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Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); 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); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (NS5)]

 POLG_ZIKV               Reviewed;        3419 AA.
Q32ZE1;
16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 1.
10-OCT-2018, entry version 118.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Capsid protein C {ECO:0000250|UniProtKB:P17763};
AltName: Full=Capsid protein;
AltName: Full=Core protein;
Contains:
RecName: Full=Protein prM {ECO:0000250|UniProtKB:P17763};
AltName: Full=Precursor membrane protein;
Contains:
RecName: Full=Peptide pr {ECO:0000250|UniProtKB:P17763};
AltName: Full=Peptide precursor;
Contains:
RecName: Full=Small envelope protein M {ECO:0000250|UniProtKB:P17763};
AltName: Full=Matrix protein;
Contains:
RecName: Full=Envelope protein E {ECO:0000250|UniProtKB:P17763};
Contains:
RecName: Full=Non-structural protein 1 {ECO:0000250|UniProtKB:P17763};
Short=NS1;
Contains:
RecName: Full=Non-structural protein 2A {ECO:0000250|UniProtKB:P17763};
Short=NS2A;
Contains:
RecName: Full=Serine protease subunit NS2B {ECO:0000250|UniProtKB:P17763};
AltName: Full=Flavivirin protease NS2B regulatory subunit;
AltName: Full=Non-structural protein 2B;
Contains:
RecName: Full=Serine protease NS3 {ECO:0000250|UniProtKB:P17763};
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 {ECO:0000250|UniProtKB:P17763};
Short=NS4A;
Contains:
RecName: Full=Peptide 2k {ECO:0000250|UniProtKB:P17763};
Contains:
RecName: Full=Non-structural protein 4B {ECO:0000250|UniProtKB:P17763};
Short=NS4B;
Contains:
RecName: Full=RNA-directed RNA polymerase NS5 {ECO:0000250|UniProtKB:P17763};
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:PRU00924};
AltName: Full=NS5;
Zika virus (strain Mr 766) (ZIKV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus.
NCBI_TaxID=64320;
NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16223950; DOI=10.1128/CMR.18.4.608-637.2005;
Kuno G., Chang G.J.;
"Biological transmission of arboviruses: reexamination of and new
insights into components, mechanisms, and unique traits as well as
their evolutionary trends.";
Clin. Microbiol. Rev. 18:608-637(2005).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=17195954; DOI=10.1007/s00705-006-0903-z;
Kuno G., Chang G.J.;
"Full-length sequencing and genomic characterization of Bagaza,
Kedougou, and Zika viruses.";
Arch. Virol. 152:687-696(2007).
[3]
INTERACTION WITH HOST TYRO3 (ENVELOPE PROTEIN E), INTERACTION WITH
HOST AXL (ENVELOPE PROTEIN E), AND INTERACTION WITH HOST DC SIGN
(ENVELOPE PROTEIN E).
PubMed=26085147; DOI=10.1128/JVI.00354-15;
Hamel R., Dejarnac O., Wichit S., Ekchariyawat P., Neyret A.,
Luplertlop N., Perera-Lecoin M., Surasombatpattana P., Talignani L.,
Thomas F., Cao-Lormeau V.M., Choumet V., Briant L., Despres P.,
Amara A., Yssel H., Misse D.;
"Biology of zika virus infection in human skin cells.";
J. Virol. 89:8880-8896(2015).
[4]
REVIEW (NON-STRUCTURAL PROTEIN 1).
PubMed=27473856; DOI=10.1186/s12985-016-0590-7;
Rastogi M., Sharma N., Singh S.K.;
"Flavivirus NS1: a multifaceted enigmatic viral protein.";
Virol. J. 13:131-131(2016).
[5]
DOMAIN (CAPSID PROTEIN C).
PubMed=27867910; DOI=10.3389/fcimb.2016.00144;
Giri R., Kumar D., Sharma N., Uversky V.N.;
"Intrinsically disordered side of the zika virus proteome.";
Front. Cell. Infect. Microbiol. 6:144-144(2016).
[6]
FUNCTION (NON-STRUCTURAL PROTEIN 4A), AND FUNCTION (NON-STRUCTURAL
PROTEIN 4B).
PubMed=27524440; DOI=10.1016/j.stem.2016.07.019;
Liang Q., Luo Z., Zeng J., Chen W., Foo S.S., Lee S.A., Ge J.,
Wang S., Goldman S.A., Zlokovic B.V., Zhao Z., Jung J.U.;
"Zika virus NS4A and NS4B proteins deregulate Akt-mTOR signaling in
human fetal neural stem cells to inhibit neurogenesis and induce
autophagy.";
Cell Stem Cell 19:663-671(2016).
[7]
FUNCTION (NON-STRUCTURAL PROTEIN 2A).
PubMed=28826723; DOI=10.1016/j.stem.2017.07.014;
Yoon K.J., Song G., Qian X., Pan J., Xu D., Rho H.S., Kim N.S.,
Habela C., Zheng L., Jacob F., Zhang F., Lee E.M., Huang W.K.,
Ringeling F.R., Vissers C., Li C., Yuan L., Kang K., Kim S., Yeo J.,
Cheng Y., Liu S., Wen Z., Qin C.F., Wu Q., Christian K.M., Tang H.,
Jin P., Xu Z., Qian J., Zhu H., Song H., Ming G.L.;
"Zika-Virus-encoded NS2A disrupts mammalian cortical neurogenesis by
degrading adherens junction proteins.";
Cell Stem Cell 21:349-358(2017).
