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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) (Non-structural protein 5)]

 POLG_MVEV5              Reviewed;        3434 AA.
P05769; Q9Q9F7;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 2.
07-NOV-2018, entry version 167.
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 {ECO:0000269|PubMed:19793813};
EC=3.6.4.13 {ECO:0000269|PubMed:19793813};
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;
Murray valley encephalitis virus (strain MVE-1-51) (MVEV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; Murray Valley encephalitis virus.
NCBI_TaxID=301478;
NCBI_TaxID=162997; Culex annulirostris (Common banded mosquito).
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=10567642;
Hurrelbrink R.J., Nestorowicz A., McMinn P.C.;
"Characterization of infectious Murray Valley encephalitis virus
derived from a stably cloned genomic-length cDNA.";
J. Gen. Virol. 80:3115-3125(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-1780.
PubMed=3009829; DOI=10.1016/0022-2836(86)90435-3;
Dalgarno L., Trent D.W., Strauss J.H., Rice C.M.;
"Partial nucleotide sequence of the Murray Valley encephalitis virus
genome. Comparison of the encoded polypeptides with yellow fever virus
structural and non-structural proteins.";
J. Mol. Biol. 187:309-323(1986).
[3]
NUCLEOTIDE SEQUENCE OF 1773-3434, AND PROTEIN SEQUENCE OF 794-807;
1504-1519 AND 2530-2537.
PubMed=1702914; DOI=10.1007/BF00265630;
Lee E., Fernon C., Simpson R., Weir R.C., Rice C.M., Dalgarno L.;
"Sequence of the 3' half of the Murray Valley encephalitis virus
genome and mapping of the nonstructural proteins NS1, NS3, and NS5.";
Virus Genes 4:197-213(1990).
[4]
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).
[5]
PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
PubMed=8392191;
Lobigs M.;
"Flavivirus premembrane protein cleavage and spike heterodimer
secretion require the function of the viral proteinase NS3.";
Proc. Natl. Acad. Sci. U.S.A. 90:6218-6222(1993).
[6]
PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN), AND MUTAGENESIS OF
121-GLY--ALA-124.
PubMed=9499070;
Stocks C.E., Lobigs M.;
"Signal peptidase cleavage at the flavivirus C-prM junction:
dependence on the viral NS2B-3 protease for efficient processing
requires determinants in C, the signal peptide, and prM.";
J. Virol. 72:2141-2149(1998).
[7]
PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
PubMed=7494334;
Stocks C.E., Lobigs M.;
"Posttranslational signal peptidase cleavage at the flavivirus C-prM
junction in vitro.";
J. Virol. 69:8123-8126(1995).
[8]
GLYCOSYLATION (NON-STRUCTURAL PROTEIN 1), AND DISULFIDE BONDS.
PubMed=11514736;
Blitvich B.J., Scanlon D., Shiell B.J., Mackenzie J.S., Pham K.,
Hall R.A.;
"Determination of the intramolecular disulfide bond arrangement and
biochemical identification of the glycosylation sites of the
nonstructural protein NS1 of Murray Valley encephalitis virus.";
J. Gen. Virol. 82:2251-2256(2001).
[9]
PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
PubMed=20207389; DOI=10.1016/j.virol.2010.02.008;
Lobigs M., Lee E., Ng M.L., Pavy M., Lobigs P.;
"A flavivirus signal peptide balances the catalytic activity of two
proteases and thereby facilitates virus morphogenesis.";
Virology 401:80-89(2010).
[10]
PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
PubMed=26377679; DOI=10.1186/s12985-015-0375-4;
Addis S.N., Lee E., Bettadapura J., Lobigs M.;
"Proteolytic cleavage analysis at the Murray Valley encephalitis virus
NS1-2A junction.";
Virol. J. 12:144-144(2015).
[11]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1681-2122.
PubMed=17893366; DOI=10.1110/ps.072843107;
Mancini E.J., Assenberg R., Verma A., Walter T.S., Tuma R.,
Grimes J.M., Owens R.J., Stuart D.I.;
"Structure of the Murray Valley encephalitis virus RNA helicase at 1.9
Angstrom resolution.";
Protein Sci. 16:2294-2300(2007).
[12]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2530-2798.
