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 POLG_TBEVW              Reviewed;        3414 AA.
P14336; Q88493;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 4.
22-NOV-2017, entry version 169.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Peptide 2k;
Contains:
RecName: Full=Capsid protein C;
AltName: Full=Core protein;
Contains:
RecName: Full=Protein prM;
Contains:
RecName: Full=Peptide pr;
Contains:
RecName: Full=Small envelope protein M;
AltName: Full=Matrix protein;
Contains:
RecName: Full=Envelope protein E;
Contains:
RecName: Full=Non-structural protein 1;
Short=NS1;
Contains:
RecName: Full=Non-structural protein 2A;
Short=NS2A;
Contains:
RecName: Full=Serine protease subunit NS2B;
AltName: Full=Flavivirin protease NS2B regulatory subunit;
AltName: Full=Non-structural protein 2B;
Contains:
RecName: Full=Serine protease NS3;
EC=3.4.21.91;
EC=3.6.1.15;
EC=3.6.4.13;
AltName: Full=Flavivirin protease NS3 catalytic subunit;
AltName: Full=Non-structural protein 3;
Contains:
RecName: Full=Non-structural protein 4A;
Short=NS4A;
Contains:
RecName: Full=Non-structural protein 4B;
Short=NS4B;
Contains:
RecName: Full=RNA-directed RNA polymerase NS5;
EC=2.1.1.56 {ECO:0000255|PROSITE-ProRule:PRU00924};
EC=2.1.1.57 {ECO:0000255|PROSITE-ProRule:PRU00924};
EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
AltName: Full=Non-structural protein 5;
Tick-borne encephalitis virus European subtype (strain Neudoerfl)
(NEUV) (Neudoerfl virus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; tick-borne encephalitis virus group.
NCBI_TaxID=11088;
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=34615; Ixodes persulcatus (Taiga tick).
NCBI_TaxID=34613; Ixodes ricinus (Common tick).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND SEQUENCE REVISION.
STRAIN=Neudoerfl;
PubMed=7483260; DOI=10.1006/viro.1995.1557;
Wallner G., Mandl C.W., Kunz C., Heinz F.X.;
"The flavivirus 3'-noncoding region: extensive size heterogeneity
independent of evolutionary relationships among strains of tick-borne
encephalitis virus.";
Virology 213:169-178(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-779.
STRAIN=Neudoerfl;
PubMed=3413985; DOI=10.1016/0042-6822(88)90161-4;
Mandl C.W., Heinz F.X., Kunz C.;
"Sequence of the structural proteins of tick-borne encephalitis virus
(western subtype) and comparative analysis with other flaviviruses.";
Virology 166:197-205(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 767-3414.
STRAIN=Neudoerfl;
PubMed=2554575; DOI=10.1016/0042-6822(89)90246-8;
Mandl C.W., Heinz F.X., Stoeckl E., Kunz C.;
"Genome sequence of tick-borne encephalitis virus (Western subtype)
and comparative analysis of nonstructural proteins with other
flaviviruses.";
Virology 173:291-301(1989).
[4]
PROTEIN SEQUENCE OF 2-18 AND 206-209.
PubMed=6305006;
Boege U., Heinz F.X., Wengler G., Kunz C.;
"Amino acid compositions and amino-terminal sequences of the
structural proteins of a flavivirus, European Tick-Borne Encephalitis
virus.";
Virology 126:651-657(1983).
[5]
GLYCOSYLATION (ENVELOPE PROTEIN E).
PubMed=2441520;
Winkler G., Heinz F.X., Kunz C.;
"Studies on the glycosylation of flavivirus E proteins and the role of
carbohydrate in antigenic structure.";
Virology 159:237-243(1987).
[6]
FUSION REGION, AND MUTAGENESIS OF LEU-387.
PubMed=11287576; DOI=10.1128/JVI.75.9.4268-4275.2001;
Allison S.L., Schalich J., Stiasny K., Mandl C.W., Heinz F.X.;
"Mutational evidence for an internal fusion peptide in flavivirus
envelope protein E.";
J. Virol. 75:4268-4275(2001).
[7]
SUBUNIT (CAPSID PROTEIN C).