[8]
CAUTION (ENVELOPE PROTEIN E).
PubMed=28880955; DOI=10.1371/journal.ppat.1006528;
Theys K., Libin P., Dallmeier K., Pineda-Pena A.C., Vandamme A.M.,
Cuypers L., Abecasis A.B.;
"Zika genomics urgently need standardized and curated reference
sequences.";
PLoS Pathog. 13:E1006528-E1006528(2017).
[9]
DOMAIN (SERINE PROTEASE SUBUNIT NS2B).
PubMed=29080786; DOI=10.1016/j.jmb.2017.10.018;
Mishra P.M., Uversky V.N., Giri R.;
"Molecular recognition features in zika virus proteome.";
J. Mol. Biol. 430:2372-2388(2018).
[10]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) (NON-STRUCTURAL PROTEIN 1), AND
SUBUNIT (NON-STRUCTURAL PROTEIN 1).
PubMed=27455458; DOI=10.1038/nsmb.3268;
Brown W.C., Akey D.L., Konwerski J.R., Tarrasch J.T., Skiniotis G.,
Kuhn R.J., Smith J.L.;
"Extended surface for membrane association in Zika virus NS1
structure.";
Nat. Struct. Mol. Biol. 23:865-867(2016).
[11]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) (SERINE PROTEASE SUBUNIT NS2B
AND SERINE PROTEASE NS3).
STRAIN=Isolate BeH823339;
PubMed=27386922; DOI=10.1126/science.aag2419;
Lei J., Hansen G., Nitsche C., Klein C.D., Zhang L., Hilgenfeld R.;
"Crystal structure of Zika virus NS2B-NS3 protease in complex with a
boronate inhibitor.";
Science 353:503-505(2016).
[12]
X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) (SERINE PROTEASE NS3).
PubMed=27399257; DOI=10.1038/nsmb.3258;
Jain R., Coloma J., Garcia-Sastre A., Aggarwal A.K.;
"Structure of the NS3 helicase from Zika virus.";
Nat. Struct. Mol. Biol. 23:752-754(2016).
[13]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2822-3419 IN COMPLEX WITH
ZINC.
PubMed=28345596; DOI=10.1038/ncomms14764;
Godoy A.S., Lima G.M., Oliveira K.I., Torres N.U., Maluf F.V.,
Guido R.V., Oliva G.;
"Crystal structure of Zika virus NS5 RNA-dependent RNA polymerase.";
Nat. Commun. 8:14764-14764(2017).
-!- FUNCTION: Capsid protein C: Plays a role in virus budding by
binding to the cell membrane and gathering the viral RNA into a
nucleocapsid that forms the core of a mature virus particle.
During virus entry, may induce genome penetration into the host
cytoplasm after hemifusion induced by the surface proteins. Can
migrate to the cell nucleus where it modulates host functions.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Capsid protein C: Inhibits RNA silencing by interfering
with host Dicer. {ECO:0000250|UniProtKB:P03314}.
-!- FUNCTION: Peptide pr: Prevents premature fusion activity of
envelope proteins in trans-Golgi by binding to envelope protein E
at pH6.0. After virion release in extracellular space, gets
dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Protein prM: Plays a role in host immune defense
modulation and protection of envelope protein E during virion
synthesis. PrM-E cleavege is inneficient, and un-matured prM-E
proteins would have an activity against host immune response. The
sequence of PrM contributes to fetal microcephaly in Humans. 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:A0A024B7W1,
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 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
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 (By
similarity). Disrupts adherens junction formation and thereby
impairs proliferation of radial cells in both embryonic mouse
cortex and human forebrain organoids (PubMed:28826723).
{ECO:0000250|UniProtKB:P14335, ECO:0000269|PubMed:28826723}.
-!- FUNCTION: Non-structural protein 2B: Required cofactor for the
serine protease function of NS3. {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.
Leads to translation arrest when expressed ex vivo (By
similarity). {ECO:0000250|UniProtKB:A0A024B7W1,
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. Cooperatively with NS4B suppress the Akt-
mTOR pathway and lead to cellular dysregulation (PubMed:27524440).
Leads to translation arrest when expressed ex vivo (By
similarity). {ECO:0000250|UniProtKB:A0A024B7W1,
ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27524440}.
-!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and
is required for the interferon antagonism activity of the latter.
{ECO:0000250}.
-!- 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. Cooperatively with NS4A suppress the Akt-mTOR pathway
and lead to cellular dysregulation (PubMed:27524440).
{ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27524440}.
-!- 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: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. Protein prM: Forms
heterodimers with envelope protein E in the endoplasmic reticulum
and Golgi (By similarity). Envelope protein E: Homodimer; in the
endoplasmic reticulum and Golgi (By similarity). Interacts with
host Tyro3, AXL and DC-SIGN proteins (PubMed:26085147). Non-
structural protein 1: Homodimer; Homohexamer when secreted
(PubMed:27455458). Interacts with envelope protein E (By
similarity). Non-structural protein 2B: Forms a heterodimer with
serine protease NS3. May form homooligomers (By similarity). Non-
structural protein 2B: Forms a heterodimer with serine protease
NS3. May form homooligomers (By similarity). 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 (By similarity). Non-structural protein 4B: Interacts
with serine protease NS3. Interacts with NS1 (By similarity). RNA-
directed RNA polymerase NS5: Homodimer (By similarity). Interacts
with host STAT2; this interaction inhibits the phosphorylation of
the latter, and, when all viral proteins are present
(polyprotein), targets STAT2 for degradation (By similarity).
{ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:26085147,
ECO:0000269|PubMed:27455458}.
-!- 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:P17763}; Multi-pass membrane protein
{ECO:0000255}. Host endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000255}. Host endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000255}.
-!- 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:P17763}; 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:P17763}; 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:P17763}.
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: Small envelope protein M: The transmembrane domain
contains an endoplasmic reticulum retention signal.
{ECO:0000250|UniProtKB:P17763}.
-!- DOMAIN: Envelope protein E: The transmembrane domain contains an
endoplasmic reticulum retention signal.
{ECO:0000250|UniProtKB:P17763}.
-!- DOMAIN: Capsid protein C: The disordered region at the N-terminus
may be involved in lipid-droplet binding.
{ECO:0000250|UniProtKB:P12823, ECO:0000269|PubMed:27867910}.
-!- DOMAIN: Serine protease subunit NS2B: The central disordered
region transitions to ordered by binding to NS3.
{ECO:0000269|PubMed:29080786}.
-!- 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: 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}.
-!- CAUTION: Envelope protein E: The strain Mr 766 lacks four amino-
acids compared to circulating strains, removing the glycosylation
site. This may be due to many cell culture passages sinse its
isolation. {ECO:0000305|PubMed:28880955}.
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EMBL; AY632535; AAV34151.1; -; Genomic_RNA.
RefSeq; YP_002790881.1; NC_012532.1.
PDB; 5GJ4; X-ray; 1.84 A; A/C/E/G=1414-1464, B/D/F/H=1499-1675.
PDB; 5GPI; X-ray; 1.58 A; A/C/E/G=1414-1464, B/D/F/H=1499-1675.
PDB; 5GXJ; X-ray; 2.60 A; A/B=1416-1668.
PDB; 5JPS; X-ray; 1.78 A; A=1674-2115.
PDB; 5JRZ; X-ray; 1.62 A; A=1669-2115.
PDB; 5K6K; X-ray; 1.89 A; A/B=790-1142.
PDB; 5T1V; X-ray; 3.10 A; A/B=1414-1467, A/B=1499-1685.
PDB; 5TFN; X-ray; 3.00 A; A/B=1416-1456, A/B=1499-1553.
PDB; 5TFO; X-ray; 2.51 A; A/B=1416-1443, A/B=1455-1462, A/B=1499-1680.
PDB; 5TFR; X-ray; 3.05 A; A/B=2517-3419.
PDB; 5TMH; X-ray; 3.28 A; A/B=2517-3418.
PDB; 5U04; X-ray; 1.90 A; A=2822-3419.
PDB; 5U0B; X-ray; 3.00 A; A/B=2517-3419.
PDB; 5U0C; X-ray; 3.00 A; A/B/C/D/E/F/G/H=2781-3419.
PDB; 5VI7; X-ray; 2.00 A; A=1677-2115.
PDB; 5VIM; X-ray; 2.10 A; A/B=2521-2781.
PDB; 5W41; X-ray; 2.20 A; B=2887-2923.
PDB; 5Y4Z; X-ray; 1.30 A; A=1676-2115.
PDB; 5YOD; X-ray; 1.90 A; A/C/E/G=1412-1464, B/D/F/H=1499-1675.
PDB; 5YOF; X-ray; 1.51 A; A=1412-1464, B=1499-1675.
PDBsum; 5GJ4; -.
PDBsum; 5GPI; -.
PDBsum; 5GXJ; -.
PDBsum; 5JPS; -.
PDBsum; 5JRZ; -.
PDBsum; 5K6K; -.
PDBsum; 5T1V; -.
PDBsum; 5TFN; -.
PDBsum; 5TFO; -.
PDBsum; 5TFR; -.
PDBsum; 5TMH; -.
PDBsum; 5U04; -.
PDBsum; 5U0B; -.
PDBsum; 5U0C; -.
PDBsum; 5VI7; -.
PDBsum; 5VIM; -.
PDBsum; 5W41; -.
PDBsum; 5Y4Z; -.
PDBsum; 5YOD; -.
PDBsum; 5YOF; -.
ProteinModelPortal; Q32ZE1; -.
SMR; Q32ZE1; -.
MEROPS; S07.003; -.
GeneID; 7751225; -.
KEGG; vg:7751225; -.
OrthoDB; VOG090001DL; -.
Proteomes; UP000054557; 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: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.
CDD; cd00079; HELICc; 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; -; 3.
Gene3D; 3.30.387.10; -; 2.
Gene3D; 3.30.67.10; -; 4.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR000069; Env_glycoprot_M_flavivir.
InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
InterPro; IPR001122; Flavi_capsidC.
InterPro; 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; 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; Nucleotide-binding;
Nucleotidyltransferase; Phosphoprotein; Protease; Reference proteome;
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 3419 Genome polyprotein.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000435828.
CHAIN 1 104 Capsid protein C.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000435829.
PROPEP 105 122 ER anchor for capsid protein C, removed
in mature form by serine protease NS3.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000435830.
CHAIN 123 290 Protein prM.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000435831.
CHAIN 123 215 Peptide pr.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000435832.
CHAIN 216 290 Small envelope protein M.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000435833.
CHAIN 291 790 Envelope protein E.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000435834.
CHAIN 791 1142 Non-structural protein 1.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000435835.
CHAIN 1143 1368 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000435836.
CHAIN 1369 1498 Serine protease subunit NS2B.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000435837.
CHAIN 1499 2115 Serine protease NS3.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000435838.
CHAIN 2116 2242 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000435839.
