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 POLG_JAEV1              Reviewed;        3432 AA.
P27395; Q82920; Q82921; Q82922; Q82923; Q82924; Q82925; Q82926;
Q82927; Q82928;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
22-NOV-2017, entry version 147.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Capsid protein C;
AltName: Full=Core protein;
Contains:
RecName: Full=Protein prM;
Contains:
RecName: Full=Peptide pr;
Contains:
RecName: Full=Small envelope protein M;
AltName: Full=Matrix protein;
Contains:
RecName: Full=Envelope protein E;
Contains:
RecName: Full=Non-structural protein 1;
Short=NS1;
Contains:
RecName: Full=Non-structural protein 2A;
Short=NS2A;
Contains:
RecName: Full=Serine protease subunit NS2B;
AltName: Full=Flavivirin protease NS2B regulatory subunit;
AltName: Full=Non-structural protein 2B;
Contains:
RecName: Full=Serine protease NS3;
EC=3.4.21.91;
EC=3.6.1.15;
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 {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;
Japanese encephalitis virus (strain SA-14).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; Japanese encephalitis virus group.
NCBI_TaxID=11073;
NCBI_TaxID=8899; Ardeidae (herons).
NCBI_TaxID=9913; Bos taurus (Bovine).
NCBI_TaxID=308713; Culex gelidus.
NCBI_TaxID=7178; Culex tritaeniorhynchus (Mosquito).
NCBI_TaxID=9796; Equus caballus (Horse).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2371768; DOI=10.1016/0042-6822(90)90519-W;
Nitayaphan S., Grant J.A., Chang G.J.J., Trent D.W.;
"Nucleotide sequence of the virulent SA-14 strain of Japanese
encephalitis virus and its attenuated vaccine derivative, SA-14-14-
2.";
Virology 177:541-552(1990).
[2]
SUBCELLULAR LOCATION (RNA-DIRECTED RNA POLYMERASE NS5).
STRAIN=P20778;
PubMed=16699025; DOI=10.1128/JVI.01982-05;
Uchil P.D., Kumar A.V., Satchidanandam V.;
"Nuclear localization of flavivirus RNA synthesis in infected cells.";
J. Virol. 80:5451-5464(2006).
[3]
FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5).
PubMed=16731929; DOI=10.1128/JVI.02714-05;
Lin R.J., Chang B.L., Yu H.P., Liao C.L., Lin Y.L.;
"Blocking of interferon-induced Jak-Stat signaling by Japanese
encephalitis virus NS5 through a protein tyrosine phosphatase-mediated
mechanism.";
J. Virol. 80:5908-5918(2006).
[4] {ECO:0000244|PDB:2Z83}
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1685-2123, AND MUTAGENESIS OF
GLY-1703; LYS-1704; THR-1705; GLN-1961; ARG-1962; ARG-1965 AND
ARG-1968.
PubMed=18201743; DOI=10.1016/j.virol.2007.12.018;
Yamashita T., Unno H., Mori Y., Tani H., Moriishi K., Takamizawa A.,
Agoh M., Tsukihara T., Matsuura Y.;
"Crystal structure of the catalytic domain of Japanese encephalitis
virus NS3 helicase/nucleoside triphosphatase at a resolution of 1.8
A.";
Virology 373:426-436(2008).
[5] {ECO:0000244|PDB:3P54}
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 295-700.
PubMed=22156523; DOI=10.1128/JVI.06072-11;
Luca V.C., AbiMansour J., Nelson C.A., Fremont D.H.;
"Crystal structure of the Japanese encephalitis virus envelope
protein.";
J. Virol. 86:2337-2346(2012).
[6] {ECO:0000244|PDB:4K6M}
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2528-3432 IN COMPLEX WITH
S-ADENOSYL-L-HOMOCYSTEINE AND ZINC.
PubMed=23950717; DOI=10.1371/journal.ppat.1003549;
Lu G., Gong P.;
"Crystal Structure of the full-length Japanese encephalitis virus NS5
reveals a conserved methyltransferase-polymerase interface.";
PLoS Pathog. 9:E1003549-E1003549(2013).
[7] {ECO:0000244|PDB:4HDG, ECO:0000244|PDB:4HDH, ECO:0000244|PDB:4MTP}
X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 2799-3432 IN COMPLEX WITH
ATP; GTP AND ZINC.