PubMed=17622627; DOI=10.1099/vir.0.82757-0;
Assenberg R., Ren J., Verma A., Walter T.S., Alderton D.,
Hurrelbrink R.J., Fuller S.D., Bressanelli S., Owens R.J.,
Stuart D.I., Grimes J.M.;
"Crystal structure of the Murray Valley encephalitis virus NS5
methyltransferase domain in complex with cap analogues.";
J. Gen. Virol. 88:2228-2236(2007).
[13]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1421-2122, CATALYTIC
ACTIVITY (SERINE PROTEASE NS3), AND FUNCTION (SERINE PROTEASE NS3).
PubMed=19793813; DOI=10.1128/JVI.00942-09;
Assenberg R., Mastrangelo E., Walter T.S., Verma A., Milani M.,
Owens R.J., Stuart D.I., Grimes J.M., Mancini E.J.;
"Crystal structure of a novel conformational state of the flavivirus
NS3 protein: implications for polyprotein processing and viral
replication.";
J. Virol. 83:12895-12906(2009).
-!- FUNCTION: Capsid protein C: Plays a role in virus budding by
binding to the cell membrane and gathering the viral RNA into a
nucleocapsid that forms the core of a mature virus particle.
During virus entry, may induce genome penetration into the host
cytoplasm after hemifusion induced by the surface proteins. Can
migrate to the cell nucleus where it modulates host functions.
Overcomes the anti-viral effects of host EXOC1 by sequestering and
degrading the latter through the proteasome degradation pathway.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Capsid protein C: Inhibits RNA silencing by interfering
with host Dicer. {ECO:0000250|UniProtKB:P03314}.
-!- FUNCTION: Peptide pr: Prevents premature fusion activity of
envelope proteins in trans-Golgi by binding to envelope protein E
at pH6.0. After virion release in extracellular space, gets
dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Protein prM: Acts as a chaperone for envelope protein E
during intracellular virion assembly by masking and inactivating
envelope protein E fusion peptide. prM is the only viral peptide
matured by host furin in the trans-Golgi network probably to avoid
catastrophic activation of the viral fusion activity in acidic
Golgi compartment prior to virion release. prM-E cleavage is
inefficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Small envelope protein M: May play a role in virus
budding. Exerts cytotoxic effects by activating a mitochondrial
apoptotic pathway through M ectodomain. May display a viroporin
activity. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Envelope protein E: Binds to host cell surface receptor
and mediates fusion between viral and cellular membranes. Envelope
protein is synthesized in the endoplasmic reticulum in the form of
heterodimer with protein prM. They play a role in virion budding
in the ER, and the newly formed immature particle is covered with
60 spikes composed of heterodimer between precursor prM and
envelope protein E. The virion is transported to the Golgi
apparatus where the low pH causes dissociation of PrM-E
heterodimers and formation of E homodimers. prM-E cleavage is
inefficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 1: Involved in immune evasion,
pathogenesis and viral replication. Once cleaved off the
polyprotein, is targeted to three destinations: the viral
replication cycle, the plasma membrane and the extracellular
compartment. Essential for viral replication. Required for
formation of the replication complex and recruitment of other non-
structural proteins to the ER-derived membrane structures.
Excreted as a hexameric lipoparticle that plays a role against
host immune response. Antagonizing the complement function. Binds
to the host macrophages and dendritic cells. Inhibits signal
transduction originating from Toll-like receptor 3 (TLR3).
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- FUNCTION: Non-structural protein 2A: Component of the viral RNA
replication complex that functions in virion assembly and
antagonizes the host alpha/beta interferon antiviral response.
{ECO:0000250|UniProtKB:P14335}.
-!- FUNCTION: Serine protease subunit NS2B: Required cofactor for the
serine protease function of NS3. May have membrane-destabilizing
activity and form viroporins (By similarity).
{ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00859}.
-!- FUNCTION: Serine protease NS3: Displays three enzymatic
activities: serine protease, NTPase and RNA helicase. NS3 serine
protease, in association with NS2B, performs its autocleavage and
cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM,
NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA
helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.
{ECO:0000255|PROSITE-ProRule:PRU00860,
ECO:0000269|PubMed:19793813}.
-!- 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 (-) RNA genome, and performs the capping of genomes in the
cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose
2'-O positions. Besides its role in RNA genome replication, also
prevents the establishment of cellular antiviral state by blocking
the interferon-alpha/beta (IFN-alpha/beta) signaling pathway.
Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing
activation of JAK-STAT signaling pathway.
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- 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.
{ECO:0000269|PubMed:19793813}.
-!- 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:
Homohexamer when secreted. NS1 interacts with NS4B. Interacts with
host complement protein CFH; this interaction leads to the
degradation of C3. 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.