PEPTIDE 2243 2265 Peptide 2k.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000435840.
CHAIN 2266 2516 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000435841.
CHAIN 2517 3419 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000435842.
TRANSMEM 105 125 Helical. {ECO:0000255}.
TRANSMEM 250 269 Helical. {ECO:0000255}.
TRANSMEM 275 290 Helical. {ECO:0000305}.
TRANSMEM 742 763 Helical. {ECO:0000255}.
TRANSMEM 770 790 Helical. {ECO:0000255}.
TRANSMEM 1174 1194 Helical. {ECO:0000255}.
TRANSMEM 1217 1237 Helical. {ECO:0000255}.
TRANSMEM 1267 1287 Helical. {ECO:0000255}.
TRANSMEM 1292 1312 Helical. {ECO:0000255}.
TRANSMEM 1342 1362 Helical. {ECO:0000255}.
TRANSMEM 1370 1390 Helical. {ECO:0000255}.
TRANSMEM 1394 1414 Helical. {ECO:0000255}.
INTRAMEM 1469 1489 Helical. {ECO:0000255}.
TRANSMEM 2167 2187 Helical. {ECO:0000255}.
INTRAMEM 2192 2212 Helical. {ECO:0000255}.
TRANSMEM 2215 2235 Helical. {ECO:0000255}.
TRANSMEM 2251 2265 Helical; Note=Signal for NS4B.
{ECO:0000305}.
INTRAMEM 2304 2324 Helical. {ECO:0000255}.
TRANSMEM 2341 2361 Helical. {ECO:0000255}.
TRANSMEM 2372 2392 Helical. {ECO:0000255}.
TRANSMEM 2438 2458 Helical. {ECO:0000255}.
DOMAIN 1499 1676 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1679 1835 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1830 2009 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2517 2781 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3045 3195 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1692 1699 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 1 25 Disordered.
{ECO:0000269|PubMed:27867910}.
REGION 37 72 Hydrophobic; homodimerization of capsid
protein C.
{ECO:0000250|UniProtKB:P29990}.
REGION 388 401 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
REGION 1421 1460 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
REGION 1425 1447 Disordered.
{ECO:0000269|PubMed:29080786}.
REGION 1683 1686 Important for RNA-binding.
{ECO:0000250|UniProtKB:P14340}.
MOTIF 1783 1786 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
ACT_SITE 1549 1549 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1573 1573 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1633 1633 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 2577 2577 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2662 2662 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2698 2698 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2734 2734 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2955 2955 Zinc 1. {ECO:0000269|PubMed:28345596}.
METAL 2959 2959 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:28345596}.
METAL 2964 2964 Zinc 1. {ECO:0000269|PubMed:28345596}.
METAL 2967 2967 Zinc 1. {ECO:0000269|PubMed:28345596}.
METAL 3230 3230 Zinc 2; via tele nitrogen.
{ECO:0000269|PubMed:28345596}.
METAL 3246 3246 Zinc 2. {ECO:0000269|PubMed:28345596}.
METAL 3365 3365 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
BINDING 2529 2529 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2532 2532 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2533 2533 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2535 2535 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2544 2544 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2572 2572 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2602 2602 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2603 2603 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2620 2620 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2621 2621 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2647 2647 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2648 2648 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2666 2666 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2729 2729 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2731 2731 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2736 2736 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 104 105 Cleavage; by viral protease NS3.
{ECO:0000303|PubMed:17195954}.
SITE 122 123 Cleavage; by host signal peptidase.
{ECO:0000303|PubMed:17195954}.
SITE 215 216 Cleavage; by host furin.
{ECO:0000303|PubMed:17195954}.
SITE 290 291 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P09732}.
SITE 790 791 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P09732}.
SITE 1142 1143 Cleavage; by host.
{ECO:0000250|UniProtKB:P09732}.
SITE 1368 1369 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P09732}.
SITE 1498 1499 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P09732}.
SITE 1954 1954 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 1957 1957 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 2115 2116 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P09732}.
SITE 2242 2243 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P09732}.
SITE 2265 2266 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P09732}.
SITE 2516 2517 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P09732}.
SITE 2540 2540 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2577 2577 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2662 2662 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2663 2663 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2698 2698 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2734 2734 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
MOD_RES 2572 2572 Phosphoserine.
{ECO:0000250|UniProtKB:P03314}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 920 920 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:Q9Q6P4}.
CARBOHYD 997 997 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 293 320 {ECO:0000250|UniProtKB:P17763}.
DISULFID 350 411 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 350 406 {ECO:0000250|UniProtKB:P17763}.
DISULFID 364 395 {ECO:0000250|UniProtKB:P17763}.
DISULFID 382 411 {ECO:0000250|UniProtKB:P17763}.
DISULFID 382 406 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 476 577 {ECO:0000250|UniProtKB:P17763}.
DISULFID 594 625 {ECO:0000250|UniProtKB:P17763}.
DISULFID 794 805 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 845 933 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 969 1013 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 1070 1119 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 1081 1102 {ECO:0000250|UniProtKB:Q9Q6P4}.
DISULFID 1103 1106 {ECO:0000250|UniProtKB:Q9Q6P4}.
STRAND 791 797 {ECO:0000244|PDB:5K6K}.
TURN 798 801 {ECO:0000244|PDB:5K6K}.
STRAND 802 812 {ECO:0000244|PDB:5K6K}.
STRAND 815 819 {ECO:0000244|PDB:5K6K}.
STRAND 822 827 {ECO:0000244|PDB:5K6K}.
