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 POLG_DEN2P              Reviewed;        3388 AA.
P12823; Q88646; Q88647; Q88648; Q88649; Q88650; Q88651; Q88652;
Q88653; Q88654; Q88655;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
10-MAY-2017, entry version 175.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Protein C;
AltName: Full=Core protein;
Contains:
RecName: Full=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=Non-structural protein 2A-alpha;
Short=NS2A-alpha;
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=Peptide 2k;
Contains:
RecName: Full=Non-structural protein 4B;
Short=NS4B;
Contains:
RecName: Full=RNA-directed RNA polymerase NS5;
EC=2.1.1.56;
EC=2.1.1.57;
EC=2.7.7.48;
AltName: Full=Non-structural protein 5;
Dengue virus type 2 (strain Puerto Rico/PR159-S1/1969) (DENV-2).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; Dengue virus group.
NCBI_TaxID=11066;
NCBI_TaxID=53540; Aedimorphus.
NCBI_TaxID=53539; Diceromyia.
NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=53541; Stegomyia.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2827375; DOI=10.1016/0042-6822(88)90406-0;
Hahn Y.S., Galler R., Hunkapiller T., Dalrymple J.M., Strauss J.H.,
Strauss E.G.;
"Nucleotide sequence of dengue 2 RNA and comparison of the encoded
proteins with those of other flaviviruses.";
Virology 162:167-180(1988).
[2]
C-TERMINUS (PROTEIN C), C-TERMINUS (ENVELOPE PROTEIN E), AND
C-TERMINUS (NON-STRUCTURAL PROTEIN 1).
STRAIN=New-Guinea;
PubMed=2741348; DOI=10.1016/0042-6822(89)90510-2;
Wright P.J., Cauchi M.R., Ng M.L.;
"Definition of the carboxy termini of the three glycoproteins
specified by dengue virus type 2.";
Virology 171:61-67(1989).
[3]
DISULFIDE BOND (NON-STRUCTURAL PROTEIN 1).
PubMed=14981082; DOI=10.1074/jbc.M312907200;
Wallis T.P., Huang C.Y., Nimkar S.B., Young P.R., Gorman J.J.;
"Determination of the disulfide bond arrangement of dengue virus NS1
protein.";
J. Biol. Chem. 279:20729-20741(2004).
[4]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2494-2783 IN COMPLEX WITH
S-ADENOSYL-L-HOMOCYSTEINE, AND CHARACTERIZATION OF METHYLTRANSFERASE
ACTIVITY (RNA-DIRECTED RNA POLYMERASE NS5).
PubMed=12032088; DOI=10.1093/emboj/21.11.2757;
Egloff M.P., Benarroch D., Selisko B., Romette J.L., Canard B.;
"An RNA cap (nucleoside-2'-O-)-methyltransferase in the flavivirus RNA
polymerase NS5: crystal structure and functional characterization.";
EMBO J. 21:2757-2768(2002).
[5]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 281-674, AND DISULFIDE BONDS
(ENVELOPE PROTEIN E).
PubMed=12759475; DOI=10.1073/pnas.0832193100;
Modis Y., Ogata S., Clements D., Harrison S.C.;
"A ligand-binding pocket in the dengue virus envelope glycoprotein.";
Proc. Natl. Acad. Sci. U.S.A. 100:6986-6991(2003).
[6]
STRUCTURE BY ELECTRON MICROSCOPY (16 ANGSTROMS) OF IMMATURE PARTICLES
(SMALL ENVELOPE PROTEIN M, AND ENVELOPE PROTEIN E).
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: 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 tot cell nucleus where it
modulates host functions. {ECO:0000250|UniProtKB:P17763}.
-!- 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 particule is covered with
60 spikes composed of heterodimer between precursor prM and
envelope protein E. The virion is transported to the Golgi
apparatus where the low pH causes dissociation of PrM-E
heterodimers and formation of E homodimers. prM-E cleavage is
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. May play a role in viral genome replication. Assist
membrane bending and envelopment of genomic RNA at the endoplasmic
reticulum. Excreted as a hexameric lipoparticle that plays a role
against host immune responce. {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: 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: Induces host endoplasmic
regulate the ATPase activity of the NS3 helicase.
{ECO:0000250|UniProtKB:P17763}.
-!- 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: 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:P17763}.
-!- 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].