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Capsid protein C: Virion
{ECO:0000250|UniProtKB:P17763}. Host nucleus
{ECO:0000250|UniProtKB:P17763}. Host cytoplasm
{ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear
region {ECO:0000250|UniProtKB:P06935}.
-!- 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:0000269|PubMed:20207389, ECO:0000269|PubMed:26377679,
ECO:0000269|PubMed:7494334, ECO:0000269|PubMed:8392191,
ECO:0000269|PubMed:9499070}.
-!- 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}.
-!- PTM: Non-structural protein 1: N-glycosylated (PubMed:11514736).
The excreted form is glycosylated and this is required for
efficient secretion of the protein from infected cells (By
similarity). {ECO:0000250|UniProtKB:P17763,
ECO:0000269|PubMed:11514736}.
-!- 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; AF161266; AAF05296.1; -; Genomic_RNA.
EMBL; X03467; CAA27184.1; -; Unassigned_RNA.
PIR; A24635; GNWVMV.
RefSeq; NP_051124.1; NC_000943.1.
PDB; 2PX2; X-ray; 2.00 A; A/B=2530-2798.
PDB; 2PX4; X-ray; 2.20 A; A=2530-2798.
PDB; 2PX5; X-ray; 2.30 A; A/B=2530-2798.
PDB; 2PX8; X-ray; 2.20 A; A/B=2530-2798.
PDB; 2PXA; X-ray; 2.30 A; A/B=2530-2798.
PDB; 2PXC; X-ray; 2.80 A; A=2530-2798.
PDB; 2V8O; X-ray; 1.90 A; A=1681-2122.
PDB; 2WV9; X-ray; 2.75 A; A=1421-1465, A=1504-2122.
PDBsum; 2PX2; -.
PDBsum; 2PX4; -.
PDBsum; 2PX5; -.
PDBsum; 2PX8; -.
PDBsum; 2PXA; -.
PDBsum; 2PXC; -.
PDBsum; 2V8O; -.
PDBsum; 2WV9; -.
ProteinModelPortal; P05769; -.
SMR; P05769; -.
MEROPS; S07.003; -.
iPTMnet; P05769; -.
PRIDE; P05769; -.
GeneID; 1489715; -.
KEGG; vg:1489715; -.
OrthoDB; VOG090000B1; -.
EvolutionaryTrace; P05769; -.
Proteomes; UP000008863; 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: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:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd12149; Flavi_E_C; 1.
Gene3D; 1.10.10.930; -; 1.
Gene3D; 1.10.8.970; -; 1.
Gene3D; 1.20.1280.260; -; 1.
Gene3D; 2.60.260.50; -; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 2.60.98.10; -; 1.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR000069; Env_glycoprot_M_flavivir.
InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
InterPro; IPR001122; Flavi_capsidC.
InterPro; IPR037172; Flavi_capsidC_sf.
InterPro; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
InterPro; IPR001157; Flavi_NS1.
InterPro; IPR000752; Flavi_NS2A.
InterPro; IPR000487; Flavi_NS2B.
InterPro; IPR000404; Flavi_NS4A.
InterPro; IPR001528; Flavi_NS4B.
InterPro; IPR002535; Flavi_propep.
InterPro; IPR038688; Flavi_propep_sf.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
InterPro; IPR038055; Glycoprot_E_dimer_dom.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR000208; RNA-dir_pol_flavivirus.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01003; Flavi_capsid; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF02832; Flavi_glycop_C; 1.
Pfam; PF00869; Flavi_glycoprot; 1.
Pfam; PF01004; Flavi_M; 1.
Pfam; PF00948; Flavi_NS1; 1.
Pfam; PF01005; Flavi_NS2A; 1.
Pfam; PF01002; Flavi_NS2B; 1.
Pfam; PF01350; Flavi_NS4A; 1.
Pfam; PF01349; Flavi_NS4B; 1.
Pfam; PF00972; Flavi_NS5; 1.
Pfam; PF01570; Flavi_propep; 1.
Pfam; PF01728; FtsJ; 1.
Pfam; PF00949; Peptidase_S7; 1.
PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF101257; SSF101257; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
TIGRFAMs; TIGR04240; flavi_E_stem; 1.
PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; 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.
CHAIN 1 3434 Genome polyprotein.
/FTId=PRO_0000405163.
CHAIN 1 105 Capsid protein C.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037782.
PROPEP 106 125 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3.
/FTId=PRO_0000405164.
CHAIN 126 292 Protein prM.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000405165.
CHAIN 126 217 Peptide pr.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037783.