HELIX 829 841 {ECO:0000244|PDB:5K6K}.
HELIX 852 871 {ECO:0000244|PDB:5K6K}.
STRAND 877 880 {ECO:0000244|PDB:5K6K}.
STRAND 885 887 {ECO:0000244|PDB:5K6K}.
STRAND 922 928 {ECO:0000244|PDB:5K6K}.
TURN 930 932 {ECO:0000244|PDB:5K6K}.
HELIX 935 937 {ECO:0000244|PDB:5K6K}.
STRAND 943 949 {ECO:0000244|PDB:5K6K}.
STRAND 952 961 {ECO:0000244|PDB:5K6K}.
HELIX 971 973 {ECO:0000244|PDB:5K6K}.
STRAND 975 979 {ECO:0000244|PDB:5K6K}.
STRAND 982 986 {ECO:0000244|PDB:5K6K}.
STRAND 988 1008 {ECO:0000244|PDB:5K6K}.
HELIX 1017 1019 {ECO:0000244|PDB:5K6K}.
HELIX 1028 1030 {ECO:0000244|PDB:5K6K}.
HELIX 1035 1037 {ECO:0000244|PDB:5K6K}.
HELIX 1043 1045 {ECO:0000244|PDB:5K6K}.
STRAND 1060 1068 {ECO:0000244|PDB:5K6K}.
STRAND 1074 1077 {ECO:0000244|PDB:5K6K}.
STRAND 1088 1091 {ECO:0000244|PDB:5K6K}.
STRAND 1100 1105 {ECO:0000244|PDB:5K6K}.
STRAND 1111 1115 {ECO:0000244|PDB:5K6K}.
STRAND 1118 1121 {ECO:0000244|PDB:5K6K}.
STRAND 1126 1130 {ECO:0000244|PDB:5K6K}.
HELIX 1132 1134 {ECO:0000244|PDB:5K6K}.
STRAND 1420 1425 {ECO:0000244|PDB:5GPI}.
STRAND 1431 1434 {ECO:0000244|PDB:5GXJ}.
STRAND 1441 1446 {ECO:0000244|PDB:5GPI}.
STRAND 1452 1454 {ECO:0000244|PDB:5GPI}.
STRAND 1519 1524 {ECO:0000244|PDB:5GPI}.
STRAND 1528 1530 {ECO:0000244|PDB:5GPI}.
STRAND 1533 1540 {ECO:0000244|PDB:5GPI}.
STRAND 1543 1547 {ECO:0000244|PDB:5GPI}.
HELIX 1548 1551 {ECO:0000244|PDB:5GPI}.
STRAND 1556 1558 {ECO:0000244|PDB:5GPI}.
STRAND 1561 1563 {ECO:0000244|PDB:5GPI}.
STRAND 1565 1569 {ECO:0000244|PDB:5GPI}.
TURN 1570 1573 {ECO:0000244|PDB:5GPI}.
STRAND 1574 1580 {ECO:0000244|PDB:5GPI}.
STRAND 1589 1591 {ECO:0000244|PDB:5GPI}.
STRAND 1593 1597 {ECO:0000244|PDB:5GPI}.
STRAND 1605 1609 {ECO:0000244|PDB:5GPI}.
STRAND 1612 1616 {ECO:0000244|PDB:5GPI}.
STRAND 1619 1624 {ECO:0000244|PDB:5GPI}.
HELIX 1630 1632 {ECO:0000244|PDB:5GPI}.
STRAND 1635 1638 {ECO:0000244|PDB:5GPI}.
STRAND 1640 1642 {ECO:0000244|PDB:5GXJ}.
STRAND 1644 1648 {ECO:0000244|PDB:5GPI}.
STRAND 1651 1653 {ECO:0000244|PDB:5GPI}.
STRAND 1659 1662 {ECO:0000244|PDB:5GPI}.
HELIX 1679 1682 {ECO:0000244|PDB:5Y4Z}.
STRAND 1687 1690 {ECO:0000244|PDB:5Y4Z}.
TURN 1698 1701 {ECO:0000244|PDB:5Y4Z}.
HELIX 1702 1712 {ECO:0000244|PDB:5Y4Z}.
STRAND 1717 1723 {ECO:0000244|PDB:5Y4Z}.
HELIX 1724 1733 {ECO:0000244|PDB:5Y4Z}.
TURN 1734 1736 {ECO:0000244|PDB:5Y4Z}.
STRAND 1739 1741 {ECO:0000244|PDB:5Y4Z}.
STRAND 1756 1760 {ECO:0000244|PDB:5Y4Z}.
HELIX 1761 1769 {ECO:0000244|PDB:5Y4Z}.
STRAND 1770 1772 {ECO:0000244|PDB:5JRZ}.
STRAND 1778 1784 {ECO:0000244|PDB:5Y4Z}.
HELIX 1790 1804 {ECO:0000244|PDB:5Y4Z}.
STRAND 1809 1813 {ECO:0000244|PDB:5Y4Z}.
STRAND 1831 1835 {ECO:0000244|PDB:5Y4Z}.
STRAND 1844 1846 {ECO:0000244|PDB:5Y4Z}.
HELIX 1848 1851 {ECO:0000244|PDB:5Y4Z}.
STRAND 1857 1860 {ECO:0000244|PDB:5Y4Z}.
HELIX 1864 1876 {ECO:0000244|PDB:5Y4Z}.
STRAND 1881 1884 {ECO:0000244|PDB:5Y4Z}.
TURN 1886 1888 {ECO:0000244|PDB:5Y4Z}.
