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 POLG_YEFV1              Reviewed;        3411 AA.
P03314; O42028; O91857; P19901; Q102J3; Q45RQ2; Q89275; Q89276;
Q9W878; Q9YWN0; Q9YWN1; Q9YWN2;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
30-AUG-2017, entry version 173.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Capsid protein C;
AltName: Full=Core protein;
Contains:
RecName: Full=prM;
Contains:
RecName: Full=Peptide pr;
Contains:
RecName: Full=Small envelope protein M;
AltName: Full=Matrix protein;
Contains:
RecName: Full=Envelope protein E;
Contains:
RecName: Full=Non-structural protein 1;
Short=NS1;
Contains:
RecName: Full=Non-structural protein 2A;
Short=NS2A;
Contains:
RecName: Full=Non-structural protein 2A-alpha {ECO:0000303|PubMed:3008425};
Short=NS2A-alpha;
Contains:
RecName: Full=Serine protease subunit NS2B;
AltName: Full=Flavivirin protease NS2B regulatory subunit;
AltName: Full=Non-structural protein 2B;
Contains:
RecName: Full=Serine protease NS3;
EC=3.4.21.91 {ECO:0000269|PubMed:21419753};
EC=3.6.1.15 {ECO:0000269|PubMed:16051820};
EC=3.6.4.13 {ECO:0000269|PubMed:16051820};
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;
Yellow fever virus (strain 17D vaccine) (YFV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; Yellow fever virus group.
NCBI_TaxID=11090;
NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
NCBI_TaxID=299629; Aedes luteocephalus (Mosquito).
NCBI_TaxID=7161; Aedes simpsoni.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=314293; Simiiformes.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=4023707; DOI=10.1126/science.4023707;
Rice C.M., Lenches E.M., Eddy S.R., Shin S.J., Sheets R.L.,
Strauss J.H.;
"Nucleotide sequence of yellow fever virus: implications for
flavivirus gene expression and evolution.";
Science 229:726-733(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate 17D-213 vaccine, and Isolate 17DD vaccine;
PubMed=7754673; DOI=10.1016/0168-1702(94)00076-O;
dos Santos C.N., Post P.R., Carvalho R., Ferreira I.I., Rice C.M.,
Galler R.;
"Complete nucleotide sequence of yellow fever virus vaccine strains
17DD and 17D-213.";
Virus Res. 35:35-41(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate 17D-204-USA HONG1 vaccine,
Isolate 17D-204-USA HONG2 vaccine, and
Isolate 17D-204-USA HONG3 vaccine;
PubMed=9712515; DOI=10.1016/S0168-1702(98)00036-7;
Xie H., Cass A.R., Barrett A.D.T.;
"Yellow fever 17D vaccine virus isolated from healthy vaccinees
accumulates very few mutations.";
Virus Res. 55:93-99(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Pasteur 17D-204 vaccine;
PubMed=2734112; DOI=10.1093/nar/17.10.3989;
Dupuy A., Despres P., Cahour A., Girard M., Bouloy M.;
"Nucleotide sequence comparison of the genome of two 17D-204 yellow
fever vaccines.";
Nucleic Acids Res. 17:3989-3989(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate 17D-204-South Africa vaccine,
Isolate 17D-204-South Africa vaccine large plaque variant, and
Isolate 17D-204-South Africa vaccine medium plaque variant;
PubMed=9714237;
Xie H., Ryman K.D., Campbell G.A., Barrett A.D.T.;
"Mutation in NS5 protein attenuates mouse neurovirulence of yellow
fever 17D vaccine virus.";
J. Gen. Virol. 79:1895-1899(1998).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Spain/AVD2791-93F/2004 vaccine;
PubMed=16597510; DOI=10.1016/j.jcv.2006.02.005;
Doblas A., Domingo C., Bae H.G., Bohorquez C.L., de Ory F.,
Niedrig M., Mora D., Carrasco F.J., Tenorio A.;
"Yellow fever vaccine-associated viscerotropic disease and death in
Spain.";
J. Clin. Virol. 36:156-158(2006).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Brazil/YF-VAVD/1975 vaccine;
PubMed=16464518; DOI=10.1016/j.vaccine.2006.01.009;
Engel A.R., Vasconcelos P.F., McArthur M.A., Barrett A.D.;
"Characterization of a viscerotropic yellow fever vaccine variant from
a patient in Brazil.";
Vaccine 24:2803-2809(2006).