PubMed=15254179; DOI=10.1128/JVI.78.15.8078-8084.2004;
Kiermayr S., Kofler R.M., Mandl C.W., Messner P., Heinz F.X.;
"Isolation of capsid protein dimers from the tick-borne encephalitis
flavivirus and in vitro assembly of capsid-like particles.";
J. Virol. 78:8078-8084(2004).
[8]
TOPOLOGY (ENVELOPE PROTEIN E).
PubMed=17305426; DOI=10.1371/journal.ppat.0030020;
Stiasny K., Kossl C., Lepault J., Rey F.A., Heinz F.X.;
"Characterization of a structural intermediate of flavivirus membrane
fusion.";
PLoS Pathog. 3:E20-E20(2007).
[9] {ECO:0000244|PDB:1SVB}
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 281-675, AND GLYCOSYLATION
AT ASN-434.
PubMed=7753193; DOI=10.1038/375291a0;
Rey F.A., Heinz F.X., Mandl C., Kunz C., Harrison S.C.;
"The envelope glycoprotein from tick-borne encephalitis virus at 2 A
resolution.";
Nature 375:291-298(1995).
[10] {ECO:0000244|PDB:1N6G, ECO:0000244|PDB:1NA4}
STRUCTURE BY ELECTRON MICROSCOPY (16.00 ANGSTROMS) OF 281-675.
PubMed=12773377; DOI=10.1093/emboj/cdg270;
Zhang Y., Corver J., Chipman P.R., Zhang W., Pletnev S.V., Sedlak D.,
Baker T.S., Strauss J.H., Kuhn R.J., Rossmann M.G.;
"Structures of immature flavivirus particles.";
EMBO J. 22:2604-2613(2003).
-!- 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: Acts as a chaperone for envelope protein E
during intracellular virion assembly by masking and inactivating
envelope protein E fusion peptide. prM is the only viral peptide
matured by host furin in the trans-Golgi network probably to avoid
catastrophic activation of the viral fusion activity in acidic
Golgi compartment prior to virion release. prM-E cleavage is
inefficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Small envelope protein M: May play a role in virus
budding. Exerts cytotoxic effects by activating a mitochondrial
apoptotic pathway through M ectodomain. May display a viroporin
activity. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Envelope protein E: Binds to host cell surface receptor
and mediates fusion between viral and cellular membranes. Envelope
protein is synthesized in the endoplasmic reticulum in the form of
heterodimer with protein prM. They play a role in virion budding
in the ER, and the newly formed immature particle is covered with
60 spikes composed of heterodimer between precursor prM and
envelope protein E. The virion is transported to the Golgi
apparatus where the low pH causes dissociation of PrM-E
heterodimers and formation of E homodimers. prM-E cleavage is
inefficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 1: Involved in immune evasion,
pathogenesis and viral replication. Once cleaved off the
polyprotein, is targeted to three destinations: the viral
replication cycle, the plasma membrane and the extracellular
compartment. Essential for viral replication. Required for
formation of the replication complex and recruitment of other non-
structural proteins to the ER-derived membrane structures.
Excreted as a hexameric lipoparticle that plays a role against
host immune response. Antagonizing the complement function. Binds
to the host macrophages and dendritic cells. Inhibits signal
transduction originating from Toll-like receptor 3 (TLR3).
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- FUNCTION: Non-structural protein 2A: Component of the viral RNA
replication complex that functions in virion assembly and
antagonizes the host immune response.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 2B: Required cofactor for the
serine protease function of NS3 (By similarity). May have
membrane-destabilizing activity and form viroporins (By
similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00859}.
-!- FUNCTION: Serine protease NS3: Displays three enzymatic
activities: serine protease, NTPase and RNA helicase. NS3 serine
protease, in association with NS2B, performs its autocleavage and
cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM,
NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA
helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.
{ECO:0000255|PROSITE-ProRule:PRU00860}.
-!- FUNCTION: Non-structural protein 4A: Regulates the ATPase activity
of the NS3 helicase activity. NS4A allows NS3 helicase to conserve
energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}.
-!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and
is required for the interferon antagonism activity of the latter.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 4B: Induces the formation of ER-
derived membrane vesicles where the viral replication takes place.