PubMed=24293643; DOI=10.1093/nar/gkt1106;
Surana P., Satchidanandam V., Nair D.T.;
"RNA-dependent RNA polymerase of Japanese encephalitis virus binds the
initiator nucleotide GTP to form a mechanistically important pre-
initiation state.";
Nucleic Acids Res. 42:2758-2773(2014).
-!- 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}.
-!- 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 (By similarity). 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 (PubMed:16731929). Inhibits host TYK2 and STAT2
phosphorylation, thereby preventing activation of JAK-STAT
signaling pathway (PubMed:16731929).
{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:0000250|UniProtKB:Q9Q6P4}.
-!- 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 {ECO:0000250|UniProtKB:P17763}. Host nucleus
{ECO:0000269|PubMed:16699025}. 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Genome polyprotein;
IsoId=P27395-1; Sequence=Displayed;
Name=Structural polyprotein;
IsoId=P0DOH7-1; Sequence=External;
Note=Product of a -1 ribosomal frameshifting.
{ECO:0000250|UniProtKB:P32886};
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=AAA46249.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; M55506; AAA46248.1; -; Genomic_RNA.
EMBL; M55506; AAA46249.1; ALT_INIT; Genomic_RNA.
PIR; A35519; GNWVJS.
PDB; 2Z83; X-ray; 1.80 A; A=1685-2123.
PDB; 3P54; X-ray; 2.10 A; A=295-700.
PDB; 4HDG; X-ray; 2.38 A; A/B=2799-3432.
PDB; 4HDH; X-ray; 2.28 A; A/B=2799-3432.
PDB; 4K6M; X-ray; 2.60 A; A/B=2528-3432.
PDB; 4MTP; X-ray; 3.65 A; A/B/C/D=2799-3432.
PDB; 5WSN; EM; 4.30 A; B/D/F=220-293.
PDBsum; 2Z83; -.
PDBsum; 3P54; -.
PDBsum; 4HDG; -.
PDBsum; 4HDH; -.
PDBsum; 4K6M; -.
PDBsum; 4MTP; -.
PDBsum; 5WSN; -.
ProteinModelPortal; P27395; -.
SMR; P27395; -.
MEROPS; S07.003; -.
OrthoDB; VOG0900007N; -.
BRENDA; 3.6.4.12; 2787.
BRENDA; 3.6.4.13; 2787.
EvolutionaryTrace; P27395; -.
Proteomes; UP000008380; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW.
GO; GO: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; IPR037172; Flavi_capsidC_sf.
InterPro; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
InterPro; IPR001157; Flavi_NS1.
InterPro; IPR000752; Flavi_NS2A.
InterPro; IPR000487; Flavi_NS2B.
InterPro; IPR000404; Flavi_NS4A.
InterPro; IPR001528; Flavi_NS4B.
InterPro; IPR002535; Flavi_propep.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
InterPro; IPR013756; GlyE_cen_dom_subdom2.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR000208; RNA-dir_pol_flavivirus.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01003; Flavi_capsid; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF02832; Flavi_glycop_C; 1.
Pfam; PF00869; Flavi_glycoprot; 1.
Pfam; 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; 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;
Inhibition of host TYK2 by virus; Membrane; Metal-binding;
Methyltransferase; mRNA capping; mRNA processing;
Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
Phosphoprotein; Protease; Ribosomal frameshifting; 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 3432 Genome polyprotein.
/FTId=PRO_0000405188.
CHAIN 1 105 Capsid protein C.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037836.
PROPEP 106 127 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000405189.
CHAIN 128 294 Protein prM.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000405190.
CHAIN 128 219 Peptide pr.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037837.
CHAIN 220 294 Small envelope protein M.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037838.
CHAIN 295 794 Envelope protein E.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037839.
CHAIN 795 1146 Non-structural protein 1.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037840.
CHAIN 1147 1373 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037841.
CHAIN 1374 1504 Serine protease subunit NS2B.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037842.
CHAIN 1505 2123 Serine protease NS3.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037843.
CHAIN 2124 2249 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037844.
PEPTIDE 2250 2272 Peptide 2k.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000405191.
CHAIN 2273 2527 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037845.
CHAIN 2528 3432 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037846.
TOPO_DOM 2 109 Cytoplasmic. {ECO:0000255}.
TRANSMEM 110 130 Helical. {ECO:0000255}.
TOPO_DOM 131 253 Extracellular. {ECO:0000255}.
TRANSMEM 254 274 Helical. {ECO:0000255}.
TOPO_DOM 275 279 Cytoplasmic. {ECO:0000255}.
TRANSMEM 280 294 Helical. {ECO:0000305}.