-!- SUBUNIT: Protein C: Homodimerizes. Protein prM: Forms homodimers
with envelope protein E in the endoplasmic reticulum and Golgi.
Envelope protein E: Forms homodimers with envelope protein E in
the endoplasmic reticulum and Golgi. Non-structural protein 1:
Forms homodimers as well as homohexamers. NS1 may interact with
NS4A. Non-structural protein 2B: Forms a heterodimer with Non-
structural protein 3. May form homooligomers. Non-structural
protein 3: Forms a heterodimer with Non-structural protein 2B.
Interacts with Non-structural protein 4B. Interacts with
unphosphorylated Non-structural protein 5; this interaction
stimulates Non-structural protein 5 guanylyltransferase activity.
Non-structural protein 4B: Interacts with non-structural protein
3. Non-structural protein 5: interacts with host STAT2; this
interaction inhibits the phosphorylation of the latter, and, when
all viral proteins are present (polyprotein), targets STAT2 for
degradation. {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Protein C: Virion
{ECO:0000250|UniProtKB:P17763}. Host nucleus
{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:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00860}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00860}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted
{ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral
membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Lumenal
side {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 2A-alpha: Host
endoplasmic reticulum membrane {ECO:0000255|PROSITE-
ProRule:PRU00860}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic
reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host
endoplasmic reticulum membrane {ECO:0000255|PROSITE-
ProRule:PRU00860}; Peripheral membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side
{ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00860}.
-!- 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 NS3
protease. {ECO:0000255|PROSITE-ProRule:PRU00860}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic
reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; 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:0000255|PROSITE-ProRule:PRU00860}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase NS5: Host
endoplasmic reticulum membrane {ECO:0000255|PROSITE-
ProRule:PRU00860}; Peripheral membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side
{ECO:0000255|PROSITE-ProRule:PRU00860}. Host nucleus
{ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated
vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:P17763}.
-!- DOMAIN: Transmembrane domains of the small envelope protein M and
envelope protein E contains an endoplasmic reticulum retention
signals. {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, wereas cleavages
in the cytoplasmic side are performed by the 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: Non-structural protein 2A-alpha: A C-terminally truncated
form of non-structural protein 2A, results from partial cleavage
by NS3. {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: Non-structural protein 1: The excreted form is glycosylated
and this is required for efficient secretion of the protein from
infected cells. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: RNA-directed RNA polymerase NS5: Phosphorylated on serines
residues. This phosphorylation may trigger NS5 nuclear
localization. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Envelope protein E: N-glycosylated.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: Non-structural protein 1: N-glycosylated.
{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=1p58";
-!- WEB RESOURCE: Name=Virus Pathogen Resource;
URL="http://www.viprbrc.org/brc/home.do?decorator=flavi_dengue";
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EMBL; M19197; AAA42962.1; -; Genomic_RNA.
PIR; A29972; GNWVDP.
PDB; 1L9K; X-ray; 2.40 A; A=2492-2784.
PDB; 1OAN; X-ray; 2.75 A; A/B=281-674.
PDB; 1OK8; X-ray; 2.00 A; A=281-674.
PDB; 1OKE; X-ray; 2.40 A; A/B=281-674.
PDB; 1P58; EM; 9.50 A; A/B/C=281-775, D/E/F=206-280.
PDB; 1R6A; X-ray; 2.60 A; A=2492-2784.
PDB; 1R6R; NMR; -; A/B=1-100.
PDB; 1THD; EM; 9.50 A; A/B/C=281-675.
PDB; 2P1D; X-ray; 2.90 A; A=2492-2784.
PDB; 2P3L; X-ray; 2.20 A; A=2492-2784.
PDB; 2P3O; X-ray; 2.76 A; A=2492-2784.
PDB; 2P3Q; X-ray; 2.75 A; A=2492-2784.
PDB; 2P40; X-ray; 2.70 A; A=2492-2784.
PDB; 2P41; X-ray; 1.80 A; A=2492-2784.
PDB; 3J8D; EM; 26.00 A; G/H/I=281-674.
PDB; 3ZKO; EM; 13.70 A; A/B/C=281-775.
PDB; 5HHG; X-ray; 2.20 A; C=3353-3388.
PDBsum; 1L9K; -.
PDBsum; 1OAN; -.
PDBsum; 1OK8; -.
PDBsum; 1OKE; -.
PDBsum; 1P58; -.