Inhibits interferon (IFN)-induced host STAT1 phosphorylation and
nuclear translocation, thereby preventing the establishment of
cellular antiviral state by blocking the IFN-alpha/beta pathway.
Inhibits STAT2 translocation in the nucleus after IFN-alpha
treatment. {ECO:0000250|UniProtKB:Q9Q6P4}.
-!- FUNCTION: RNA-directed RNA polymerase NS5: Replicates the viral
(+) and (-) 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 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 (PubMed:15254179). Interacts
(via N-terminus) with host EXOC1 (via C-terminus); this
interaction results in EXOC1 degradation through the proteasome
degradation pathway (By similarity). Protein prM: Forms
heterodimers with envelope protein E in the endoplasmic reticulum
and Golgi (By similarity). Envelope protein E: Homodimer; in the
endoplasmic reticulum and Golgi (By similarity). Interacts with
protein prM (By similarity). Interacts with non-structural protein
1 (By similarity). Non-structural protein 1: Homodimer;
Homohexamer when secreted. Interacts with envelope protein E (By
similarity). Non-structural protein 2A: Interacts (via N-terminus)
with serine protease NS3 (By similarity). Non-structural protein
2B: Forms a heterodimer with serine protease NS3 (By similarity).
May form homooligomers (By similarity). Serine protease NS3: Forms
a heterodimer with NS2B (By similarity). Interacts with NS4B (By
similarity). Interacts with unphosphorylated RNA-directed RNA
polymerase NS5; this interaction stimulates RNA-directed RNA
polymerase NS5 guanylyltransferase activity (By similarity). Non-
structural protein 4B: Interacts with serine protease NS3 (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). Interacts with serine protease NS3 (By similarity).
Interacts with host SCRIB; this interaction targets NS5 to the
cell membrane periphery and nucleus, thereby allowing efficient
host nuclear STAT1 inhibition. {ECO:0000250|UniProtKB:P17763,
ECO:0000269|PubMed:15254179}.
-!- SUBCELLULAR LOCATION: Capsid protein C: Virion
{ECO:0000250|UniProtKB:P17763}. Host nucleus
{ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear
region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Peptide pr: Secreted
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane
{ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
protein {ECO:0000255}. Note=ER membrane retention is mediated by
the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
-!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
{ECO:0000305}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
protein {ECO:0000255}. Note=ER membrane retention is mediated by
the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
-!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted
{ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
membrane; Peripheral membrane protein; Lumenal side
{ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived
vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host
endoplasmic reticulum membrane; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic
reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860};
Peripheral membrane protein {ECO:0000255|PROSITE-
ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-
ProRule:PRU00860}. Note=Remains non-covalently associated to
serine protease subunit NS2B. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in
RE-associated vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in
RE-derived vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase NS5: Host
endoplasmic reticulum membrane; Peripheral membrane protein;
Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}.
Note=Located in RE-associated vesicles hosting the replication
complex. NS5 protein is mainly localized in the nucleus rather
than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
-!- DOMAIN: The transmembrane domains of the small envelope protein M
and envelope protein E contain an endoplasmic reticulum retention
signal. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Genome polyprotein: Specific enzymatic cleavages in vivo
yield mature proteins. Cleavages in the lumen of endoplasmic
reticulum are performed by host signal peptidase, whereas
cleavages in the cytoplasmic side are performed by serine protease
NS3. Signal cleavage at the 2K-4B site requires a prior NS3
protease-mediated cleavage at the 4A-2K site.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: Protein prM: Cleaved in post-Golgi vesicles by a host furin,
releasing the mature small envelope protein M, and peptide pr.
This cleavage is incomplete as up to 30% of viral particles still
carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Envelope protein E: N-glycosylated.
{ECO:0000269|PubMed:2441520, ECO:0000269|PubMed:7753193}.
-!- 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=Virus Particle ExploreR db; Note=Icosahedral
capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1na4";
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EMBL; U27495; AAA86870.1; -; Genomic_RNA.
PIR; A31052; GNWVNE.
RefSeq; NP_043135.1; NC_001672.1.
PDB; 1N6G; EM; 16.00 A; A/B/C=281-675.
PDB; 1NA4; EM; -; A/B/C=281-675.
PDB; 1SVB; X-ray; 1.90 A; A=281-675.