CHAIN 218 292 Small envelope protein M.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037784.
CHAIN 293 793 Envelope protein E.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037785.
CHAIN 794 1145 Non-structural protein 1.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037786.
CHAIN 1146 1372 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037787.
CHAIN 1373 1503 Serine protease subunit NS2B.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037788.
CHAIN 1504 2122 Serine protease NS3.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037789.
CHAIN 2123 2248 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037790.
PEPTIDE 2249 2271 Peptide 2k.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000405166.
CHAIN 2272 2529 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037791.
CHAIN 2530 3434 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037792.
TOPO_DOM 2 110 Cytoplasmic. {ECO:0000255}.
TRANSMEM 111 131 Helical. {ECO:0000255}.
TOPO_DOM 132 251 Extracellular. {ECO:0000255}.
TRANSMEM 252 272 Helical. {ECO:0000255}.
TOPO_DOM 273 277 Cytoplasmic. {ECO:0000255}.
TRANSMEM 278 292 Helical. {ECO:0000305}.
TOPO_DOM 293 745 Extracellular. {ECO:0000255}.
TRANSMEM 746 766 Helical. {ECO:0000255}.
TOPO_DOM 767 772 Cytoplasmic. {ECO:0000255}.
TRANSMEM 773 793 Helical. {ECO:0000255}.
TOPO_DOM 794 1218 Extracellular. {ECO:0000255}.
TRANSMEM 1219 1239 Helical. {ECO:0000255}.
TOPO_DOM 1240 1249 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1250 1270 Helical. {ECO:0000255}.
TOPO_DOM 1271 1286 Lumenal. {ECO:0000255}.
TRANSMEM 1287 1307 Helical. {ECO:0000255}.
TOPO_DOM 1308 1308 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1309 1329 Helical. {ECO:0000255}.
TOPO_DOM 1330 1340 Lumenal. {ECO:0000255}.
TRANSMEM 1341 1361 Helical. {ECO:0000255}.
TOPO_DOM 1362 1373 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1374 1394 Helical. {ECO:0000255}.
TOPO_DOM 1395 1397 Lumenal. {ECO:0000255}.
TRANSMEM 1398 1418 Helical. {ECO:0000255}.
TOPO_DOM 1419 1475 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1476 1496 Helical. {ECO:0000255}.
TOPO_DOM 1497 2172 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2173 2193 Helical. {ECO:0000255}.
TOPO_DOM 2194 2197 Lumenal. {ECO:0000255}.
INTRAMEM 2198 2218 Helical. {ECO:0000255}.
TOPO_DOM 2219 2220 Lumenal. {ECO:0000255}.
TRANSMEM 2221 2241 Helical. {ECO:0000255}.
TOPO_DOM 2242 2256 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2257 2271 Helical; Note=Signal for NS4B.
{ECO:0000305}.
TOPO_DOM 2272 2309 Lumenal. {ECO:0000255}.
INTRAMEM 2310 2330 Helical. {ECO:0000255}.
TOPO_DOM 2331 2366 Lumenal. {ECO:0000255}.
TRANSMEM 2367 2394 Helical. {ECO:0000255}.
TOPO_DOM 2395 2446 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2447 2467 Helical. {ECO:0000255}.
TOPO_DOM 2468 2498 Lumenal. {ECO:0000255}.
TRANSMEM 2499 2519 Helical. {ECO:0000255}.
TOPO_DOM 2520 3434 Cytoplasmic. {ECO:0000255}.
DOMAIN 1504 1681 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1684 1840 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1851 2016 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2530 2795 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3059 3211 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1697 1704 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 2 15 Interaction with host EXOC1.
{ECO:0000250|UniProtKB:P06935}.
REGION 37 72 Hydrophobic; homodimerization of capsid
protein C.
{ECO:0000250|UniProtKB:P29990}.
REGION 390 403 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
REGION 1426 1465 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
REGION 1688 1691 Important for RNA-binding.
{ECO:0000250|UniProtKB:P14340}.
REGION 2167 2171 Regulates the ATPase activity of NS3
helicase. {ECO:0000250|UniProtKB:Q9Q6P4}.
MOTIF 1788 1791 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
ACT_SITE 1554 1554 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1578 1578 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1638 1638 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 2590 2590 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2675 2675 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2711 2711 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2747 2747 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2969 2969 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 2973 2973 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:P14335}.
METAL 2978 2978 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 2981 2981 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 3246 3246 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:P14335}.
