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Genome polyprotein [Cleaved into: Peptide 2k; 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); Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (NS5)]

 POLG_LANVT              Reviewed;        3414 AA.
P29837;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 2.
23-MAY-2018, entry version 155.
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=NS5;
Langat virus (strain TP21).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; tick-borne encephalitis virus group.
NCBI_TaxID=31638;
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=6935; Ixodida (ticks).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-776.
PubMed=1720591; DOI=10.1016/0042-6822(91)90567-U;
Mandl C.W., Iacono-Connors L.C., Wallner G., Holzmann H., Kunz C.,
Heinz F.X.;
"Sequence of the genes encoding the structural proteins of the low-
virulence tick-borne flaviviruses Langat TP21 and Yelantsev.";
Virology 185:891-895(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 777-3414.
PubMed=1316684; DOI=10.1016/0042-6822(92)90545-Z;
Iacono-Connors L.C., Schmaljohn C.S.;
"Cloning and sequence analysis of the genes encoding the nonstructural
proteins of Langat virus and comparative analysis with other
flaviviruses.";
Virology 188:875-880(1992).
[3]
FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5).
PubMed=16188985; DOI=10.1128/JVI.79.20.12828-12839.2005;
Best S.M., Morris K.L., Shannon J.G., Robertson S.J., Mitzel D.N.,
Park G.S., Boer E., Wolfinbarger J.B., Bloom M.E.;
"Inhibition of interferon-stimulated JAK-STAT signaling by a tick-
borne flavivirus and identification of NS5 as an interferon
antagonist.";
J. Virol. 79:12828-12839(2005).
[4]
STRUCTURE BY NMR OF 580-675, AND DISULFIDE BOND.
PubMed=16731969; DOI=10.1110/ps.051844006;
Mukherjee M., Dutta K., White M.A., Cowburn D., Fox R.O.;
"NMR solution structure and backbone dynamics of domain III of the E
protein of tick-borne Langat flavivirus suggests a potential site for
molecular recognition.";
Protein Sci. 15:1342-1355(2006).
-!- FUNCTION: Capsid protein C: Plays a role in virus budding by
binding to 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 in host
cytoplasm after hemifusion induced by 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. Presumably to
avoid catastrophic activation of the viral fusion activity in
acidic GolGi compartment prior to virion release. prM-E cleavage
is ineficient, 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 extodomain. 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
ineficient, 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 (By similarity). NS5 methylates viral RNA cap at guanine
N-7 and ribose 2'-O positions (By similarity). 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 (PubMed:16188985). Inhibits host
TYK2 and STAT2 phosphorylation, thereby preventing activation of
JAK-STAT signaling pathway (PubMed:16188985).
{ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:16188985}.
-!- 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 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. 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}.
-!- 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: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}.
-!- SIMILARITY: In the N-terminal section; belongs to the class I-like
SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}.
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EMBL; M73835; AAA02740.1; ALT_TERM; Unassigned_RNA.
EMBL; S35365; AAB22165.1; -; Genomic_RNA.
PIR; A42545; A42545.
PDB; 1Z66; NMR; -; A=580-675.
PDB; 2GG1; NMR; -; A=580-675.
PDBsum; 1Z66; -.
PDBsum; 2GG1; -.
ProteinModelPortal; P29837; -.
SMR; P29837; -.
PRIDE; P29837; -.
OrthoDB; VOG0900007N; -.
BRENDA; 3.4.21.91; 9644.
EvolutionaryTrace; P29837; -.
Proteomes; UP000007766; 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: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:0039651; P:induction by virus of host cysteine-type endopeptidase activity involved in apoptotic process; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0039576; P:suppression by virus of host JAK1 activity; IDA:UniProtKB.
GO; GO:0039563; P:suppression by virus of host STAT1 activity; IDA:UniProtKB.
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; IDA:UniProtKB.