HELIX 1889 1898 {ECO:0000244|PDB:5Y4Z}.
STRAND 1902 1906 {ECO:0000244|PDB:5Y4Z}.
HELIX 1908 1911 {ECO:0000244|PDB:5Y4Z}.
STRAND 1919 1923 {ECO:0000244|PDB:5Y4Z}.
STRAND 1926 1933 {ECO:0000244|PDB:5Y4Z}.
TURN 1934 1936 {ECO:0000244|PDB:5Y4Z}.
STRAND 1937 1945 {ECO:0000244|PDB:5Y4Z}.
HELIX 1948 1955 {ECO:0000244|PDB:5Y4Z}.
STRAND 1967 1971 {ECO:0000244|PDB:5Y4Z}.
TURN 1978 1981 {ECO:0000244|PDB:5Y4Z}.
HELIX 1983 1992 {ECO:0000244|PDB:5Y4Z}.
HELIX 2007 2012 {ECO:0000244|PDB:5Y4Z}.
TURN 2017 2020 {ECO:0000244|PDB:5Y4Z}.
HELIX 2024 2035 {ECO:0000244|PDB:5Y4Z}.
HELIX 2041 2049 {ECO:0000244|PDB:5Y4Z}.
HELIX 2058 2060 {ECO:0000244|PDB:5Y4Z}.
HELIX 2065 2067 {ECO:0000244|PDB:5Y4Z}.
STRAND 2077 2079 {ECO:0000244|PDB:5Y4Z}.
STRAND 2085 2087 {ECO:0000244|PDB:5Y4Z}.
STRAND 2091 2094 {ECO:0000244|PDB:5Y4Z}.
HELIX 2095 2097 {ECO:0000244|PDB:5Y4Z}.
STRAND 2098 2100 {ECO:0000244|PDB:5Y4Z}.
HELIX 2101 2111 {ECO:0000244|PDB:5Y4Z}.
HELIX 2524 2534 {ECO:0000244|PDB:5VIM}.
HELIX 2537 2543 {ECO:0000244|PDB:5VIM}.
TURN 2544 2547 {ECO:0000244|PDB:5VIM}.
STRAND 2549 2552 {ECO:0000244|PDB:5VIM}.
HELIX 2554 2561 {ECO:0000244|PDB:5VIM}.
HELIX 2574 2583 {ECO:0000244|PDB:5VIM}.
STRAND 2591 2596 {ECO:0000244|PDB:5VIM}.
TURN 2599 2601 {ECO:0000244|PDB:5U0B}.
HELIX 2602 2607 {ECO:0000244|PDB:5VIM}.
STRAND 2613 2619 {ECO:0000244|PDB:5VIM}.
STRAND 2623 2626 {ECO:0000244|PDB:5TFR}.
HELIX 2637 2639 {ECO:0000244|PDB:5VIM}.
STRAND 2640 2643 {ECO:0000244|PDB:5VIM}.
HELIX 2648 2650 {ECO:0000244|PDB:5VIM}.
STRAND 2657 2661 {ECO:0000244|PDB:5VIM}.
HELIX 2670 2688 {ECO:0000244|PDB:5VIM}.
STRAND 2693 2700 {ECO:0000244|PDB:5VIM}.
HELIX 2705 2718 {ECO:0000244|PDB:5VIM}.
STRAND 2721 2723 {ECO:0000244|PDB:5VIM}.
STRAND 2726 2728 {ECO:0000244|PDB:5U0B}.
STRAND 2735 2738 {ECO:0000244|PDB:5VIM}.
HELIX 2745 2760 {ECO:0000244|PDB:5VIM}.
STRAND 2761 2763 {ECO:0000244|PDB:5U0B}.
STRAND 2768 2771 {ECO:0000244|PDB:5VIM}.
TURN 2791 2793 {ECO:0000244|PDB:5U0B}.
HELIX 2795 2804 {ECO:0000244|PDB:5U0B}.
TURN 2805 2808 {ECO:0000244|PDB:5U0B}.
STRAND 2818 2827 {ECO:0000244|PDB:5U0B}.
HELIX 2840 2844 {ECO:0000244|PDB:5U04}.
HELIX 2847 2851 {ECO:0000244|PDB:5U04}.
TURN 2853 2855 {ECO:0000244|PDB:5U04}.
STRAND 2858 2860 {ECO:0000244|PDB:5U0B}.
HELIX 2865 2875 {ECO:0000244|PDB:5U0B}.
HELIX 2885 2902 {ECO:0000244|PDB:5U04}.
TURN 2903 2905 {ECO:0000244|PDB:5U0B}.
HELIX 2913 2920 {ECO:0000244|PDB:5U04}.
TURN 2921 2923 {ECO:0000244|PDB:5U04}.
HELIX 2931 2933 {ECO:0000244|PDB:5U0B}.
HELIX 2935 2944 {ECO:0000244|PDB:5U04}.
HELIX 2946 2959 {ECO:0000244|PDB:5U04}.
TURN 2960 2962 {ECO:0000244|PDB:5U04}.
STRAND 2969 2973 {ECO:0000244|PDB:5U0B}.
STRAND 2977 2979 {ECO:0000244|PDB:5U0B}.
HELIX 2989 3006 {ECO:0000244|PDB:5U04}.
HELIX 3008 3011 {ECO:0000244|PDB:5U04}.
TURN 3012 3015 {ECO:0000244|PDB:5U04}.
HELIX 3017 3020 {ECO:0000244|PDB:5U04}.