TOPO_DOM 295 746 Extracellular. {ECO:0000255}.
TRANSMEM 747 767 Helical. {ECO:0000255}.
TOPO_DOM 768 773 Cytoplasmic. {ECO:0000255}.
TRANSMEM 774 794 Helical. {ECO:0000255}.
TOPO_DOM 795 1219 Extracellular. {ECO:0000255}.
TRANSMEM 1220 1240 Helical. {ECO:0000255}.
TOPO_DOM 1241 1250 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1251 1271 Helical. {ECO:0000255}.
TOPO_DOM 1272 1272 Lumenal. {ECO:0000255}.
TRANSMEM 1273 1293 Helical. {ECO:0000255}.
TOPO_DOM 1294 1309 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1310 1330 Helical. {ECO:0000255}.
TOPO_DOM 1331 1341 Lumenal. {ECO:0000255}.
TRANSMEM 1342 1362 Helical. {ECO:0000255}.
TOPO_DOM 1363 1374 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1375 1395 Helical. {ECO:0000255}.
TOPO_DOM 1396 1398 Lumenal. {ECO:0000255}.
TRANSMEM 1399 1419 Helical. {ECO:0000255}.
TOPO_DOM 1420 1476 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1477 1497 Helical. {ECO:0000255}.
TOPO_DOM 1498 2173 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2174 2194 Helical. {ECO:0000255}.
TOPO_DOM 2195 2199 Lumenal. {ECO:0000255}.
INTRAMEM 2200 2220 Helical. {ECO:0000255}.
TOPO_DOM 2221 2221 Lumenal. {ECO:0000255}.
TRANSMEM 2222 2242 Helical. {ECO:0000255}.
TOPO_DOM 2243 2257 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2258 2278 Helical; Note=Signal for NS4B.
{ECO:0000255}.
TOPO_DOM 2279 2311 Lumenal. {ECO:0000255}.
INTRAMEM 2312 2332 Helical. {ECO:0000255}.
TOPO_DOM 2333 2368 Lumenal. {ECO:0000255}.
TRANSMEM 2369 2389 Helical. {ECO:0000255}.
TOPO_DOM 2390 2444 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2445 2465 Helical. {ECO:0000255}.
TOPO_DOM 2466 2469 Lumenal. {ECO:0000255}.
TRANSMEM 2470 2490 Helical. {ECO:0000255}.
TOPO_DOM 2491 3432 Cytoplasmic. {ECO:0000255}.
DOMAIN 1505 1682 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1685 1841 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1852 2017 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2528 2793 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3057 3209 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1698 1705 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 392 405 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
REGION 1427 1466 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
REGION 1689 1692 Important for RNA-binding.
{ECO:0000250|UniProtKB:P14340}.
REGION 2168 2172 Regulates the ATPase activity of NS3
helicase. {ECO:0000250|UniProtKB:Q9Q6P4}.
MOTIF 1789 1792 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
ACT_SITE 1555 1555 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1579 1579 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1639 1639 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 2588 2588 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2673 2673 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2709 2709 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2745 2745 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2967 2967 Zinc 1. {ECO:0000269|PubMed:24293643}.
METAL 2971 2971 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:24293643}.
METAL 2976 2976 Zinc 1. {ECO:0000269|PubMed:24293643}.
METAL 2979 2979 Zinc 1. {ECO:0000269|PubMed:24293643}.
METAL 3244 3244 Zinc 2; via tele nitrogen.
{ECO:0000269|PubMed:24293643}.
METAL 3260 3260 Zinc 2. {ECO:0000269|PubMed:24293643}.
METAL 3379 3379 Zinc 2. {ECO:0000269|PubMed:24293643}.
BINDING 2540 2540 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2543 2543 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2544 2544 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2546 2546 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2555 2555 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2583 2583 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2613 2613 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2614 2614 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2631 2631 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2632 2632 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2658 2658 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2659 2659 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2677 2677 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2740 2740 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2742 2742 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2747 2747 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 105 106 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 127 128 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 219 220 Cleavage; by host furin. {ECO:0000250}.
SITE 294 295 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 794 795 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 1146 1147 Cleavage; by host. {ECO:0000250}.
SITE 1373 1374 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 1504 1505 Cleavage; by autolysis. {ECO:0000255}.
SITE 1962 1962 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 1965 1965 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 2123 2124 Cleavage; by autolysis. {ECO:0000255}.