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; 1.10.8.970; -; 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; 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; 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;
Activation of host caspases by virus; ATP-binding; Capsid protein;
Clathrin-mediated endocytosis of virus by host;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
Host cytoplasm; Host endoplasmic reticulum; Host membrane;
Host nucleus; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host JAK1 by virus; Inhibition of host STAT1 by virus;
Inhibition of host STAT2 by virus; Inhibition of host TYK2 by virus;
Membrane; Metal-binding; Methyltransferase;
Modulation of host cell apoptosis by virus; mRNA capping;
mRNA processing; Multifunctional enzyme; Nucleotide-binding;
Nucleotidyltransferase; Phosphoprotein; Protease; RNA-binding;
RNA-directed RNA polymerase; S-adenosyl-L-methionine; Secreted;
Serine protease; Suppressor of RNA silencing; Transcription;
Transcription regulation; Transferase; Transmembrane;
Transmembrane helix; Viral attachment to host cell;
Viral envelope protein; Viral immunoevasion;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus endocytosis by host; Virus entry into host cell; Zinc.
CHAIN 1 3414 Genome polyprotein.
/FTId=PRO_0000405129.
CHAIN 1 96 Capsid protein C.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037688.
PROPEP 97 117 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000405130.
CHAIN 118 280 Protein prM.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000405131.
CHAIN 118 205 Peptide pr.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037689.
CHAIN 206 280 Small envelope protein M.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037690.
CHAIN 281 776 Envelope protein E.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037691.
CHAIN 777 1128 Non-structural protein 1.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037692.
CHAIN 1129 1358 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037693.
CHAIN 1359 1489 Serine protease subunit NS2B.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037694.
CHAIN 1490 2110 Serine protease NS3.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037695.
CHAIN 2111 2236 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037696.
PEPTIDE 2237 2259 Peptide 2k.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000405132.
CHAIN 2260 2511 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037697.
CHAIN 2512 3414 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037698.
TOPO_DOM 1 98 Cytoplasmic. {ECO:0000255}.
TRANSMEM 99 117 Helical. {ECO:0000255}.
TOPO_DOM 118 242 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 Cytoplasmic. {ECO:0000255}.
TRANSMEM 756 776 Helical. {ECO:0000255}.
TOPO_DOM 777 1187 Extracellular. {ECO:0000255}.
TRANSMEM 1188 1208 Helical. {ECO:0000255}.
TOPO_DOM 1209 1232 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1233 1253 Helical. {ECO:0000255}.
TOPO_DOM 1254 1267 Lumenal. {ECO:0000255}.
TRANSMEM 1268 1288 Helical. {ECO:0000255}.
TOPO_DOM 1289 1300 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1301 1319 Helical. {ECO:0000255}.
TOPO_DOM 1320 1325 Lumenal. {ECO:0000255}.
TRANSMEM 1326 1346 Helical. {ECO:0000255}.
TOPO_DOM 1347 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 2209 Helical. {ECO:0000255}.
TOPO_DOM 2210 2210 Lumenal. {ECO:0000255}.
TRANSMEM 2211 2231 Helical. {ECO:0000255}.
TOPO_DOM 2232 2238 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2239 2259 Helical; Note=Signal for NS4B.
{ECO:0000255}.
TOPO_DOM 2260 2296 Lumenal. {ECO:0000255}.
INTRAMEM 2297 2315 Helical. {ECO:0000255}.
TOPO_DOM 2316 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:0000250|UniProtKB:P14336}.
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.
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:0000250|UniProtKB:P14336,
ECO:0000255|PROSITE-ProRule:PRU00498}.
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:0000250|UniProtKB:P14336}.
DISULFID 340 401 {ECO:0000250|UniProtKB:P17763}.
DISULFID 340 396 {ECO:0000250|UniProtKB:P14336}.
DISULFID 354 385 {ECO:0000250|UniProtKB:P14336}.
DISULFID 372 401 {ECO:0000250|UniProtKB:P14336}.
DISULFID 372 396 {ECO:0000250|UniProtKB:P17763}.
DISULFID 466 570 {ECO:0000250|UniProtKB:P14336}.
DISULFID 587 618 {ECO:0000269|PubMed:16731969}.
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}.
TURN 589 591 {ECO:0000244|PDB:1Z66}.
STRAND 593 600 {ECO:0000244|PDB:1Z66}.
STRAND 602 611 {ECO:0000244|PDB:1Z66}.
STRAND 616 619 {ECO:0000244|PDB:1Z66}.
STRAND 622 626 {ECO:0000244|PDB:1Z66}.
STRAND 629 633 {ECO:0000244|PDB:2GG1}.
STRAND 643 645 {ECO:0000244|PDB:1Z66}.
STRAND 648 654 {ECO:0000244|PDB:1Z66}.