STRAND 3021 3023 {ECO:0000244|PDB:5U04}.
HELIX 3029 3041 {ECO:0000244|PDB:5U04}.
STRAND 3042 3045 {ECO:0000244|PDB:5U04}.
HELIX 3055 3057 {ECO:0000244|PDB:5U0B}.
HELIX 3061 3067 {ECO:0000244|PDB:5U04}.
HELIX 3068 3073 {ECO:0000244|PDB:5U04}.
HELIX 3076 3091 {ECO:0000244|PDB:5U04}.
HELIX 3102 3104 {ECO:0000244|PDB:5U0C}.
STRAND 3106 3116 {ECO:0000244|PDB:5U0B}.
HELIX 3123 3143 {ECO:0000244|PDB:5U04}.
HELIX 3149 3152 {ECO:0000244|PDB:5U04}.
HELIX 3159 3173 {ECO:0000244|PDB:5U04}.
STRAND 3176 3179 {ECO:0000244|PDB:5U04}.
STRAND 3182 3185 {ECO:0000244|PDB:5U04}.
HELIX 3190 3194 {ECO:0000244|PDB:5U04}.
HELIX 3197 3201 {ECO:0000244|PDB:5U04}.
STRAND 3206 3209 {ECO:0000244|PDB:5U0B}.
STRAND 3218 3220 {ECO:0000244|PDB:5TMH}.
HELIX 3221 3223 {ECO:0000244|PDB:5U04}.
STRAND 3229 3235 {ECO:0000244|PDB:5U04}.
STRAND 3237 3239 {ECO:0000244|PDB:5U0B}.
STRAND 3241 3246 {ECO:0000244|PDB:5U04}.
HELIX 3249 3256 {ECO:0000244|PDB:5U04}.
STRAND 3258 3261 {ECO:0000244|PDB:5U0C}.
HELIX 3266 3283 {ECO:0000244|PDB:5U04}.
HELIX 3288 3300 {ECO:0000244|PDB:5U04}.
STRAND 3322 3325 {ECO:0000244|PDB:5U04}.
HELIX 3327 3335 {ECO:0000244|PDB:5U04}.
TURN 3336 3338 {ECO:0000244|PDB:5U04}.
HELIX 3351 3353 {ECO:0000244|PDB:5U04}.
HELIX 3359 3364 {ECO:0000244|PDB:5U04}.
STRAND 3369 3371 {ECO:0000244|PDB:5U0B}.
HELIX 3372 3379 {ECO:0000244|PDB:5U04}.
HELIX 3381 3392 {ECO:0000244|PDB:5U04}.
STRAND 3394 3396 {ECO:0000244|PDB:5TMH}.
SEQUENCE 3419 AA; 378736 MW; B20F0526BB24B098 CRC64;
MKNPKEEIRR IRIVNMLKRG VARVNPLGGL KRLPAGLLLG HGPIRMVLAI LAFLRFTAIK
PSLGLINRWG SVGKKEAMEI IKKFKKDLAA MLRIINARKE RKRRGADTSI GIIGLLLTTA
MAAEITRRGS AYYMYLDRSD AGKAISFATT LGVNKCHVQI MDLGHMCDAT MSYECPMLDE
GVEPDDVDCW CNTTSTWVVY GTCHHKKGEA RRSRRAVTLP SHSTRKLQTR SQTWLESREY
TKHLIKVENW IFRNPGFALV AVAIAWLLGS STSQKVIYLV MILLIAPAYS IRCIGVSNRD
FVEGMSGGTW VDVVLEHGGC VTVMAQDKPT VDIELVTTTV SNMAEVRSYC YEASISDMAS
DSRCPTQGEA YLDKQSDTQY VCKRTLVDRG WGNGCGLFGK GSLVTCAKFT CSKKMTGKSI
QPENLEYRIM LSVHGSQHSG MIGYETDEDR AKVEVTPNSP RAEATLGGFG SLGLDCEPRT
GLDFSDLYYL TMNNKHWLVH KEWFHDIPLP WHAGADTGTP HWNNKEALVE FKDAHAKRQT
VVVLGSQEGA VHTALAGALE AEMDGAKGRL FSGHLKCRLK MDKLRLKGVS YSLCTAAFTF
TKVPAETLHG TVTVEVQYAG TDGPCKIPVQ MAVDMQTLTP VGRLITANPV ITESTENSKM
MLELDPPFGD SYIVIGVGDK KITHHWHRSG STIGKAFEAT VRGAKRMAVL GDTAWDFGSV
GGVFNSLGKG IHQIFGAAFK SLFGGMSWFS QILIGTLLVW LGLNTKNGSI SLTCLALGGV
MIFLSTAVSA DVGCSVDFSK KETRCGTGVF IYNDVEAWRD RYKYHPDSPR RLAAAVKQAW
EEGICGISSV SRMENIMWKS VEGELNAILE ENGVQLTVVV GSVKNPMWRG PQRLPVPVNE
LPHGWKAWGK SYFVRAAKTN NSFVVDGDTL KECPLEHRAW NSFLVEDHGF GVFHTSVWLK
VREDYSLECD PAVIGTAVKG REAAHSDLGY WIESEKNDTW RLKRAHLIEM KTCEWPKSHT
LWTDGVEESD LIIPKSLAGP LSHHNTREGY RTQVKGPWHS EELEIRFEEC PGTKVYVEET