[8]
PROTEIN SEQUENCE OF 779-798; 1485-1497 AND 2507-2510, AND PROTEOLYTIC
CLEAVAGE (GENOME POLYPROTEIN).
PubMed=3008425; DOI=10.1016/0042-6822(86)90098-X;
Rice C.M., Aebersold R., Teplow D.B., Pata J., Bell J.R.,
Vorndam A.V., Trent D.W., Brandriss M.W., Schlesinger J.J.,
Strauss J.H.;
"Partial N-terminal amino acid sequences of three nonstructural
proteins of two flaviviruses.";
Virology 151:1-9(1986).
[9]
PROTEIN SEQUENCE OF 2257-2276.
PubMed=2922923; DOI=10.1016/0042-6822(89)90045-7;
Chambers T.J., McCourt D.W., Rice C.M.;
"Yellow fever virus proteins NS2A, NS2B, and NS4B: identification and
partial N-terminal amino acid sequence analysis.";
Virology 169:100-109(1989).
[10]
PROTEIN SEQUENCE OF 102-121, AND PROTEOLYTIC CLEAVAGE (GENOME
POLYPROTEIN).
PubMed=8189517;
Amberg S.M., Nestorowicz A., McCourt D.W., Rice C.M.;
"NS2B-3 proteinase-mediated processing in the yellow fever virus
structural region: in vitro and in vivo studies.";
J. Virol. 68:3794-3802(1994).
[11]
CHARACTERIZATION (SERINE PROTEASE NS3), AND MUTAGENESIS OF HIS-1537;
ASP-1561 AND SER-1622.
PubMed=2147282; DOI=10.1073/pnas.87.22.8898;
Chambers T.J., Weir R.C., Grakoui A., McCourt D.W., Bazan J.F.,
Fletterick R.J., Rice C.M.;
"Evidence that the N-terminal domain of nonstructural protein NS3 from
yellow fever virus is a serine protease responsible for site-specific
cleavages in the viral polyprotein.";
Proc. Natl. Acad. Sci. U.S.A. 87:8898-8902(1990).
[12]
PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
PubMed=1833562;
Chambers T.J., Grakoui A., Rice C.M.;
"Processing of the yellow fever virus nonstructural polyprotein: a
catalytically active NS3 proteinase domain and NS2B are required for
cleavages at dibasic sites.";
J. Virol. 65:6042-6050(1991).
[13]
CHARACTERIZATION (SERINE PROTEASE NS3).
PubMed=7853494;
Chambers T.J., Nestorowicz A., Rice C.M.;
"Mutagenesis of the yellow fever virus NS2B/3 cleavage site:
determinants of cleavage site specificity and effects on polyprotein
processing and viral replication.";
J. Virol. 69:1600-1605(1995).
[14]
MUTAGENESIS OF ARG-2107; ARG-2505 AND ARG-2506, AND PROTEOLYTIC
CLEAVAGE (GENOME POLYPROTEIN).
PubMed=8421901; DOI=10.1006/viro.1993.1076;
Lin C., Chambers T.J., Rice C.M.;
"Mutagenesis of conserved residues at the yellow fever virus 3/4A and
4B/5 dibasic cleavage sites: effects on cleavage efficiency and
polyprotein processing.";
Virology 192:596-604(1993).
[15]
MUTAGENESIS OF ARG-2107; SER-2234 AND ARG-2506, AND PROTEOLYTIC
CLEAVAGE (GENOME POLYPROTEIN).
PubMed=8445732;
Lin C., Amberg S.M., Chambers T.J., Rice C.M.;
"Cleavage at a novel site in the NS4A region by the yellow fever virus
NS2B-3 proteinase is a prerequisite for processing at the downstream
4A/4B signalase site.";
J. Virol. 67:2327-2335(1993).
[16]
MUTAGENESIS OF PHE-1351; GLY-1352; ARG-1353; ARG-1354 AND SER-1355,
AND PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
PubMed=8116234; DOI=10.1006/viro.1994.1103;
Nestorowicz A., Chambers T.J., Rice C.M.;
"Mutagenesis of the yellow fever virus NS2A/2B cleavage site: effects
on proteolytic processing, viral replication, and evidence for
alternative processing of the NS2A protein.";
Virology 199:114-123(1994).