SITE 2249 2250 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 2272 2273 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 2527 2528 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 2551 2551 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2588 2588 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2673 2673 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2674 2674 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2709 2709 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2745 2745 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
MOD_RES 2583 2583 Phosphoserine.
{ECO:0000250|UniProtKB:P03314}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:P14335}.
CARBOHYD 448 448 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 924 924 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:Q9Q6P4}.
CARBOHYD 1001 1001 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 297 324 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 354 415 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 354 410 {ECO:0000250|UniProtKB:P06935}.
DISULFID 368 399 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 386 415 {ECO:0000250|UniProtKB:P06935}.
DISULFID 386 410 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 484 581 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 598 629 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 798 809 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 849 937 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 973 1017 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 1074 1123 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 1085 1106 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 1107 1110 {ECO:0000250|UniProtKB:Q9Q6P4}.
MUTAGEN 1703 1703 G->A: Complete loss of both the ATPase
and helicase activities.
{ECO:0000269|PubMed:18201743}.
MUTAGEN 1704 1704 K->D,E,H,N,Q,R: Complete loss of both the
ATPase and helicase activities.
{ECO:0000269|PubMed:18201743}.
MUTAGEN 1705 1705 T->A: Complete loss of both the ATPase
and helicase activities.
{ECO:0000269|PubMed:18201743}.
MUTAGEN 1961 1961 Q->A: 80% loss of ATPase activity.
{ECO:0000269|PubMed:18201743}.
MUTAGEN 1962 1962 R->A: 90% loss of ATPase activity.
{ECO:0000269|PubMed:18201743}.
MUTAGEN 1965 1965 R->A: Complete loss of ATPase activity.
{ECO:0000269|PubMed:18201743}.
MUTAGEN 1968 1968 R->A: Complete loss of ATPase activity.
{ECO:0000269|PubMed:18201743}.
STRAND 301 307 {ECO:0000244|PDB:3P54}.
STRAND 313 322 {ECO:0000244|PDB:3P54}.
STRAND 324 328 {ECO:0000244|PDB:3P54}.
STRAND 335 344 {ECO:0000244|PDB:3P54}.
STRAND 348 366 {ECO:0000244|PDB:3P54}.
HELIX 377 380 {ECO:0000244|PDB:3P54}.
STRAND 384 394 {ECO:0000244|PDB:3P54}.
HELIX 395 397 {ECO:0000244|PDB:3P54}.
STRAND 403 423 {ECO:0000244|PDB:3P54}.
STRAND 428 437 {ECO:0000244|PDB:3P54}.
TURN 443 447 {ECO:0000244|PDB:3P54}.
HELIX 449 454 {ECO:0000244|PDB:3P54}.
STRAND 458 463 {ECO:0000244|PDB:3P54}.
STRAND 465 467 {ECO:0000244|PDB:3P54}.
STRAND 469 473 {ECO:0000244|PDB:3P54}.
HELIX 475 477 {ECO:0000244|PDB:3P54}.
STRAND 478 485 {ECO:0000244|PDB:3P54}.
HELIX 486 488 {ECO:0000244|PDB:3P54}.
STRAND 494 500 {ECO:0000244|PDB:3P54}.
STRAND 503 508 {ECO:0000244|PDB:3P54}.
TURN 509 514 {ECO:0000244|PDB:3P54}.
STRAND 519 521 {ECO:0000244|PDB:3P54}.
STRAND 524 528 {ECO:0000244|PDB:3P54}.
HELIX 530 533 {ECO:0000244|PDB:3P54}.
STRAND 534 540 {ECO:0000244|PDB:3P54}.
STRAND 543 548 {ECO:0000244|PDB:3P54}.
HELIX 553 559 {ECO:0000244|PDB:3P54}.
STRAND 561 575 {ECO:0000244|PDB:3P54}.
STRAND 578 584 {ECO:0000244|PDB:3P54}.
TURN 591 594 {ECO:0000244|PDB:3P54}.
STRAND 602 610 {ECO:0000244|PDB:3P54}.
STRAND 612 614 {ECO:0000244|PDB:3P54}.
STRAND 616 622 {ECO:0000244|PDB:3P54}.
STRAND 628 630 {ECO:0000244|PDB:3P54}.
STRAND 633 638 {ECO:0000244|PDB:3P54}.
STRAND 641 644 {ECO:0000244|PDB:3P54}.
STRAND 646 650 {ECO:0000244|PDB:3P54}.
STRAND 662 669 {ECO:0000244|PDB:3P54}.
STRAND 672 681 {ECO:0000244|PDB:3P54}.