PDB; 1URZ; X-ray; 2.70 A; A/B/C/D/E/F=281-681.
PDBsum; 1N6G; -.
PDBsum; 1NA4; -.
PDBsum; 1SVB; -.
PDBsum; 1URZ; -.
ProteinModelPortal; P14336; -.
SMR; P14336; -.
TCDB; 1.G.3.1.1; the viral pore-forming membrane fusion protein-3 (vmfp3) family.
GeneID; 1489719; -.
KEGG; vg:1489719; -.
OrthoDB; VOG09000016; -.
EvolutionaryTrace; P14336; -.
Proteomes; UP000007402; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO: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:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd12149; Flavi_E_C; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 3.30.387.10; -; 1.
Gene3D; 3.30.67.10; -; 1.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
InterPro; IPR001122; Flavi_capsidC.
InterPro; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
InterPro; IPR001157; Flavi_NS1.
InterPro; IPR000752; Flavi_NS2A.
InterPro; IPR000487; Flavi_NS2B.
InterPro; IPR000404; Flavi_NS4A.
InterPro; IPR001528; Flavi_NS4B.
InterPro; IPR002535; Flavi_propep.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
InterPro; IPR013756; GlyE_cen_dom_subdom2.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR000208; RNA-dir_pol_flavivirus.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01003; Flavi_capsid; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF02832; Flavi_glycop_C; 1.
Pfam; PF00869; Flavi_glycoprot; 1.
Pfam; PF00948; Flavi_NS1; 1.
Pfam; PF01005; Flavi_NS2A; 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; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
TIGRFAMs; TIGR04240; flavi_E_stem; 1.
PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus; ATP-binding;
Capsid protein; Clathrin-mediated endocytosis of virus by host;
Cleavage on pair of basic residues; Complete proteome;
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 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;
Membrane; Metal-binding; Methyltransferase; mRNA capping;
mRNA processing; Multifunctional enzyme; Nucleotide-binding;
Nucleotidyltransferase; Phosphoprotein; Protease; RNA-binding;
RNA-directed RNA polymerase; S-adenosyl-L-methionine; Secreted;
Serine protease; Suppressor of RNA silencing; Transcription;
Transcription regulation; Transferase; Transmembrane;
Transmembrane helix; Viral attachment to host cell;
Viral envelope protein; Viral immunoevasion;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus endocytosis by host; Virus entry into host cell; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:6305006}.
CHAIN 2 3414 Genome polyprotein.
/FTId=PRO_0000405175.
CHAIN 2 96 Capsid protein C.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037815.
PROPEP 97 117 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000405176.
CHAIN 118 280 Protein prM.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000405177.
CHAIN 118 205 Peptide pr.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037816.
CHAIN 206 280 Small envelope protein M.
{ECO:0000269|PubMed:6305006}.
/FTId=PRO_0000037817.
CHAIN 281 776 Envelope protein E.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037818.
CHAIN 777 1128 Non-structural protein 1.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037819.
CHAIN 1129 1358 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037820.
CHAIN 1359 1489 Serine protease subunit NS2B.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037821.
CHAIN 1490 2110 Serine protease NS3.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037822.
CHAIN 2111 2236 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037823.
PEPTIDE 2237 2259 Peptide 2k.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000405178.
CHAIN 2260 2511 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037824.
CHAIN 2512 3414 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037825.
TOPO_DOM 2 98 Cytoplasmic. {ECO:0000255}.
TRANSMEM 99 119 Helical. {ECO:0000255}.
TOPO_DOM 120 242 Extracellular. {ECO:0000255}.
TRANSMEM 243 260 Helical. {ECO:0000255}.
TOPO_DOM 261 261 Cytoplasmic. {ECO:0000255}.
TRANSMEM 262 280 Helical. {ECO:0000255}.
TOPO_DOM 281 727 Extracellular. {ECO:0000255}.
TRANSMEM 728 748 Helical. {ECO:0000255}.
TOPO_DOM 749 755 Extracellular. {ECO:0000255}.
TRANSMEM 756 776 Helical. {ECO:0000255}.
TOPO_DOM 777 1132 Extracellular. {ECO:0000255}.
TRANSMEM 1133 1153 Helical. {ECO:0000255}.