[17]
MUTAGENESIS OF ASN-908; SER-910; ASN-986 AND THR-988.
PubMed=8806496; DOI=10.1006/viro.1996.0406;
Muylaert I.R., Chambers T.J., Galler R., Rice C.M.;
"Mutagenesis of the N-linked glycosylation sites of the yellow fever
virus NS1 protein: effects on virus replication and mouse
neurovirulence.";
Virology 222:159-168(1996).
[18]
MUTAGENESIS OF ARG-1077.
PubMed=8985349;
Muylaert I.R., Galler R., Rice C.M.;
"Genetic analysis of the yellow fever virus NS1 protein:
identification of a temperature-sensitive mutation which blocks RNA
accumulation.";
J. Virol. 71:291-298(1997).
[19]
FUNCTION (NON-STRUCTURAL PROTEIN 1).
PubMed=9371625;
Lindenbach B.D., Rice C.M.;
"Trans-complementation of yellow fever virus NS1 reveals a role in
early RNA replication.";
J. Virol. 71:9608-9617(1997).
[20]
PHOSPHORYLATION (RNA-DIRECTED RNA POLYMERASE NS5).
PubMed=9621090;
Reed K.E., Gorbalenya A.E., Rice C.M.;
"The NS5A/NS5 proteins of viruses from three genera of the family
flaviviridae are phosphorylated by associated serine/threonine
kinases.";
J. Virol. 72:6199-6206(1998).
[21]
INTERACTION WITH NON-STRUCTURAL PROTEIN 4A (NON-STRUCTURAL PROTEIN 1),
AND INTERACTION WITH NON-STRUCTURAL PROTEIN 1 (NON-STRUCTURAL PROTEIN
4A).
PubMed=10233920;
Lindenbach B.D., Rice C.M.;
"Genetic interaction of flavivirus nonstructural proteins NS1 and NS4A
as a determinant of replicase function.";
J. Virol. 73:4611-4621(1999).
[22]
MUTAGENESIS OF 99-ARG--ARG-101.
PubMed=10482557;
Amberg S.M., Rice C.M.;
"Mutagenesis of the NS2B-NS3-mediated cleavage site in the flavivirus
capsid protein demonstrates a requirement for coordinated
processing.";
J. Virol. 73:8083-8094(1999).
[23]
MUTAGENESIS OF 116-LEU--GLY-121.
PubMed=10590087; DOI=10.1128/JVI.74.1.24-32.2000;
Lee E., Stocks C.E., Amberg S.M., Rice C.M., Lobigs M.;
"Mutagenesis of the signal sequence of yellow fever virus prM protein:
enhancement of signalase cleavage In vitro is lethal for virus
production.";
J. Virol. 74:24-32(2000).
[24]
MUTAGENESIS OF 1406-GLU--LYS-1409.
PubMed=10998334; DOI=10.1006/viro.2000.0488;
Droll D.A., Krishna Murthy H.M., Chambers T.J.;
"Yellow fever virus NS2B-NS3 protease: charged-to-alanine mutagenesis
and deletion analysis define regions important for protease complex
formation and function.";
Virology 275:335-347(2000).
[25]
MUTAGENESIS OF 1319-GLN--THR-1321.
PubMed=11967294; DOI=10.1128/JVI.76.10.4773-4784.2002;
Kummerer B.M., Rice C.M.;
"Mutations in the yellow fever virus nonstructural protein NS2A
selectively block production of infectious particles.";
J. Virol. 76:4773-4784(2002).
[26]
SUBUNIT (CAPSID PROTEIN C).
PubMed=12768036; DOI=10.1128/JVI.77.12.7143-7149.2003;
Jones C.T., Ma L., Burgner J.W., Groesch T.D., Post C.B., Kuhn R.J.;
"Flavivirus capsid is a dimeric alpha-helical protein.";
J. Virol. 77:7143-7149(2003).
[27]
SUBCELLULAR LOCATION (SMALL ENVELOPE PROTEIN M), AND SUBCELLULAR
LOCATION (ENVELOPE PROTEIN E).