METAL 3262 3262 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
METAL 3381 3381 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
BINDING 2542 2542 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2545 2545 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2546 2546 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2548 2548 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2557 2557 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2585 2585 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2615 2615 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2616 2616 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2633 2633 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2634 2634 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2660 2660 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2661 2661 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2679 2679 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2742 2742 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2744 2744 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2749 2749 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 105 106 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 125 126 Cleavage; by host signal peptidase.
{ECO:0000269|PubMed:20207389}.
SITE 217 218 Cleavage; by host furin. {ECO:0000250}.
SITE 292 293 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 793 794 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 1145 1146 Cleavage; by host.
{ECO:0000269|PubMed:26377679}.
SITE 1372 1373 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 1503 1504 Cleavage; by autolysis. {ECO:0000255}.
SITE 1961 1961 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 1964 1964 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 2122 2123 Cleavage; by autolysis. {ECO:0000255}.
SITE 2248 2249 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 2271 2272 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 2529 2530 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 2590 2590 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2675 2675 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2676 2676 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2711 2711 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2747 2747 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
MOD_RES 2585 2585 Phosphoserine.
{ECO:0000250|UniProtKB:P03314}.
CARBOHYD 140 140 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:P14335}.
CARBOHYD 446 446 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 923 923 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000269|PubMed:11514736}.
CARBOHYD 968 968 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000269|PubMed:11514736}.
CARBOHYD 1000 1000 N-linked (GlcNAc...) (high mannose)
asparagine; by host.
{ECO:0000269|PubMed:11514736}.
DISULFID 295 322 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 352 413 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 352 408 {ECO:0000250|UniProtKB:P06935}.
DISULFID 366 397 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 384 413 {ECO:0000250|UniProtKB:P06935}.
DISULFID 384 408 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 482 580 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 597 628 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 797 808 {ECO:0000269|PubMed:11514736}.
DISULFID 848 936 {ECO:0000269|PubMed:11514736}.
DISULFID 972 1016 {ECO:0000269|PubMed:11514736}.
DISULFID 1073 1122 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 1084 1105 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 1106 1109 {ECO:0000250|UniProtKB:Q9Q6P4}.
MUTAGEN 121 124 GFAA->PQAQ: Increased cleavage of prM.
{ECO:0000269|PubMed:9499070}.
CONFLICT 115 115 L -> V (in Ref. 2; CAA27184).
{ECO:0000305}.
CONFLICT 754 754 P -> Q (in Ref. 2; CAA27184).
{ECO:0000305}.
CONFLICT 960 960 G -> V (in Ref. 2; CAA27184).
{ECO:0000305}.
CONFLICT 1485 1485 R -> W (in Ref. 2; CAA27184).
{ECO:0000305}.
CONFLICT 1779 1779 V -> G (in Ref. 2; CAA27184).
{ECO:0000305}.
STRAND 1423 1430 {ECO:0000244|PDB:2WV9}.
STRAND 1436 1440 {ECO:0000244|PDB:2WV9}.
STRAND 1523 1531 {ECO:0000244|PDB:2WV9}.
STRAND 1536 1545 {ECO:0000244|PDB:2WV9}.
STRAND 1548 1551 {ECO:0000244|PDB:2WV9}.
HELIX 1553 1556 {ECO:0000244|PDB:2WV9}.
STRAND 1564 1568 {ECO:0000244|PDB:2WV9}.
STRAND 1570 1574 {ECO:0000244|PDB:2WV9}.
TURN 1575 1578 {ECO:0000244|PDB:2WV9}.
STRAND 1579 1585 {ECO:0000244|PDB:2WV9}.
STRAND 1598 1602 {ECO:0000244|PDB:2WV9}.
STRAND 1610 1614 {ECO:0000244|PDB:2WV9}.
STRAND 1617 1619 {ECO:0000244|PDB:2WV9}.
STRAND 1622 1624 {ECO:0000244|PDB:2WV9}.
STRAND 1626 1629 {ECO:0000244|PDB:2WV9}.
HELIX 1635 1637 {ECO:0000244|PDB:2WV9}.
STRAND 1641 1643 {ECO:0000244|PDB:2WV9}.
STRAND 1649 1658 {ECO:0000244|PDB:2WV9}.
STRAND 1660 1662 {ECO:0000244|PDB:2WV9}.
STRAND 1664 1669 {ECO:0000244|PDB:2WV9}.
HELIX 1684 1687 {ECO:0000244|PDB:2V8O}.
STRAND 1692 1695 {ECO:0000244|PDB:2V8O}.
STRAND 1699 1701 {ECO:0000244|PDB:2V8O}.