HELIX 682 684 {ECO:0000244|PDB:3P54}.
STRAND 686 692 {ECO:0000244|PDB:3P54}.
HELIX 1686 1688 {ECO:0000244|PDB:2Z83}.
STRAND 1693 1696 {ECO:0000244|PDB:2Z83}.
TURN 1704 1707 {ECO:0000244|PDB:2Z83}.
HELIX 1708 1718 {ECO:0000244|PDB:2Z83}.
STRAND 1723 1727 {ECO:0000244|PDB:2Z83}.
HELIX 1730 1739 {ECO:0000244|PDB:2Z83}.
TURN 1740 1742 {ECO:0000244|PDB:2Z83}.
STRAND 1745 1747 {ECO:0000244|PDB:2Z83}.
STRAND 1761 1766 {ECO:0000244|PDB:2Z83}.
HELIX 1767 1775 {ECO:0000244|PDB:2Z83}.
STRAND 1784 1790 {ECO:0000244|PDB:2Z83}.
HELIX 1796 1810 {ECO:0000244|PDB:2Z83}.
STRAND 1815 1819 {ECO:0000244|PDB:2Z83}.
STRAND 1837 1841 {ECO:0000244|PDB:2Z83}.
HELIX 1854 1858 {ECO:0000244|PDB:2Z83}.
STRAND 1863 1866 {ECO:0000244|PDB:2Z83}.
HELIX 1870 1882 {ECO:0000244|PDB:2Z83}.
STRAND 1887 1891 {ECO:0000244|PDB:2Z83}.
HELIX 1894 1898 {ECO:0000244|PDB:2Z83}.
HELIX 1899 1901 {ECO:0000244|PDB:2Z83}.
STRAND 1902 1904 {ECO:0000244|PDB:2Z83}.
STRAND 1908 1914 {ECO:0000244|PDB:2Z83}.
STRAND 1925 1929 {ECO:0000244|PDB:2Z83}.
STRAND 1936 1939 {ECO:0000244|PDB:2Z83}.
STRAND 1941 1943 {ECO:0000244|PDB:2Z83}.
STRAND 1945 1948 {ECO:0000244|PDB:2Z83}.
HELIX 1956 1963 {ECO:0000244|PDB:2Z83}.
STRAND 1975 1979 {ECO:0000244|PDB:2Z83}.
HELIX 1991 2001 {ECO:0000244|PDB:2Z83}.
HELIX 2015 2020 {ECO:0000244|PDB:2Z83}.
TURN 2025 2028 {ECO:0000244|PDB:2Z83}.
HELIX 2032 2043 {ECO:0000244|PDB:2Z83}.
HELIX 2049 2057 {ECO:0000244|PDB:2Z83}.
HELIX 2066 2068 {ECO:0000244|PDB:2Z83}.
HELIX 2073 2075 {ECO:0000244|PDB:2Z83}.
STRAND 2085 2087 {ECO:0000244|PDB:2Z83}.
STRAND 2093 2095 {ECO:0000244|PDB:2Z83}.
STRAND 2099 2102 {ECO:0000244|PDB:2Z83}.
HELIX 2103 2106 {ECO:0000244|PDB:2Z83}.
HELIX 2109 2120 {ECO:0000244|PDB:2Z83}.
HELIX 2535 2544 {ECO:0000244|PDB:4K6M}.
HELIX 2548 2554 {ECO:0000244|PDB:4K6M}.
TURN 2555 2558 {ECO:0000244|PDB:4K6M}.
STRAND 2560 2562 {ECO:0000244|PDB:4K6M}.
HELIX 2565 2572 {ECO:0000244|PDB:4K6M}.
HELIX 2585 2593 {ECO:0000244|PDB:4K6M}.
TURN 2594 2596 {ECO:0000244|PDB:4K6M}.
STRAND 2602 2607 {ECO:0000244|PDB:4K6M}.
HELIX 2613 2619 {ECO:0000244|PDB:4K6M}.
STRAND 2624 2630 {ECO:0000244|PDB:4K6M}.
HELIX 2648 2650 {ECO:0000244|PDB:4K6M}.
STRAND 2651 2654 {ECO:0000244|PDB:4K6M}.
HELIX 2659 2661 {ECO:0000244|PDB:4K6M}.
STRAND 2668 2672 {ECO:0000244|PDB:4K6M}.
HELIX 2681 2699 {ECO:0000244|PDB:4K6M}.
STRAND 2704 2711 {ECO:0000244|PDB:4K6M}.