PubMed=15507646; DOI=10.1128/JVI.78.22.12591-12602.2004;
Op De Beeck A., Rouille Y., Caron M., Duvet S., Dubuisson J.;
"The transmembrane domains of the prM and E proteins of yellow fever
virus are endoplasmic reticulum localization signals.";
J. Virol. 78:12591-12602(2004).
[28]
FUNCTION (NON-STRUCTURAL PROTEIN 4B).
PubMed=15956546; DOI=10.1128/JVI.79.13.8004-8013.2005;
Munoz-Jordan J.L., Laurent-Rolle M., Ashour J., Martinez-Sobrido L.,
Ashok M., Lipkin W.I., Garcia-Sastre A.;
"Inhibition of alpha/beta interferon signaling by the NS4B protein of
flaviviruses.";
J. Virol. 79:8004-8013(2005).
[29]
PHOSPHORYLATION AT SER-2562, AND MUTAGENESIS OF SER-2562.
PubMed=18757072; DOI=10.1016/j.virol.2008.07.013;
Bhattacharya D., Hoover S., Falk S.P., Weisblum B., Vestling M.,
Striker R.;
"Phosphorylation of yellow fever virus NS5 alters methyltransferase
activity.";
Virology 380:276-284(2008).
[30]
FUNCTION (SERINE PROTEASE NS3), AND MUTAGENESIS OF TRP-1833.
PubMed=18199634; DOI=10.1128/JVI.02447-07;
Patkar C.G., Kuhn R.J.;
"Yellow Fever virus NS3 plays an essential role in virus assembly
independent of its known enzymatic functions.";
J. Virol. 82:3342-3352(2008).
[31]
FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5).
PubMed=19850911; DOI=10.1261/rna.1609709;
Issur M., Geiss B.J., Bougie I., Picard-Jean F., Despins S.,
Mayette J., Hobdey S.E., Bisaillon M.;
"The flavivirus NS5 protein is a true RNA guanylyltransferase that
catalyzes a two-step reaction to form the RNA cap structure.";
RNA 15:2340-2350(2009).
[32]
INTERACTION WITH HUMAN PDCD6IP (SERINE PROTEASE NS3).
PubMed=21044891; DOI=10.1016/j.micinf.2010.10.010;
Carpp L.N., Galler R., Bonaldo M.C.;
"Interaction between the yellow fever virus nonstructural protein NS3
and the host protein Alix contributes to the release of infectious
particles.";
Microbes Infect. 13:85-95(2011).
[33]
BIOPHYSICOCHEMICAL PROPERTIES (SERINE PROTEASE NS3), CATALYTIC
ACTIVITY (SERINE PROTEASE NS3), AND PROTEOLYTIC CLEAVAGE
(POLYPROTEIN).
PubMed=21419753; DOI=10.1016/j.bbrc.2011.03.054;
Kondo M.Y., Oliveira L.C., Okamoto D.N., de Araujo M.R.,
Duarte dos Santos C.N., Juliano M.A., Juliano L., Gouvea I.E.;
"Yellow fever virus NS2B/NS3 protease: hydrolytic properties and
substrate specificity.";
Biochem. Biophys. Res. Commun. 407:640-644(2011).
[34]
FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), UBIQUITINATION AT LYS-5
(RNA-DIRECTED RNA POLYMERASE NS5), INTERACTION WITH HOST STAT2
(RNA-DIRECTED RNA POLYMERASE NS5), MUTAGENESIS OF LYS-2512, AND
INTERACTION WITH HOST TRIM23 (RNA-DIRECTED RNA POLYMERASE NS5).
PubMed=25211074; DOI=10.1016/j.chom.2014.07.015;
Laurent-Rolle M., Morrison J., Rajsbaum R., Macleod J.M.,
Pisanelli G., Pham A., Ayllon J., Miorin L., Martinez-Romero C.,
tenOever B.R., Garcia-Sastre A.;
"The interferon signaling antagonist function of yellow fever virus
NS5 protein is activated by type I interferon.";
Cell Host Microbe 16:314-327(2014).