CGTRGPSLRS TTASGRVIEE WCCRECTMPP LSFRAKDGCW YGMEIRPRKE PESNLVRSMV
TAGSTDHMDH FSLGVLVILL MVQEGLKKRM TTKIIMSTSM AVLVVMILGG FSMSDLAKLV
ILMGATFAEM NTGGDVAHLA LVAAFKVRPA LLVSFIFRAN WTPRESMLLA LASCLLQTAI
SALEGDLMVL INGFALAWLA IRAMAVPRTD NIALPILAAL TPLARGTLLV AWRAGLATCG
GIMLLSLKGK GSVKKNLPFV MALGLTAVRV VDPINVVGLL LLTRSGKRSW PPSEVLTAVG
LICALAGGFA KADIEMAGPM AAVGLLIVSY VVSGKSVDMY IERAGDITWE KDAEVTGNSP
RLDVALDESG DFSLVEEDGP PMREIILKVV LMAICGMNPI AIPFAAGAWY VYVKTGKRSG
ALWDVPAPKE VKKGETTDGV YRVMTRRLLG STQVGVGVMQ EGVFHTMWHV TKGAALRSGE
GRLDPYWGDV KQDLVSYCGP WKLDAAWDGL SEVQLLAVPP GERARNIQTL PGIFKTKDGD
IGAVALDYPA GTSGSPILDK CGRVIGLYGN GVVIKNGSYV SAITQGKREE ETPVECFEPS
MLKKKQLTVL DLHPGAGKTR RVLPEIVREA IKKRLRTVIL APTRVVAAEM EEALRGLPVR
YMTTAVNVTH SGTEIVDLMC HATFTSRLLQ PIRVPNYNLN IMDEAHFTDP SSIAARGYIS
TRVEMGEAAA IFMTATPPGT RDAFPDSNSP IMDTEVEVPE RAWSSGFDWV TDHSGKTVWF
VPSVRNGNEI AACLTKAGKR VIQLSRKTFE TEFQKTKNQE WDFVITTDIS EMGANFKADR
VIDSRRCLKP VILDGERVIL AGPMPVTHAS AAQRRGRIGR NPNKPGDEYM YGGGCAETDE
GHAHWLEARM LLDNIYLQDG LIASLYRPEA DKVAAIEGEF KLRTEQRKTF VELMKRGDLP
VWLAYQVASA GITYTDRRWC FDGTTNNTIM EDSVPAEVWT KYGEKRVLKP RWMDARVCSD
HAALKSFKEF AAGKRGAALG VMEALGTLPG HMTERFQEAI DNLAVLMRAE TGSRPYKAAA
AQLPETLETI MLLGLLGTVS LGIFFVLMRN KGIGKMGFGM VTLGASAWLM WLSEIEPARI
ACVLIVVFLL LVVLIPEPEK QRSPQDNQMA IIIMVAVGLL GLITANELGW LERTKNDIAH
LMGRREEGAT MGFSMDIDLR PASAWAIYAA LTTLITPAVQ HAVTTSYNNY SLMAMATQAG
VLFGMGKGMP FMHGDLGVPL LMMGCYSQLT PLTLIVAIIL LVAHYMYLIP GLQAAAARAA
QKRTAAGIMK NPVVDGIVVT DIDTMTIDPQ VEKKMGQVLL IAVAISSAVL LRTAWGWGEA
GALITAATST LWEGSPNKYW NSSTATSLCN IFRGSYLAGA SLIYTVTRNA GLVKRRGGGT
GETLGEKWKA RLNQMSALEF YSYKKSGITE VCREEARRAL KDGVATGGHA VSRGSAKIRW
LEERGYLQPY GKVVDLGCGR GGWSYYAATI RKVQEVRGYT KGGPGHEEPM LVQSYGWNIV
RLKSGVDVFH MAAEPCDTLL CDIGESSSSP EVEETRTLRV LSMVGDWLEK RPGAFCIKVL
CPYTSTMMET MERLQRRHGG GLVRVPLCRN STHEMYWVSG AKSNIIKSVS TTSQLLLGRM
DGPRRPVKYE EDVNLGSGTR AVASCAEAPN MKIIGRRIER IRNEHAETWF LDENHPYRTW
AYHGSYEAPT QGSASSLVNG VVRLLSKPWD VVTGVTGIAM TDTTPYGQQR VFKEKVDTRV
PDPQEGTRQV MNIVSSWLWK ELGKRKRPRV CTKEEFINKV RSNAALGAIF EEEKEWKTAV
EAVNDPRFWA LVDREREHHL RGECHSCVYN MMGKREKKQG EFGKAKGSRA IWYMWLGARF
LEFEALGFLN EDHWMGRENS GGGVEGLGLQ RLGYILEEMN RAPGGKMYAD DTAGWDTRIS
KFDLENEALI TNQMEEGHRT LALAVIKYTY QNKVVKVLRP AEGGKTVMDI ISRQDQRGSG
QVVTYALNTF TNLVVQLIRN MEAEEVLEMQ DLWLLRKPEK VTRWLQSNGW DRLKRMAVSG
DDCVVKPIDD RFAHALRFLN DMGKVRKDTQ EWKPSTGWSN WEEVPFCSHH FNKLYLKDGR
SIVVPCRHQD ELIGRARVSP GAGWSIRETA CLAKSYAQMW QLLYFHRRDL RLMANAICSA
VPVDWVPTGR TTWSIHGKGE WMTTEDMLMV WNRVWIEEND HMEDKTPVTK WTDIPYLGKR
EDLWCGSLIG HRPRTTWAEN IKDTVNMVRR IIGDEEKYMD YLSTQVRYLG EEGSTPGVL


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