HELIX 2716 2729 {ECO:0000244|PDB:4K6M}.
STRAND 2732 2734 {ECO:0000244|PDB:4K6M}.
STRAND 2746 2749 {ECO:0000244|PDB:4K6M}.
HELIX 2756 2770 {ECO:0000244|PDB:4K6M}.
STRAND 2780 2782 {ECO:0000244|PDB:4K6M}.
HELIX 2802 2816 {ECO:0000244|PDB:4HDH}.
TURN 2817 2820 {ECO:0000244|PDB:4HDH}.
STRAND 2830 2839 {ECO:0000244|PDB:4HDH}.
HELIX 2852 2856 {ECO:0000244|PDB:4HDH}.
HELIX 2859 2863 {ECO:0000244|PDB:4HDH}.
HELIX 2865 2868 {ECO:0000244|PDB:4HDH}.
STRAND 2870 2872 {ECO:0000244|PDB:4K6M}.
HELIX 2877 2887 {ECO:0000244|PDB:4HDH}.
HELIX 2897 2914 {ECO:0000244|PDB:4HDH}.
TURN 2915 2917 {ECO:0000244|PDB:4K6M}.
HELIX 2925 2932 {ECO:0000244|PDB:4HDH}.
TURN 2933 2935 {ECO:0000244|PDB:4HDH}.
HELIX 2943 2945 {ECO:0000244|PDB:4K6M}.
TURN 2946 2948 {ECO:0000244|PDB:4HDH}.
HELIX 2951 2956 {ECO:0000244|PDB:4HDH}.
HELIX 2958 2972 {ECO:0000244|PDB:4HDH}.
STRAND 2981 2987 {ECO:0000244|PDB:4HDH}.
STRAND 2989 2991 {ECO:0000244|PDB:4K6M}.
TURN 2994 2996 {ECO:0000244|PDB:4HDH}.
STRAND 3001 3005 {ECO:0000244|PDB:4HDH}.
HELIX 3008 3018 {ECO:0000244|PDB:4HDH}.
HELIX 3020 3023 {ECO:0000244|PDB:4HDH}.
TURN 3024 3027 {ECO:0000244|PDB:4HDH}.
HELIX 3029 3032 {ECO:0000244|PDB:4HDH}.
STRAND 3033 3035 {ECO:0000244|PDB:4HDH}.
HELIX 3041 3053 {ECO:0000244|PDB:4HDH}.
STRAND 3054 3057 {ECO:0000244|PDB:4HDH}.
HELIX 3067 3069 {ECO:0000244|PDB:4HDH}.
HELIX 3073 3079 {ECO:0000244|PDB:4HDH}.
HELIX 3080 3085 {ECO:0000244|PDB:4HDH}.
HELIX 3088 3100 {ECO:0000244|PDB:4HDH}.
TURN 3101 3103 {ECO:0000244|PDB:4HDH}.
STRAND 3104 3113 {ECO:0000244|PDB:4HDH}.
TURN 3114 3116 {ECO:0000244|PDB:4HDH}.
STRAND 3117 3126 {ECO:0000244|PDB:4HDH}.
HELIX 3136 3155 {ECO:0000244|PDB:4HDH}.
HELIX 3161 3163 {ECO:0000244|PDB:4HDH}.
HELIX 3169 3187 {ECO:0000244|PDB:4HDH}.
STRAND 3190 3193 {ECO:0000244|PDB:4HDH}.
STRAND 3196 3199 {ECO:0000244|PDB:4HDH}.
HELIX 3204 3208 {ECO:0000244|PDB:4HDH}.
HELIX 3211 3215 {ECO:0000244|PDB:4HDH}.
STRAND 3220 3223 {ECO:0000244|PDB:4K6M}.
STRAND 3232 3234 {ECO:0000244|PDB:4K6M}.
HELIX 3235 3237 {ECO:0000244|PDB:4HDH}.
STRAND 3243 3249 {ECO:0000244|PDB:4HDH}.
STRAND 3255 3260 {ECO:0000244|PDB:4HDH}.
HELIX 3263 3270 {ECO:0000244|PDB:4HDH}.
STRAND 3272 3275 {ECO:0000244|PDB:4K6M}.
HELIX 3280 3297 {ECO:0000244|PDB:4HDH}.
HELIX 3302 3314 {ECO:0000244|PDB:4HDH}.
STRAND 3336 3339 {ECO:0000244|PDB:4HDH}.
HELIX 3341 3349 {ECO:0000244|PDB:4HDH}.
