHS WEDIPYLGKR EDLWCGSLIG LSSRATWAKN IHTAITQVRN
LIGKEEYVDY MPVMKRYSAP SESEGVL


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