TOPO_DOM 1154 1158 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1159 1179 Helical. {ECO:0000255}.
TOPO_DOM 1180 1187 Lumenal. {ECO:0000255}.
TRANSMEM 1188 1208 Helical. {ECO:0000255}.
TOPO_DOM 1209 1293 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1294 1314 Helical. {ECO:0000255}.
TOPO_DOM 1315 1327 Lumenal. {ECO:0000255}.
TRANSMEM 1328 1348 Helical. {ECO:0000255}.
TOPO_DOM 1349 1359 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1360 1378 Helical. {ECO:0000255}.
TOPO_DOM 1379 1382 Lumenal. {ECO:0000255}.
TRANSMEM 1383 1403 Helical. {ECO:0000255}.
TOPO_DOM 1404 1454 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1455 1475 Helical. {ECO:0000255}.
TOPO_DOM 1476 2160 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2161 2181 Helical. {ECO:0000255}.
TOPO_DOM 2182 2189 Lumenal. {ECO:0000255}.
INTRAMEM 2190 2210 Helical. {ECO:0000255}.
TOPO_DOM 2211 2211 Lumenal. {ECO:0000255}.
TRANSMEM 2212 2232 Helical. {ECO:0000255}.
TOPO_DOM 2233 2244 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2245 2265 Helical; Note=Signal for NS4B.
{ECO:0000255}.
TOPO_DOM 2266 2299 Lumenal. {ECO:0000255}.
INTRAMEM 2300 2320 Helical. {ECO:0000255}.
TOPO_DOM 2321 2343 Lumenal. {ECO:0000255}.
INTRAMEM 2344 2364 Helical. {ECO:0000255}.
TOPO_DOM 2365 2368 Lumenal. {ECO:0000255}.
TRANSMEM 2369 2389 Helical. {ECO:0000255}.
TOPO_DOM 2390 2432 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2433 2453 Helical. {ECO:0000255}.
TOPO_DOM 2454 2477 Lumenal. {ECO:0000255}.
TRANSMEM 2478 2498 Helical. {ECO:0000255}.
TOPO_DOM 2499 3414 Cytoplasmic. {ECO:0000255}.
DOMAIN 1490 1669 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1675 1831 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1841 2000 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2512 2776 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3040 3189 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1688 1695 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 378 391 Fusion peptide.
{ECO:0000269|PubMed:11287576}.
REGION 1410 1449 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
REGION 2730 2734 Interaction with host SCRIB.
{ECO:0000250|UniProtKB:Q01299}.
MOTIF 1779 1782 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
COMPBIAS 1970 1973 Poly-Asp.
COMPBIAS 2201 2204 Poly-Leu.
ACT_SITE 1543 1543 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1567 1567 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1627 1627 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 2572 2572 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2657 2657 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2694 2694 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2730 2730 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2950 2950 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 2954 2954 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:P14335}.
METAL 2959 2959 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 2962 2962 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 3224 3224 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:P14335}.
METAL 3240 3240 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
METAL 3359 3359 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
BINDING 2524 2524 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2527 2527 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2528 2528 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2530 2530 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2539 2539 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2567 2567 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2597 2597 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2598 2598 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2615 2615 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2616 2616 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2642 2642 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2643 2643 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2661 2661 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2725 2725 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2727 2727 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2732 2732 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 96 97 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P03314}.
SITE 117 118 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P03314}.
SITE 205 206 Cleavage; by host furin.
{ECO:0000250|UniProtKB:P06935}.
SITE 280 281 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P06935}.
SITE 776 777 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P03314}.
SITE 1128 1129 Cleavage; by host.
{ECO:0000250|UniProtKB:P06935}.
SITE 1358 1359 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P06935}.
SITE 1489 1490 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P03314}.
SITE 1949 1949 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 1952 1952 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 2110 2111 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P03314}.
SITE 2236 2237 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P03314}.
SITE 2259 2260 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P03314}.
SITE 2511 2512 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P03314}.
SITE 2535 2535 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2572 2572 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2657 2657 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2658 2658 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2694 2694 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2730 2730 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
MOD_RES 2567 2567 Phosphoserine.
{ECO:0000250|UniProtKB:P03314}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 434 434 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498,
ECO:0000269|PubMed:7753193}.