TURN 3350 3352 {ECO:0000244|PDB:4K6M}.
HELIX 3365 3367 {ECO:0000244|PDB:4HDH}.
HELIX 3373 3378 {ECO:0000244|PDB:4HDH}.
HELIX 3386 3406 {ECO:0000244|PDB:4HDH}.
HELIX 3415 3417 {ECO:0000244|PDB:4K6M}.
HELIX 3419 3421 {ECO:0000244|PDB:4K6M}.
SEQUENCE 3432 AA; 380211 MW; 11B9423735B1B5FE CRC64;
MTKKPGGPGK NRAINMLKRG LPRVFPLVGV KRVVMSLLDG RGPVRFVLAL ITFFKFTALA
PTKALLGRWK AVEKSVAMKH LTSFKRELGT LIDAVNKRGR KQNKRGGNEG SIMWLASLAV
VIACAGAMKL SNFQGKLLMT INNTDIADVI VIPTSKGENR CWVRAIDVGY MCEDTITYEC
PKLTMGNDPE DVDCWCDNQE VYVQYGRCTR TRHSKRSRRS VSVQTHGESS LVNKKEAWLD
STKATRYLMK TENWIIRNPG YAFLAAVLGW MLGSNNGQRV VFTILLLLVA PAYSFNCLGM
GNRDFIEGAS GATWVDLVLE GDSCLTIMAN DKPTLDVRMI NIEASQLAEV RSYCYHASVT
DISTVARCPT TGEAHNEKRA DSSYVCKQGF TDRGWGNGCG LFGKGSIDTC AKFSCTSKAI
GRTIQPENIK YEVGIFVHGT TTSENHGNYS AQVGASQAAK FTVTPNAPSI TLKLGDYGEV
TLDCEPRSGL NTEAFYVMTV GSKSFLVHRE WFHDLALPWT SPSSTAWRNR ELLMEFEGAH
ATKQSVVALG SQEGGLHQAL AGAIVVEYSS SVKLTSGHLK CRLKMDKLAL KGTTYGMCTE
KFSFAKNPVD TGHGTVVIEL SYSGSDGPCK IPIVSVASLN DMTPVGRLVT VNPFVATSSA
NSKVLVEMEP PFGDSYIVVG RGDKQINHHW HKAGSTLGKA FSTTLKGAQR LAALGDTAWD
FGSIGGVFNS IGRAVHQVFG GAFRTLFGGM SWITQGLMGA LLLWMGVNAR DRSIALAFLA
TGGVLVFLAT NVHADTGCAI DITRKEMRCG SGIFVHNDVE AWVDRYKYLP ETPRSLAKIV
HKAHKEGVCG VRSVTRLEHQ MWEAVRDELN VLLKENAVDL SVVVNKPVGR YRSAPKRLSM
TQEKFEMGWK AWGKSILFAP ELANSTFVVD GPETKECPDE HRAWNSMQIE DFGFGITSTR
VWLKIREEST DECDGAIIGT AVKGHVAVHS DLSYWIESRY NDTWKLERAV FGEVKSCTWP
ETHTLWGDDV EESELIIPHT IAGPKSKHNR REGYKTQNQG PWDENGIVLD FDYCPGTKVT
ITEDCSKRGP SVRTTTDSGK LITDWCCRSC SLPPLRFRTE NGCWYGMEIR PVMHDETTLV
RSQVDAFKGE MVDPFQLGLL VMFLATQEVL RKRWTARLTI PAVLGVLLVL MLGGITYTDL
ARYVVLVAAA FAEANSGGDV LHLALIAVFK IQPAFLVMNM LSTRWTNQEN VILVLGAAFF
QLASVDLQIG VHGILNAAAI AWMIVRAITF PTTSSVTMPV LALLTPGMRA LYLDTYRIIL
LVIGICSLLH ERKKTMAKKK GAVLLGLALT STGWFSPTTI AAGLMVCNPN KKRGWPATEF
LSAVGLMFAI VGGLAELDIE SMSIPFMLAG LMAVSYVVSG KATDMWLERA ADISWEMDAA
ITGSSRRLDV KLDDDGDFHL IDDPGVPWKV WVLRMSCIGL AALTPWAIVP AAFGYWLTLK
TTKRGGVFWD TPSPKPCSKG DTTTGVYRIM ARGILGTYQA GVGVMYENVF HTLWHTTRGA
AIMSGEGKLT PYWGSVREDR IAYGGPWRFD RKWNGTDDVQ VIVVEPGKAA VNIQTKPGVF