PDBsum; 1R6A; -.
PDBsum; 1R6R; -.
PDBsum; 1THD; -.
PDBsum; 2P1D; -.
PDBsum; 2P3L; -.
PDBsum; 2P3O; -.
PDBsum; 2P3Q; -.
PDBsum; 2P40; -.
PDBsum; 2P41; -.
PDBsum; 3J8D; -.
PDBsum; 3ZKO; -.
PDBsum; 5HHG; -.
ProteinModelPortal; P12823; -.
SMR; P12823; -.
DrugBank; DB00811; Ribavirin.
DrugBank; DB01752; S-Adenosyl-L-Homocysteine.
OrthoDB; VOG090000B1; -.
BRENDA; 2.1.1.57; 1867.
EvolutionaryTrace; P12823; -.
PRO; PR:P12823; -.
Proteomes; UP000007197; 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: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: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:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; 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; 2.60.40.350; -; 1.
Gene3D; 3.30.387.10; -; 1.
Gene3D; 3.30.67.10; -; 1.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR000069; Env_glycoprot_M_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.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
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; 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; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
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 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; Transcription;
Transcription regulation; Transferase; Transmembrane;
Transmembrane helix; Transport; 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.
CHAIN 1 3388 Genome polyprotein.
/FTId=PRO_0000405217.
CHAIN 1 100 Protein C.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000037969.
PROPEP 101 114 ER anchor for the protein C, removed in
mature form by serine protease NS3.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000037970.
CHAIN 115 280 prM. {ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000308286.
CHAIN 115 205 Peptide pr.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000308287.
CHAIN 206 280 Small envelope protein M.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000037971.
CHAIN 281 775 Envelope protein E.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000037972.
CHAIN 776 1127 Non-structural protein 1.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000037973.
CHAIN 1128 1345 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000037974.
CHAIN 1128 1315 Non-structural protein 2A-alpha.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000308288.
CHAIN 1346 1475 Serine protease subunit NS2B.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000037975.
CHAIN 1476 2090 Serine protease NS3.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000037976.
CHAIN 2091 2217 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000037977.
PEPTIDE 2218 2240 Peptide 2k.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000308289.
CHAIN 2241 2488 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000037978.
CHAIN 2489 3388 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000037979.
TOPO_DOM 1 101 Cytoplasmic. {ECO:0000255}.
TRANSMEM 102 122 Helical. {ECO:0000255}.
TOPO_DOM 123 238 Extracellular. {ECO:0000255}.
TRANSMEM 239 259 Helical. {ECO:0000255}.
TOPO_DOM 260 265 Cytoplasmic. {ECO:0000255}.
TRANSMEM 266 280 Helical. {ECO:0000255}.
TOPO_DOM 281 725 Extracellular. {ECO:0000255}.
INTRAMEM 726 746 Helical. {ECO:0000255}.
TOPO_DOM 747 752 Extracellular. {ECO:0000255}.
INTRAMEM 753 773 Helical. {ECO:0000255}.
TOPO_DOM 774 1124 Extracellular. {ECO:0000255}.
TRANSMEM 1125 1145 Helical. {ECO:0000255}.
TOPO_DOM 1146 1156 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1157 1177 Helical. {ECO:0000255}.
TOPO_DOM 1178 1184 Lumenal. {ECO:0000255}.
TRANSMEM 1185 1205 Helical. {ECO:0000255}.
TOPO_DOM 1206 1271 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1272 1292 Helical. {ECO:0000255}.
TOPO_DOM 1293 1317 Lumenal. {ECO:0000255}.
TRANSMEM 1318 1338 Helical. {ECO:0000255}.
TOPO_DOM 1339 1346 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1347 1367 Helical. {ECO:0000255}.
TOPO_DOM 1368 1370 Lumenal. {ECO:0000255}.
TRANSMEM 1371 1391 Helical. {ECO:0000255}.
TOPO_DOM 1392 1447 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1448 1468 Helical. {ECO:0000255}.
TOPO_DOM 1469 2144 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2145 2165 Helical. {ECO:0000255}.
TOPO_DOM 2166 2167 Lumenal. {ECO:0000255}.
INTRAMEM 2168 2188 Helical. {ECO:0000255}.
TOPO_DOM 2189 2189 Lumenal. {ECO:0000255}.
TRANSMEM 2190 2210 Helical. {ECO:0000255}.