CARBOHYD 861 861 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 983 983 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 999 999 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 283 310 {ECO:0000269|PubMed:7753193}.
DISULFID 340 401 {ECO:0000250|UniProtKB:P17763}.
DISULFID 340 396 {ECO:0000269|PubMed:7753193}.
DISULFID 354 385 {ECO:0000269|PubMed:7753193}.
DISULFID 372 401 {ECO:0000269|PubMed:7753193}.
DISULFID 372 396 {ECO:0000250|UniProtKB:P17763}.
DISULFID 466 570 {ECO:0000269|PubMed:7753193}.
DISULFID 587 618 {ECO:0000269|PubMed:7753193}.
DISULFID 780 791 {ECO:0000250|UniProtKB:P17763}.
DISULFID 831 920 {ECO:0000250|UniProtKB:P17763}.
DISULFID 955 1000 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1057 1106 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1068 1090 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1089 1093 {ECO:0000250|UniProtKB:P17763}.
MUTAGEN 387 387 L->D: Complete loss of envelope protein E
fusion activity.
{ECO:0000269|PubMed:11287576}.
MUTAGEN 387 387 L->F: About 50% loss of envelope protein
E fusion activity.
{ECO:0000269|PubMed:11287576}.
MUTAGEN 387 387 L->T: About 70% loss of envelope protein
E fusion activity.
{ECO:0000269|PubMed:11287576}.
HELIX 282 285 {ECO:0000244|PDB:1SVB}.
STRAND 290 294 {ECO:0000244|PDB:1SVB}.
STRAND 300 306 {ECO:0000244|PDB:1SVB}.
STRAND 311 315 {ECO:0000244|PDB:1SVB}.
STRAND 318 332 {ECO:0000244|PDB:1SVB}.
STRAND 334 352 {ECO:0000244|PDB:1SVB}.
HELIX 363 366 {ECO:0000244|PDB:1SVB}.
STRAND 370 380 {ECO:0000244|PDB:1SVB}.
HELIX 381 383 {ECO:0000244|PDB:1SVB}.
STRAND 389 401 {ECO:0000244|PDB:1SVB}.
STRAND 406 411 {ECO:0000244|PDB:1SVB}.
TURN 414 416 {ECO:0000244|PDB:1SVB}.
STRAND 418 425 {ECO:0000244|PDB:1SVB}.
STRAND 441 446 {ECO:0000244|PDB:1SVB}.
STRAND 451 455 {ECO:0000244|PDB:1SVB}.
HELIX 457 459 {ECO:0000244|PDB:1SVB}.
STRAND 460 467 {ECO:0000244|PDB:1SVB}.
HELIX 468 470 {ECO:0000244|PDB:1SVB}.
STRAND 477 482 {ECO:0000244|PDB:1SVB}.
STRAND 491 496 {ECO:0000244|PDB:1SVB}.
HELIX 497 501 {ECO:0000244|PDB:1SVB}.
HELIX 518 521 {ECO:0000244|PDB:1SVB}.
STRAND 522 524 {ECO:0000244|PDB:1SVB}.
STRAND 534 536 {ECO:0000244|PDB:1SVB}.
HELIX 541 547 {ECO:0000244|PDB:1SVB}.
TURN 548 550 {ECO:0000244|PDB:1SVB}.
STRAND 553 557 {ECO:0000244|PDB:1SVB}.
STRAND 560 562 {ECO:0000244|PDB:1SVB}.
STRAND 567 573 {ECO:0000244|PDB:1SVB}.
STRAND 591 600 {ECO:0000244|PDB:1SVB}.
STRAND 602 604 {ECO:0000244|PDB:1SVB}.
STRAND 606 612 {ECO:0000244|PDB:1SVB}.
STRAND 616 619 {ECO:0000244|PDB:1SVB}.
STRAND 622 626 {ECO:0000244|PDB:1SVB}.
STRAND 636 641 {ECO:0000244|PDB:1SVB}.
STRAND 643 645 {ECO:0000244|PDB:1SVB}.
STRAND 651 655 {ECO:0000244|PDB:1SVB}.
STRAND 658 665 {ECO:0000244|PDB:1SVB}.
STRAND 668 674 {ECO:0000244|PDB:1SVB}.