STRAND 657 665 {ECO:0000244|PDB:1Z66}.
STRAND 668 674 {ECO:0000244|PDB:1Z66}.
SEQUENCE 3414 AA; 378023 MW; 59CB7E95DD70D82E CRC64;
MAGKAVLKGK GGGPPRRASK VAPKKTRQLR VQMPNGLVLM RMLGVLWHAL TGTARSPVLK
AFWKVVPLKQ ATLALRKIKR TVSTLMVGLH RRGSRRTTID WMTPLLITVM LGMCLTATVR
RERDGSMVIR AEGRDAATQV RVENGTCVIL ATDMGSWCDD SLAYECVTID QGEEPVDVDC
FCRGVEKVTL EYGRCGRREG SRSRRSVLIP SHAQRDLTGR GHQWLEGEAV KAHLTRVEGW
VWKNKLFTLS LVMVAWLMVD GLLPRILIVV VALALVPAYA SRCTHLENRD FVTGVQGTTR
LTLVLELGGC VTVTADGKPS LDVWLDSIYQ ESPAQTREYC LHAKLTGTKV AARCPTMGPA
TLPEEHQSGT VCKRDQSDRG WGNHCGLFGK GSIVTCVKFT CEDKKKATGH VYDVNKITYT
IKVEPHTGEF VAANETHSGR KSASFTVSSE KTILTLGDYG DVSLLCRVAS GVDLAQTVVL
ALDKTHEHLP TAWQVHRDWF NDLALPWKHD GAEAWNEAGR LVEFGTPHAV KMDVFNLGDQ
TGVLLKSLAG VPVASIEGTK YHLKSGHVTC EVGLEKLKMK GLTYTVCDKT KFTWKRAPTD
SGHDTVVMEV GFSGTRPCRI PVRAVAHGVP EVNVAMLITP NPTMENNGGG FIEMQLPPGD
NIIYVGDLNH QWFQKGSSIG RVLQKTRKGI ERLTVLGEHA WDFGSVGGVM TSIGRAMHTV
LGGAFNTLLG GVGFLPKILL GVAMAWLGLN MRNPTLSMGF LLSGGLVLAM TLGVGADVGC
AVDTERMELR CGEGLVVWRE VSEWYDNYVF HPETPAVLAS AVQRAYEEEI CGIVPQNRLE
MAMWRSSLVE LNLALAEGEA NLTVVVDKAD PSDYRGGVPG LLNKGKDIKV SWRSWGRSML
WSVPEAPRRF MIGVEGGREC PFARRKTGVM TVAEFGIGLR TKVFMDLRQE LTTECDTGVM
GAAVKNGMAV HTDQSLWMKS IKNDTTVTIV ELIVTDLRNC TWPASHTIDN AGVVNSKLFL
PASLAGPRST YNVIPGYAEQ VRGPWAHTPV RIKREECPGT RVTIDKACDK RGASVRSTTE
SGKVIPEWCC RTCELPPVTY RTGTDCWYAM EIRPVHTQGG LVRSMVVADN GALLSEGGVP
GVVALFVVLE LVIRRRPATG GTVIWGGIAI LALLVTGLVS VESLFRYLVA VGLVFQLELG
PEAVAMVLLQ AVFEMRTCLL SGFVLRRSIT TREIVTVYFL LLVLEMGIPV KGLEHLWRWT
DALAMGAIIF RACTAEGKTG IGLLLAAFMT QSDMNIIHDG LTAFLCVATT MAIWRYIRGQ
GERKGLTWIV PLAGILGGEG SGVRLLAFWE LAASRGRRSF NEPMTVIGVM LTLASGMMRH
TSQEAVCAMA LAAFLLLMLT LGTRKMQLLA EWSGNIEWNP ELTSEGGEVS LRVRQDALGN
LHLTELEKEE RMMAFWLVVG LIASAFHWSG ILIVMGLWTI SEMLGSPRRT DLVFSGCSEG
RSDSRPLDVK NGVYRIYTPG LLWGQRQIGV GYGAKGVLHT MWHVTRGAAL LVDGVAVGPY
WADVREDVVC YGGAWSLESR WRGETVQVHA FPPGRAHETH QCQPGELILE NGRKMGAIPI
DLAKGTSGSP IMNSQGEVVG LYGNGLKTND TYVSSIAQGE VEKSRPNLPQ SVVGTGWTAK