TOPO_DOM 2211 2225 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2226 2246 Helical; Note=Signal for NS4B.
{ECO:0000255}.
TOPO_DOM 2247 2274 Lumenal. {ECO:0000255}.
INTRAMEM 2275 2292 Helical. {ECO:0000255}.
TOPO_DOM 2293 2313 Lumenal. {ECO:0000255}.
INTRAMEM 2314 2334 Helical. {ECO:0000255}.
TOPO_DOM 2335 2344 Lumenal. {ECO:0000255}.
TRANSMEM 2345 2365 Helical. {ECO:0000255}.
TOPO_DOM 2366 2410 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2411 2431 Helical. {ECO:0000255}.
TOPO_DOM 2432 2456 Lumenal. {ECO:0000255}.
TRANSMEM 2457 2477 Helical. {ECO:0000255}.
TOPO_DOM 2478 3388 Cytoplasmic. {ECO:0000255}.
DOMAIN 1476 1653 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1655 1811 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1821 1988 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2490 2752 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3017 3166 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1668 1675 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 33 74 Hydrophobic; homodimerization of capsid
protein C. {ECO:0000250}.
REGION 1398 1437 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
MOTIF 1759 1762 DEAH box.
COMPBIAS 97 100 Poly-Arg.
COMPBIAS 1434 1437 Poly-Glu.
COMPBIAS 2145 2151 Poly-Leu.
COMPBIAS 2351 2354 Poly-Leu.
COMPBIAS 3380 3383 Poly-Glu.
ACT_SITE 1526 1526 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1550 1550 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1610 1610 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
BINDING 2502 2502 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2505 2505 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2506 2506 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2508 2508 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2517 2517 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2544 2544 S-adenosyl-L-methionine.
BINDING 2574 2574 S-adenosyl-L-methionine; via carbonyl
oxygen.
BINDING 2575 2575 S-adenosyl-L-methionine; via carbonyl
oxygen.
BINDING 2592 2592 S-adenosyl-L-methionine.
BINDING 2593 2593 S-adenosyl-L-methionine; via carbonyl
oxygen.
BINDING 2619 2619 S-adenosyl-L-methionine.
BINDING 2620 2620 S-adenosyl-L-methionine; via carbonyl
oxygen.
BINDING 2638 2638 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2700 2700 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2702 2702 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2707 2707 S-adenosyl-L-methionine.
SITE 100 101 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 114 115 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 205 206 Cleavage; by host furin. {ECO:0000255}.
SITE 280 281 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 775 776 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 1127 1128 Cleavage; by host. {ECO:0000250}.
SITE 1345 1346 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 1475 1476 Cleavage; by autolysis. {ECO:0000255}.
SITE 2090 2091 Cleavage; by autolysis. {ECO:0000255}.
SITE 2217 2218 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 2240 2241 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 2488 2489 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 2513 2513 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2549 2549 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2634 2634 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2635 2635 S-adenosyl-L-methionine binding.
SITE 2669 2669 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2705 2705 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 347 347 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 433 433 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 905 905 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 982 982 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2298 2298 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2302 2302 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 283 310 {ECO:0000269|PubMed:12759475}.
DISULFID 340 401 {ECO:0000269|PubMed:12759475}.
DISULFID 354 385 {ECO:0000269|PubMed:12759475}.
DISULFID 372 396 {ECO:0000269|PubMed:12759475}.
DISULFID 465 565 {ECO:0000269|PubMed:12759475}.
DISULFID 582 613 {ECO:0000269|PubMed:12759475}.
DISULFID 779 790 {ECO:0000269|PubMed:14981082}.
DISULFID 830 918 {ECO:0000269|PubMed:14981082}.
DISULFID 954 998 {ECO:0000269|PubMed:14981082}.
DISULFID 1055 1104 {ECO:0000269|PubMed:14981082}.
DISULFID 1066 1088 {ECO:0000269|PubMed:14981082}.
DISULFID 1087 1091 {ECO:0000269|PubMed:14981082}.
CONFLICT 351 351 D -> E (in Ref. 5). {ECO:0000305}.
CONFLICT 615 615 T -> I (in Ref. 5). {ECO:0000305}.
CONFLICT 632 632 T -> I (in Ref. 5). {ECO:0000305}.
CONFLICT 670 670 D -> N (in Ref. 5). {ECO:0000305}.