TURN 1703 1706 {ECO:0000244|PDB:2V8O}.
HELIX 1707 1717 {ECO:0000244|PDB:2V8O}.
STRAND 1722 1728 {ECO:0000244|PDB:2V8O}.
HELIX 1729 1738 {ECO:0000244|PDB:2V8O}.
TURN 1739 1741 {ECO:0000244|PDB:2V8O}.
STRAND 1744 1746 {ECO:0000244|PDB:2V8O}.
STRAND 1761 1765 {ECO:0000244|PDB:2V8O}.
HELIX 1766 1773 {ECO:0000244|PDB:2V8O}.
STRAND 1775 1777 {ECO:0000244|PDB:2V8O}.
STRAND 1783 1789 {ECO:0000244|PDB:2V8O}.
HELIX 1795 1809 {ECO:0000244|PDB:2V8O}.
STRAND 1814 1818 {ECO:0000244|PDB:2V8O}.
STRAND 1836 1840 {ECO:0000244|PDB:2V8O}.
STRAND 1849 1851 {ECO:0000244|PDB:2V8O}.
HELIX 1853 1857 {ECO:0000244|PDB:2V8O}.
STRAND 1862 1865 {ECO:0000244|PDB:2V8O}.
HELIX 1869 1881 {ECO:0000244|PDB:2V8O}.
STRAND 1886 1889 {ECO:0000244|PDB:2V8O}.
TURN 1891 1893 {ECO:0000244|PDB:2V8O}.
HELIX 1894 1901 {ECO:0000244|PDB:2V8O}.
STRAND 1907 1911 {ECO:0000244|PDB:2V8O}.
HELIX 1913 1916 {ECO:0000244|PDB:2V8O}.
STRAND 1924 1928 {ECO:0000244|PDB:2V8O}.
STRAND 1935 1938 {ECO:0000244|PDB:2V8O}.
STRAND 1944 1947 {ECO:0000244|PDB:2V8O}.
STRAND 1950 1952 {ECO:0000244|PDB:2WV9}.
HELIX 1955 1962 {ECO:0000244|PDB:2V8O}.
STRAND 1974 1978 {ECO:0000244|PDB:2V8O}.
HELIX 1990 1999 {ECO:0000244|PDB:2V8O}.
TURN 2005 2007 {ECO:0000244|PDB:2WV9}.
HELIX 2014 2016 {ECO:0000244|PDB:2V8O}.
TURN 2024 2027 {ECO:0000244|PDB:2V8O}.
HELIX 2031 2042 {ECO:0000244|PDB:2V8O}.
HELIX 2048 2055 {ECO:0000244|PDB:2V8O}.
TURN 2056 2058 {ECO:0000244|PDB:2V8O}.
HELIX 2064 2067 {ECO:0000244|PDB:2V8O}.
HELIX 2072 2074 {ECO:0000244|PDB:2V8O}.
STRAND 2078 2081 {ECO:0000244|PDB:2V8O}.
STRAND 2098 2101 {ECO:0000244|PDB:2V8O}.
HELIX 2102 2104 {ECO:0000244|PDB:2V8O}.
HELIX 2108 2118 {ECO:0000244|PDB:2V8O}.
HELIX 2537 2546 {ECO:0000244|PDB:2PX2}.
HELIX 2550 2557 {ECO:0000244|PDB:2PX2}.
TURN 2558 2560 {ECO:0000244|PDB:2PX2}.
STRAND 2562 2564 {ECO:0000244|PDB:2PX2}.
HELIX 2566 2568 {ECO:0000244|PDB:2PX2}.
TURN 2571 2576 {ECO:0000244|PDB:2PXA}.
STRAND 2578 2580 {ECO:0000244|PDB:2PX5}.
STRAND 2584 2586 {ECO:0000244|PDB:2PXA}.
HELIX 2587 2596 {ECO:0000244|PDB:2PX2}.
STRAND 2604 2609 {ECO:0000244|PDB:2PX2}.
HELIX 2615 2620 {ECO:0000244|PDB:2PX2}.
STRAND 2626 2632 {ECO:0000244|PDB:2PX2}.
HELIX 2650 2652 {ECO:0000244|PDB:2PX2}.
STRAND 2653 2656 {ECO:0000244|PDB:2PX2}.
HELIX 2661 2663 {ECO:0000244|PDB:2PX2}.
STRAND 2670 2674 {ECO:0000244|PDB:2PX2}.
HELIX 2683 2701 {ECO:0000244|PDB:2PX2}.