SEQUENCE 3414 AA; 378322 MW; 35DBCE014B310B79 CRC64;
MVKKAILKGK GGGPPRRVSK ETATKTRQPR VQMPNGLVLM RMMGILWHAV AGTARNPVLK
AFWNSVPLKQ ATAALRKIKR TVSALMVGLQ KRGKRRSATD WMSWLLVITL LGMTLAATVR
KERDGSTVIR AEGKDAATQV RVENGTCVIL ATDMGSWCDD SLSYECVTID QGEEPVDVDC
FCRNVDGVYL EYGRCGKQEG SRTRRSVLIP SHAQGELTGR GHKWLEGDSL RTHLTRVEGW
VWKNKLLALA MVTVVWLTLE SVVTRVAVLV VLLCLAPVYA SRCTHLENRD FVTGTQGTTR
VTLVLELGGC VTITAEGKPS MDVWLDAIYQ ENPAKTREYC LHAKLSDTKV AARCPTMGPA
TLAEEHQGGT VCKRDQSDRG WGNHCGLFGK GSIVACVKAA CEAKKKATGH VYDANKIVYT
VKVEPHTGDY VAANETHSGR KTASFTISSE KTILTMGEYG DVSLLCRVAS GVDLAQTVIL
ELDKTVEHLP TAWQVHRDWF NDLALPWKHE GAQNWNNAER LVEFGAPHAV KMDVYNLGDQ
TGVLLKALAG VPVAHIEGTK YHLKSGHVTC EVGLEKLKMK GLTYTMCDKT KFTWKRAPTD
SGHDTVVMEV TFSGTKPCRI PVRAVAHGSP DVNVAMLITP NPTIENNGGG FIEMQLPPGD
NIIYVGELSH QWFQKGSSIG RVFQKTKKGI ERLTVIGEHA WDFGSAGGFL SSIGKAVHTV
LGGAFNSIFG GVGFLPKLLL GVALAWLGLN MRNPTMSMSF LLAGGLVLAM TLGVGADVGC
AVDTERMELR CGEGLVVWRE VSEWYDNYAY YPETPGALAS AIKETFEEGS CGVVPQNRLE
MAMWRSSVTE LNLALAEGEA NLTVVVDKFD PTDYRGGVPG LLKKGKDIKV SWKSWGHSMI
WSIPEAPRRF MVGTEGQSEC PLERRKTGVF TVAEFGVGLR TKVFLDFRQE PTHECDTGVM
GAAVKNGMAI HTDQSLWMRS MKNDTGTYIV ELLVTDLRNC SWPASHTIDN ADVVDSELFL
PASLAGPRSW YNRIPGYSEQ VKGPWKYTPI RVIREECPGT TVTINAKCDK RGASVRSTTE
SGKVIPEWCC RACTMPPVTF RTGTDCWYAM EIRPVHDQGG LVRSMVVADN GELLSEGGVP
GIVALFVVLE YIIRRRPSTG TTVVWGGIVV LALLVTGMVR IESLVRYVVA VGITFHLELG
PEIVALMLLQ AVFELRVGLL SAFALRRSLT VREMVTTYFL LLVLELGLPG ASLEEFWKWG
DALAMGALIF RACTAEGKTG AGLLLMALMT QQDVVTVHHG LVCFLSVASA CSVWRLLKGH
REQKGLTWVV PLAGLLGGEG SGIRLLAFWE LSAHRGRRSF SEPLTVVGVM LTLASGMMRH
TSQEALCALA VASFLLLMLV LGTRKMQLVA EWSGCVEWYP ELVNEGGEVS LRVRQDAMGN
FHLTELEKEE RMMAFWLIAG LAASAIHWSG ILGVMGLWTL TEMLRSSRRS DLVFSGQGGR
ERGDRPFEVK DGVYRIFSPG LFWGQNQVGV GYGSKGVLHT MWHVTRGAAL SIDDAVAGPY
WADVREDVVC YGGAWSLEEK WKGETVQVHA FPPGRAHEVH QCQPGELILD TGRKLGAIPI
DLVKGTSGSP ILNAQGVVVG LYGNGLKTNE TYVSSIAQGE AEKSRPNLPQ AVVGTGWTSK