STRAND 23 25 {ECO:0000244|PDB:1R6R}.
HELIX 27 32 {ECO:0000244|PDB:1R6R}.
STRAND 34 36 {ECO:0000244|PDB:1R6R}.
HELIX 45 57 {ECO:0000244|PDB:1R6R}.
HELIX 63 69 {ECO:0000244|PDB:1R6R}.
HELIX 75 95 {ECO:0000244|PDB:1R6R}.
TURN 282 285 {ECO:0000244|PDB:1OKE}.
HELIX 288 290 {ECO:0000244|PDB:1OK8}.
STRAND 291 293 {ECO:0000244|PDB:1OK8}.
STRAND 295 306 {ECO:0000244|PDB:1OK8}.
STRAND 311 315 {ECO:0000244|PDB:1OK8}.
STRAND 320 332 {ECO:0000244|PDB:1OK8}.
STRAND 334 352 {ECO:0000244|PDB:1OK8}.
HELIX 363 366 {ECO:0000244|PDB:1OK8}.
STRAND 370 379 {ECO:0000244|PDB:1OK8}.
HELIX 381 383 {ECO:0000244|PDB:1OK8}.
STRAND 389 409 {ECO:0000244|PDB:1OK8}.
HELIX 412 414 {ECO:0000244|PDB:1OK8}.
STRAND 415 424 {ECO:0000244|PDB:1OK8}.
TURN 428 432 {ECO:0000244|PDB:1OKE}.
STRAND 440 444 {ECO:0000244|PDB:1OK8}.
STRAND 450 455 {ECO:0000244|PDB:1OK8}.
TURN 456 458 {ECO:0000244|PDB:1OK8}.
STRAND 459 467 {ECO:0000244|PDB:1OK8}.
TURN 473 475 {ECO:0000244|PDB:1OK8}.
STRAND 476 481 {ECO:0000244|PDB:1OK8}.
STRAND 484 489 {ECO:0000244|PDB:1OK8}.
HELIX 490 495 {ECO:0000244|PDB:1OK8}.
STRAND 500 502 {ECO:0000244|PDB:1OK8}.
HELIX 514 516 {ECO:0000244|PDB:1OK8}.
STRAND 518 520 {ECO:0000244|PDB:1OK8}.
STRAND 523 526 {ECO:0000244|PDB:1OKE}.
STRAND 530 532 {ECO:0000244|PDB:1OK8}.
HELIX 537 543 {ECO:0000244|PDB:1OK8}.
TURN 544 546 {ECO:0000244|PDB:1OK8}.
STRAND 547 550 {ECO:0000244|PDB:1OK8}.
STRAND 552 559 {ECO:0000244|PDB:1OK8}.
STRAND 562 571 {ECO:0000244|PDB:1OK8}.
STRAND 586 594 {ECO:0000244|PDB:1OK8}.
STRAND 600 606 {ECO:0000244|PDB:1OK8}.
STRAND 608 610 {ECO:0000244|PDB:1OK8}.
STRAND 612 614 {ECO:0000244|PDB:1OK8}.
STRAND 617 624 {ECO:0000244|PDB:1OK8}.
STRAND 631 633 {ECO:0000244|PDB:1OK8}.
STRAND 645 649 {ECO:0000244|PDB:1OK8}.
STRAND 653 661 {ECO:0000244|PDB:1OK8}.
STRAND 667 673 {ECO:0000244|PDB:1OK8}.
HELIX 2497 2507 {ECO:0000244|PDB:1L9K}.
HELIX 2510 2517 {ECO:0000244|PDB:1L9K}.
TURN 2518 2520 {ECO:0000244|PDB:1L9K}.
STRAND 2522 2525 {ECO:0000244|PDB:1L9K}.
HELIX 2527 2535 {ECO:0000244|PDB:1L9K}.
STRAND 2543 2545 {ECO:0000244|PDB:2P1D}.
HELIX 2546 2554 {ECO:0000244|PDB:1L9K}.
TURN 2555 2557 {ECO:0000244|PDB:1L9K}.
STRAND 2563 2568 {ECO:0000244|PDB:1L9K}.
TURN 2571 2573 {ECO:0000244|PDB:1L9K}.
HELIX 2574 2579 {ECO:0000244|PDB:1L9K}.
STRAND 2585 2591 {ECO:0000244|PDB:1L9K}.
HELIX 2609 2611 {ECO:0000244|PDB:1L9K}.