RTPFGEVGAV SLDYPRGTSG SPILDSNGDI IGLYGNGVEL GDGSYVSAIV QGDRQEEPVP
EAYTPNMLRK RQMTVLDLHP GSGKTRKILP QIIKDAIQQR LRTAVLAPTR VVAAEMAEAL
RGLPVRYQTS AVQREHQGNE IVDVMCHATL THRLMSPNRV PNYNLFVMDE AHFTDPASIA
ARGYIATKVE LGEAAAIFMT ATPPGTTDPF PDSNAPIHDL QDEIPDRAWS SGYEWITEYA
GKTVWFVASV KMGNEIAMCL QRAGKKVIQL NRKSYDTEYP KCKNGDWDFV ITTDISEMGA
NFGASRVIDC RKSVKPTILE EGEGRVILGN PSPITSASAA QRRGRVGRNP NQVGDEYHYG
GATSEDDSNL AHWTEAKIML DNIHMPNGLV AQLYGPEREK AFTMDGEYRL RGEEKKNFLE
LLRTADLPVW LAYKVASNGI QYTDRKWCFD GPRTNAILED NTEVEIVTRM GERKILKPRW
LDARVYADHQ ALKWFKDFAA GKRSAVSFIE VLGRMPEHFM GKTREALDTM YLVATAEKGG
KAHRMALEEL PDALETITLI VAITVMTGGF FLLMMQRKGI GKMGLGALVL TLATFFLWAA
EVPGTKIAGT LLIALLLMVV LIPEPEKQRS QTDNQLAVFL ICVLTVVGVV AANEYGMLEK
TKADLKSMFG GKTQASGLTG LPSMALDLRP ATAWALYGGS TVVLTPLLKH LITSEYVTTS
LASINSQAGS LFVLPRGVPF TDLDLTVGLV FLGCWGQITL TTFLTAMVLA TLHYGYMLPG
WQAEALRAAQ RRTAAGIMKN AVVDGMVATD VPELERTTPL MQKKVGQVLL IGVSVAAFLV
NPNVTTVREA GVLVTAATLT LWDNGASAVW NSTTATGLCH VMRGSYLAGG SIAWTLIKNA
DKPSLKRGRP GGRTLGEQWK EKLNAMSREE FFKYRREAII EVDRTEARRA RRENNIVGGH
PVSRGSAKLR WLVEKGFVSP IGKVIDLGCG RGGWSYYAAT LKKVQEVRGY TKGGAGHEEP
MLMQSYGWNL VSLKSGVDVF YKPSEPSDTL FCDIGESSPS PEVEEQRTLR VLEMTSDWLH
RGPREFCIKV LCPYMPKVIE KMEVLQRRFG GGLVRLPLSR NSNHEMYWVS GAAGNVVHAV
NMTSQVLLGR MDRTVWRGPK YEEDVNLGSG TRAVGKGEVH SNQEKIKKRI QKLKEEFATT
WHKDPEHPYR TWTYHGSYEV KATGSASSLV NGVVELMSKP WDAIANVTTM AMTDTTPFGQ
QRVFKEKVDT KAPEPPAGAK EVLNETTNWL WAHLSREKRP RLCTKEEFIK KVNSNAALGA
VFAEQNQWST AREAVDDPRF WEMVDEEREN HLRGECHTCI YNMMGKREKK PGEFGKAKGS
RAIWFMWLGA RYLEFEALGF LNEDHWLSRE NSGGGVEGSG VQKLGYILRD IAGKQGGKMY
ADDTAGWDTR ITRTDLENEA KVLELLDGEH RMLARAIIEL TYRHKVVKVM RPAAEGKTVM
DVISREDQRG SGQVVTYALN TFTNIAVQLV RLMEAEGVIG PQHLEQLPRK TKIAVRTWLF
ENGEERVTRM AISGDDCVVK PLDDRFATAL HFLNAMSKVR KDIQEWKPSH GWHDWQQVPF
CSNHFQEIVM KDGRSIVVPC RGQDELIGRA RISPGAGWNV KDTACLAKAY AQMWLLLYFH
RRDLRLMANA ICSAVPVDWV PTGRTSWSIH SKGEWMTTED MLQVWNRVWI EENEWMMDKT
PITSWTDVPY VGKREDIWCG SLIGTRSRAT WAENIYAAIN QVRAVIGKEN YVDYMTSLRR
YEDVLIQEDR VI


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