GQITVLDMHP GSGKTHRVLP ELIRQCVERR LRTLVLAPTR VVLREMERAL SGKNVRFHSP
AVTEQHANGA IVDVMCHATY VNRRLLPQGR QNWEVAIMDE AHWTDPHSIA ARGHLYSLAK
ENRCAFVLMT ATPPGKSEPF PESNGAIASE ERQIPDGEWR DGFDWITEYE GRTAWFVPSI
ARGGAIARAL RQRGKSVICL NSKTFDKEYS RVKDEKPDFV VTTDISEMGA NLDVTRVIDG
RTNIKPEEVD GRIELTGTRR VTTASAAQRR GRVGRQGGRT DEYIYSGQCD DDDSGLVQWK
EAQILLDNIT TARGPVATFY GPEQERMTET AGHYRLPEEK RKHFRHLLAQ CDFTPWLAWH
VAANVASVTD RSWTWEGPEE NAVDENNGEL VTFRSPNGAE RTLRPVWRDA RMFREGRDIR
EFVSYASGRR SVGDVLMGMS GVPALLRQRC TSAMDVFYTL MHEEPGSRAM RIGERDAPEA
FLTAVEMLVL GLATLGVVWC FVVRTSVSRM VLGTLVLATS LIFLWAGGVG YGNMAGVALV
FYTLLTVLQP ETGKQRSSDD NKLAYFLLTL CGLAGMVAAN EMGLLEKTKA DLAALFARDQ
GETVRWGEWT NLDIQPARSW GTYVLVVSLF TPYMLHQLQT RIQQLVNSAV ASGAQAMRDL
GGGTPFFGVA GHVLALGVAS LVGATPTSLI LGVGLAAFHL AIVVSGLEAE LTQRAHKVFF
SAMVRNPMVD GDVINPFGDG EAKPALYERK LSLILALVLC LASVVMNRTF VAVTEAGAVG
VAAAMQLLRP EMDVLWTMPV ACGMSGVVRG SLWGLLPLGH RLWLRTTGTR RGGSEGDTLG
DMWKARLNSC TKEEFFAYRR AGVMETDREK ARELLKRGET NMGLAVSRGT SKLAWMEERG
YVTLKGEVVD LGCGRGGWSY YAASRPAVMS VRAYTIGGKG HESPRMVTSL GWNLIKFRAG
MDVFSMEPHR ADAILCDIGE SNPDAVVEGE RSRRVILLME QWKNRNPTAT CVFKVLAPYR
PEVIEALHRF QLQWGGGLVR TPFSRNSTHE MYFSTAITGN IVNSVNIQSR KLLARFGDQR
GPTRVPEIDL GVGTRSVVLA EDKVKEKDVM ERIQALKDQY CDTWHEDHEH PYRTWQYWGS
YKTAATGSSA SLLNGVVKLL SWPWNAREDV VRMAMTDTTA FGQQRVFKDK VDTKAQEPQP
GTKIIMRAVN DWLLERLVKK SRPRMCSREE FIAKVRSNAA LAAWSDEQNK WKSAREAVED
PEFWSLVEAE RERHLQGRCA HCVYNMMGKR EKKLGEFGVA KGSRAIWYMW LGSRFLEFEA
LGFLNEDHWA SRASSGAGVE GISLNYLGWH LKKLASLSGG LFYADDTAGW DTRITNADLD
DEEQILRYMD GDHKKLAATV LRKAYHAKVV RVARPSREGG CVMDIITRRD QRGSGQVVTY
ALNTITNIKV QLVRMMEGEG VIEVADSHNP RLLRVEKCVE EHGEERLSRM LVSGDDCVVR
PVDDRFSKAL YFLNDMAKTR KDTGEWEPST GFASWEEVPF CSHHFHELVM KDGRALVVPC
RDQDELVGRA RVSPGCGWSV RETACLSKAY GQMWLLSYFH RRDLRTLGFA ICSAVPVDWV
PTGRTTWSIH ASGAWMTTED MLEVWNRVWI YDNPFMEDKT RVDEWRDTPY LPKSQDILCS
SLVGRGERAE WAKNIWGAVE KVRRMIGPEH YRDYLSSMDR HDLHWELKLE SSIF


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