STRAND 2612 2615 {ECO:0000244|PDB:1L9K}.
HELIX 2620 2622 {ECO:0000244|PDB:1L9K}.
STRAND 2629 2633 {ECO:0000244|PDB:1L9K}.
HELIX 2642 2657 {ECO:0000244|PDB:1L9K}.
STRAND 2665 2671 {ECO:0000244|PDB:1L9K}.
HELIX 2676 2688 {ECO:0000244|PDB:1L9K}.
STRAND 2692 2694 {ECO:0000244|PDB:1L9K}.
STRAND 2706 2709 {ECO:0000244|PDB:1L9K}.
HELIX 2716 2729 {ECO:0000244|PDB:1L9K}.
STRAND 2739 2742 {ECO:0000244|PDB:1L9K}.
SEQUENCE 3388 AA; 379219 MW; 79B7C87BE64D2D8F CRC64;
MNDQRKKARN TPFNMLKRER NRVSTVQQLT KRFSLGMLQG RGPLKLFMAL VAFLRFLTIP
PTAGILKRWG TIKKSKAINV LRGFRKEIGR MLNILNRRRR TAGMIIMLIP TVMAFHLTTR
NGEPHMIVSR QEKGKSLLFK TKDGTNMCTL MAMDLGELCE DTITYKCPFL KQNEPEDIDC
WCNSTSTWVT YGTCTTTGEH RREKRSVALV PHVGMGLETR TETWMSSEGA WKHAQRIETW
ILRHPGFTIM AAILAYTIGT THFQRVLIFI LLTAIAPSMT MRCIGISNRD FVEGVSGGSW
VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC IEAKLTNTTT DSRCPTQGEP
TLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFT CKKNMEGKIV QPENLEYTVV
ITPHSGEEHA VGNDTGKHGK EVKITPQSSI TEAELTGYGT VTMECSPRTG LDFNEMVLLQ
MKDKAWLVHR QWFLDLPLPW LPGADTQGSN WIQKETLVTF KNPHAKKQDV VVLGSQEGAM
HTALTGATEI QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS MCTGKFKVVK EIAETQHGTI
VIRVQYEGDG SPCKTPFEIM DLEKRHVLGR LTTVNPIVTE KDSPVNIEAE PPFGDSYIII
GVEPGQLKLD WFKKGSSIGQ MFETTMRGAK RMAILGDTAW DFGSLGGVFT SIGKALHQVF
GAIYGAAFSG VSWTMKILIG VIITWIGMNS RSTSLSVSLV LVGIVTLYLG VMVQADSGCV
VSWKNKELKC GSGIFVTDNV HTWTEQYKFQ PESPSKLASA IQKAHEEGIC GIRSVTRLEN
LMWKQITSEL NHILSENEVK LTIMTGDIKG IMQVGKRSLR PQPTELRYSW KTWGKAKMLS
TELHNQTFLI DGPETAECPN TNRAWNSLEV EDYGFGVFTT NIWLRLREKQ DAFCDSKLMS
AAIKDNRAVH ADMGYWIESA LNDTWKIEKA SFIEVKSCHW PKSHTLWSNG VLESEMVIPK
NFAGPVSQHN NRPGYHTQTA GPWHLGKLEM DFDFCEGTTV VVTEDCGNRG PSLRTTTASG
KLITEWCCRS CTLPPLRYRG EDGCWYGMEI RPLKEKEENL VSSLVTAGHG QIDNFSLGIL
GMALFLEEML RTRVGTKHAI LLVAVSFVTL ITGNMSFRDL GRVMVMVGAT MTDDIGMGVT
YLALLAAFKV RPTFAAGLLL RKLTSKELMM TTIGIVLLSQ SSIPETILEL TDALALGMMV
LKMVRNMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTILA VVSVSPLFLT SSQQKADWIP
LALTIKGLNP TAIFLTTLSR TSKKRSWPLN EAIMAVGMVS ILASSLLKND TPMTGPLVAG
GLLTVCYVLT GRSADLELER ATDVKWDDQA EISGSSPILS ITISEDGSMS IKNEEEEQTL
TILIRTGLLV ISGLFPVSIP ITAAAWYLWE VKKQRAGVLW DVPSPPPVGK AELEDGAYRI
KQKGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHKGKRI EPSWADVKKD LISYGGGWKL
EGEWKEGEEV QVLALEPGKN PRAVQTKPGL FRTNTGTIGA VSLDFSPGTS GSPIVDKKGK
VVGLYGNGVV TRSGAYVSAI AQTEKSIEDN PEIEDDIFRK RRLTIMDLHP GAGKTKRYLP
AIVREAIKRG LRTLILAPTR VVAAEMEEAL RGLPIRYQTP AIRAEHTGRE IVDLMCHATF
TMRLLSPIRV PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT ATPPGSRDPF
PQSNAPIMDE EREIPERSWN SGHEWVTDFK GKTVWFVPSI KTGNDIAACL RKNGKRVIQL
SRKTFDSEYV KTRTNDWDFV VTTDISEMGA NFKAERVIDP RRCMKPVILT DGEERVILAG
PMPVTHSSAA QRRGRIGRNP RNENDQYIYM GEPLENDEDC AHWKEAKMLL DNINTPEGII
PSMFEPEREK VDAIDGEYRL RGEARKTFVD LMRRGDLPVW LAYKVAAEGI NYADRRWCFD
GTRNNQILEE NVEVEIWTKE GERKKLKPRW LDARIYSDPL ALKEFAAGRK SLTLNLITEM
GRLPTFMTQK ARDALDNLAV LHTAEAGGKA YNHALSELPE TLETLLLLTL LATVTGGIFL
FLMSGRGIGK MTLGMCCIIT ASILLWYAQI QPHWIAASII LEFFLIVLLI PEPEKQRTPQ
DNQLTYVIIA ILTVVAATMA NEMGFLEKTK KDLGLGNIAT QQPESNILDI DLRPASAWTL
YAVATTFITP MLRHSIENSS VNVSLTAIAN QATVLMGLGK GWPLSKMDIG VPLLAIGCYS
QVNPITLTAA LLLLVAHYAI IGPGLQAKAT REAQKRAAAG IMKNPTVDGI TVIDLDPIPY
DPKFEKQLGQ VMLLVLCVTQ VLMMRTTWAL CEALTLATGP VSTLWEGNPG RFWNTTIAVS
MANIFRGSYL AGAGLLFSIM KNTTSTRRGT GNIGETLGEK WKSRLNALGK SEFQIYKKSG
IQEVDRTLAK EGIKRGETDH HAVSRGSAKL RWFVERNLVT PEGKVVDLGC GRGGWSYYCG
GLKNVREVKG LTKGGPGHEE PIPMSTYGWN LVRLQSGVDV FFVPPEKCDT LLCDIGESSP
NPTVEAGRTL RVLNLVENWL NNNTQFCVKV LNPYMPSVIE RMETLQRKYG GALVRNPLSR
NSTHEMYWVS NASGNIVSSV NMISRMLINR FTMRHKKATY EPDVDLGSGT RNIGIESETP
NLDIIGKRIE KIKQEHETSW HYDQDHPYKT WAYHGSYETK QTGSASSMVN GVVRLLTKPW
DVVPMVTQMA MTDTTPFGQQ RVFKEKVDTR TQEPKEGTKK LMKITAEWLW KELGKKKTPR
MCTREEFTKK VRSNAALGAI FTDENKWKSA REAVEDSRFW ELVDKERNLH LEGKCETCVY
NMMGKREKKL GEFGKAKGSR AIWYMWLGAR FLEFEALGFL NEDHWFSREN SLSGVEGEGL
HKLGYILREV SKKEGGAMYA DDTAGWDTRI TIEDLKNEEM ITNHMAGEHK KLAEAIFKLT
YQNKVVRVQR PTPRGTVMDI ISRRDQRGSG QVGTYGLNTF TNMEAQLIRQ MEGEGIFKSI
QHLTASEEIA VQDWLARVGR ERLSRMAISG DDCVVKPLDD RFARALTALN DMGKVRKDIQ
QWEPSRGWND WTQVPFCSHH FHELIMKDGR TLVVPCRNQD ELIGRARISQ GAGWSLRETA
CLGKSYAQMW SLMYFHRRDL RLAANAICSA VPSHWVPTSR TTWSIHASHE WMTTEDMLTV
WNKVWILENP WMEDKTPVES WEEIPYLGKR EDQWCGSLIG LTSRATWAKN IQTAINQVRS
LIGNEEYTDY MPSMKRFRRE EEEAGVLW


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