STRAND 2706 2713 {ECO:0000244|PDB:2PX2}.
HELIX 2718 2731 {ECO:0000244|PDB:2PX2}.
STRAND 2734 2736 {ECO:0000244|PDB:2PX2}.
STRAND 2748 2751 {ECO:0000244|PDB:2PX2}.
HELIX 2758 2771 {ECO:0000244|PDB:2PX2}.
TURN 2772 2774 {ECO:0000244|PDB:2PX4}.
STRAND 2782 2784 {ECO:0000244|PDB:2PX2}.
SEQUENCE 3434 AA; 380577 MW; 20D7110791C567A9 CRC64;
MSKKPGGPGK PRVVNMLKRG IPRVFPLVGV KRVVMNLLDG RGPIRFVLAL LAFFRFTALA
PTKALMRRWK SVNKTTAMKH LTSFKKELGT LIDVVNKRGK KQKKRGGSET SVLMLIFMLI
GFAAALKLST FQGKIMMTVN ATDIADVIAI PTPKGPNQCW IRAIDIGFMC DDTITYECPK
LESGNDPEDI DCWCDKQAVY VNYGRCTRAR HSKRSRRSIT VQTHGESTLV NKKDAWLDST
KATRYLTKTE NWIIRNPGYA LVAVVLGWML GSNTGQKVIF TVLLLLVAPA YSFNCLGMSS
RDFIEGASGA TWVDLVLEGD SCITIMAADK PTLDIRMMNI EATNLALVRN YCYAATVSDV
STVSNCPTTG ESHNTKRADH NYLCKRGVTD RGWGNGCGLF GKGSIDTCAK FTCSNSAAGR
LILPEDIKYE VGVFVHGSTD STSHGNYSTQ IGANQAVRFT ISPNAPAITA KMGDYGEVTV
ECEPRSGLNT EAYYVMTIGT KHFLVHREWF NDLLLPWTSP ASTEWRNREI LVEFEEPHAT
KQSVVALGSQ EGALHQALAG AIPVEFSSST LKLTSGHLKC RVKMEKLKLK GTTYGMCTEK
FTFSKNPADT GHGTVVLELQ YTGSDGPCKI PISSVASLND MTPVGRMVTA NPYVASSTAN
AKVLVEIEPP FGDSYIVVGR GDKQINHHWH KEGSSIGKAF STTLKGAQRL AALGDTAWDF
GSVGGVFNSI GKAVHQVFGG AFRTLFGGMS WISPGLLGAL LLWMGVNARD KSIALAFLAT
GGVLLFLATN VHADTGCAID ITRRELKCGS GIFIHNDVEA WIDRYKYLPE TPKQLAKVVE
NAHKSGICGI RSVNRFEHQM WESVRDELNA LLKENAIDLS VVVEKQKGMY RAAPNRLRLT
VEELDIGWKA WGKSLLFAAE LANSTFVVDG PETAECPNSK RAWNSFEIED FGFGITSTRG
WLKLREENTS ECDSTIIGTA VKGNHAVHSD LSYWIESGLN GTWKLERAIF GEVKSCTWPE
THTLWGDAVE ETELIIPVTL AGPRSKHNRR EGYKVQVQGP WDEEDIKLDF DYCPGTTVTV
SEHCGKRGPS VRTTTDSGKL VTDWCCRSCT LPPLRFTTAS GCWYGMEIRP MKHDESTLVK
SRVQAFNGDM IDPFQLGLLV MFLATQEVLR KRWTARLTLP AAVGALLVLL LGGITYTDLV
RYLILVGSAF AESNNGGDVI HLALIAVFKV QPAFLVASLT RSRWTNQENL VLVLGAAFFQ
MAASDLELTI PGLLNSAATA WMVLRAMAFP STSAIAMPML AMLAPGMRML HLDTYRIVLL
LIGICSLLNE RRRSVEKKKG AVLIGLALTS TGYFSPTIMA AGLMICNPNK KRGWPATEVL
TAVGLMFAIV GGLAELDIDS MSVPFTIAGL MLVSYVISGK ATDMWLERAA DVSWEAGAAI
TGTSERLDVQ LDDDGDFHLL NDPGVPWKIW VLRMTCLSVA AITPRAILPS AFGYWLTLKY
TKRGGVFWDT PSPKVYPKGD TTPGVYRIMA RGILGRYQAG VGVMHEGVFH TLWHTTRGAA