GQITVLDMHP GSGKTHRVLP ELIRQCIDRR LRTLVLAPTR VVLKEMERAL NGKRVRFHSP
AVSDQQAGGA IVDVMCHATY VNRRLLPQGR QNWEVAIMDE AHWTDPHSIA ARGHLYTLAK
ENKCALVLMT ATPPGKSEPF PESNGAITSE ERQIPDGEWR DGFDWITEYE GRTAWFVPSI
AKGGAIARTL RQKGKSVICL NSKTFEKDYS RVRDEKPDFV VTTDISEMGA NLDVSRVIDG
RTNIKPEEVD GKVELTGTRR VTTASAAQRR GRVGRQDGRT DEYIYSGQCD DDDSGLVQWK
EAQILLDNIT TLRGPVATFY GPEQDKMPEV AGHFRLTEEK RKHFRHLLTH CDFTPWLAWH
VAANVSSVTD RSWTWEGPEA NAVDEASGDL VTFRSPNGAE RTLRPVWKDA RMFKEGRDIK
EFVAYASGRR SFGDVLTGMS GVPELLRHRC VSALDVFYTL MHEEPGSRAM RMAERDAPEA
FLTMVEMMVL GLATLGVIWC FVVRTSISRM MLGTLVLLAS LLLLWAGGVG YGNMAGVALI
FYTLLTVLQP EAGKQRSSDD NKLAYFLLTL CSLAGLVAAN EMGFLEKTKA DLSTALWSER
EEPRPWSEWT NVDIQPARSW GTYVLVVSLF TPYIIHQLQT KIQQLVNSAV ASGAQAMRDL
GGGAPFFGVA GHVMTLGVVS LIGATPTSLM VGVGLAALHL AIVVSGLEAE LTQRAHKVFF
SAMVRNPMVD GDVINPFGEG EAKPALYERK MSLVLATVLC LMSVVMNRTV ASITEASAVG
LAAAGQLLRP EADTLWTMPV ACGMSGVVRG SLWGFLPLGH RLWLRASGGR RGGSEGDTLG
DLWKRRLNNC TREEFFVYRR TGILETERDK ARELLRRGET NVGLAVSRGT AKLAWLEERG
YATLKGEVVD LGCGRGGWSY YAASRPAVMS VRAYTIGGKG HEAPKMVTSL GWNLIKFRSG
MDVFSMQPHR ADTVMCDIGE SSPDAAVEGE RTRKVILLME QWKNRNPTAA CVFKVLAPYR
PEVIEALHRF QLQWGGGLVR TPFSRNSTHE MYYSTAVTGN IVNSVNVQSR KLLARFGDQR
GPTKVPELDL GVGTRCVVLA EDKVKEQDVQ ERIRALREQY SETWHMDEEH PYRTWQYWGS
YRTAPTGSAA SLINGVVKLL SWPWNAREDV VRMAMTDTTA FGQQRVFKDK VDTKAQEPQP
GTRVIMRAVN DWILERLAQK SKPRMCSREE FIAKVKSNAA LGAWSDEQNR WASAREAVED
PAFWRLVDEE RERHLMGRCA HCVYNMMGKR EKKLGEFGVA KGSRAIWYMW LGSRFLEFEA
LGFLNEDHWA SRESSGAGVE GISLNYLGWH LKKLSTLNGG LFYADDTAGW DTKVTNADLE
DEEQILRYME GEHKQLATTI MQKAYHAKVV KVARPSRDGG CIMDVITRRD QRGSGQVVTY
ALNTLTNIKV QLIRMMEGEG VIEAADAHNP RLLRVERWLK EHGEERLGRM LVSGDDCVVR
PLDDRFGKAL YFLNDMAKTR KDIGEWEHSA GFSSWEEVPF CSHHFHELVM KDGRTLVVPC
RDQDELVGRA RISPGCGWSV RETACLSKAY GQMWLLSYFH RRDLRTLGLA INSAVPADWV
PTGRTTWSIH ASGAWMTTED MLDVWNRVWI LDNPFMQNKE RVMEWRDVPY LPKAQDMLCS
SLVGRRERAE WAKNIWGAVE KVRKMIGPEK FKDYLSCMDR HDLHWELRLE SSII


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