IMSGEGRLTP YWGNVKEDRV TYGGPWKLDQ KWNGVDDVQM IVVEPGKPAI NVQTKPGIFK
TAHGEIGAVS LDYPIGTSGS PIVNSNGEII GLYGNGVILG NGAYVSAIVQ GERVEEPVPE
AYNPEMLKKR QLTVLDLHPG AGKTRRILPQ IIKDAIQKRL RTAVLAPTRV VAAEMAEALR
GLPVRYLTPA VQREHSGNEI VDVMCHATLT HRLMSPLRVP NYNLFVMDEA HFTDPASIAA
RGYIATRVEA GEAAAIFMTA TPPGTSDPFP DTNSPVHDVS SEIPDRAWSS GFEWITDYAG
KTVWFVASVK MSNEIAQCLQ RAGKRVIQLN RKSYDTEYPK CKNGDWDFVI TTDISEMGAN
FGASRVIDCR KSVKPTILDE GEGRVILSVP SAITSASAAQ RRGRVGRNPS QIGDEYHYGG
GTSEDDTMLA HWTEAKILLD NIHLPNGLVA QLYGPERDKT YTMDGEYRLR GEERKTFLEL
IKTADLPVWL AYKVASNGIQ YNDRKWCFDG PRSNIILEDN NEVEIITRIG ERKVLKPRWL
DARVYSDHQS LKWFKDFAAG KRSAIGFFEV LGRMPEHFAG KTREALDTMY LVATSEKGGK
AHRMALEELP DALETITLIA ALGVMTAGFF LLMMQRKGIG KLGLGALVLV VATFFLWMSD
VSGTKIAGVL LLALLMMVVL IPEPEKQRSQ TDNQLAVFLI CVLLVVGLVA ANEYGMLERT
KTDIRNLFGK SLIEENEVHI PPFDFFTLDL KPATAWALYG GSTVVLTPLI KHLVTSQYVT
TSLASINAQA GSLFTLPKGI PFTDFDLSVA LVFLGCWGQV TLTTLIMATI LVTLHYGYLL
PGWQAEALRA AQKRTAAGIM KNAVVDGIVA TDVPELERTT PQMQKRLGQI LLVLASVAAV
CVNPRITTIR EAGILCTAAA LTLWDNNASA AWNSTTATGL CHVMRGSWIA GASIAWTLIK
NAEKPAFKRG RAGGRTLGEQ WKEKLNAMGK EEFFSYRKEA ILEVDRTEAR RARREGNKVG
GHPVSRGTAK LRWLVERRFV QPIGKVVDLG CGRGGWSYYA ATMKNVQEVR GYTKGGPGHE
EPMLMQSYGW NIVTMKSGVD VFYKPSEISD TLLCDIGESS PSAEIEEQRT LRILEMVSDW
LSRGPKEFCI KILCPYMPKV IEKLESLQRR FGGGLVRVPL SRNSNHEMYW VSGASGNIVH
AVNMTSQVLI GRMDKKIWKG PKYEEDVNLG SGTRAVGKGV QHTDYKRIKS RIEKLKEEYA
ATWHTDDNHP YRTWTYHGSY EVKPSGSAST LVNGVVRLLS KPWDAITGVT TMAMTDTTPF
GQQRVFKEKV DTKAPEPPQG VKTVMDETTN WLWAYLARNK KARLCTREEF VKKVNSHAAL
GAMFEEQNQW KNAREAVEDP KFWEMVDEER ECHLRGECRT CIYNMMGKRE KKPGEFGKAK
GSRAIWFMWL GARFLEFEAL GFLNEDHWMS RENSGGGVEG AGIQKLGYIL RDVAQKPGGK
IYADDTAGWD TRITQADLEN EAKVLELMEG EQRTLARAII ELTYRHKVVK VMRPAAGGKT
VMDVISREDQ RGSGQVVTYA LNTFTNIAVQ LVRLMEAEAV IGPDDIESIE RKKKFAVRTW
LFENAEERVQ RMAVSGDDCV VKPLDDRFST ALHFLNAMSK VRKDIQEWKP SQGWYDWQQV
PFCSNHFQEV IMKDGRTLVV PCRGQDELIG RARISPGSGW NVRDTACLAK AYAQMWLVLY
FHRRDLRLMA NAICSSVPVD WVPTGRTTWS IHGKGEWMTT EDMLSVWNRV WILENEWMED
KTTVSDWTEV PYVGKREDIW CGSLIGTRTR ATWAENIYAA INQVRSVIGK EKYVDYVQSL
RRYEETHVSE DRVL


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