[35]
INTERACTION WITH SERINE PROTEASE NS3 (NON-STRUCTURAL PROTEIN 2A),
INTERACTION WITH NON-STRUCTURAL PROTEIN 2A (SERINE PROTEASE NS3),
MUTAGENESIS OF 1152-ARG--ARG-1154; 1229-ARG--ARG-1231 AND GLN-1319,
AND TOPOLOGY (NON-STRUCTURAL PROTEIN 2A).
PubMed=25694595; DOI=10.1128/JVI.03351-14;
Vossmann S., Wieseler J., Kerber R., Kuemmerer B.M.;
"A basic cluster in the N terminus of yellow fever virus NS2A
contributes to infectious particle production.";
J. Virol. 89:4951-4965(2015).
[36]
FUNCTION (CAPSID PROTEIN C).
PubMed=27849599; DOI=10.1073/pnas.1600544113;
Samuel G.H., Wiley M.R., Badawi A., Adelman Z.N., Myles K.M.;
"Yellow fever virus capsid protein is a potent suppressor of RNA
silencing that binds double-stranded RNA.";
Proc. Natl. Acad. Sci. U.S.A. 113:13863-13868(2016).
[37]
STRUCTURE BY ELECTRON MICROSCOPY (25 ANGSTROMS) OF IMMATURE PARTICLES.
PubMed=12773377; DOI=10.1093/emboj/cdg270;
Zhang Y., Corver J., Chipman P.R., Zhang W., Pletnev S.V., Sedlak D.,
Baker T.S., Strauss J.H., Kuhn R.J., Rossmann M.G.;
"Structures of immature flavivirus particles.";
EMBO J. 22:2604-2613(2003).
[38]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1671-2107, AND CATALYTIC
ACTIVITY (SERINE PROTEASE NS3).
PubMed=16051820; DOI=10.1128/JVI.79.16.10268-10277.2005;
Wu J., Bera A.K., Kuhn R.J., Smith J.L.;
"Structure of the Flavivirus helicase: implications for catalytic
activity, protein interactions, and proteolytic processing.";
J. Virol. 79:10268-10277(2005).
[39] {ECO:0000244|PDB:3EVA, ECO:0000244|PDB:3EVB, ECO:0000244|PDB:3EVC, ECO:0000244|PDB:3EVD, ECO:0000244|PDB:3EVE, ECO:0000244|PDB:3EVF}
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 2507-2772 IN COMPLEX WITH
GTP; GUANOSINE-P3-ADENOSINE-5',5'-TRIPHOSPHATE;
P1-7-METHYLGUANOSINE-P3-ADENOSINE-5',5'-TRIPHOSPHATE AND
S-ADENOSYL-L-HOMOCYSTEINE.
PubMed=19101564; DOI=10.1016/j.jmb.2008.11.058;
Geiss B.J., Thompson A.A., Andrews A.J., Sons R.L., Gari H.H.,
Keenan S.M., Peersen O.B.;
"Analysis of flavivirus NS5 methyltransferase cap binding.";
J. Mol. Biol. 385:1643-1654(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.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Capsid protein C: Inhibits RNA silencing by interfering
with host Dicer. {ECO:0000269|PubMed:27849599}.
-!- 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 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, ECO:0000269|PubMed:9371625}.
-!- FUNCTION: Non-structural protein 2A: Component of the viral RNA
replication complex that functions in virion assembly and
antagonizes the host immune response.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: 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.
Also plays a role in virus assembly (PubMed:18199634).
{ECO:0000255|PROSITE-ProRule:PRU00860,
ECO:0000269|PubMed:18199634}.
-!- 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
(PubMed:15956546). {ECO:0000250|UniProtKB:Q9Q6P4,
ECO:0000269|PubMed:15956546}.
-!- FUNCTION: RNA-directed RNA polymerase NS5: Replicates the viral
(+) and (-) RNA genome, and performs the capping of genomes in the
cytoplasm (PubMed:19850911). NS5 methylates viral RNA cap at
guanine N-7 and ribose 2'-O positions (PubMed:19850911). 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:25211074). IFN-I induces binding of NS5 to host IFN-
activated transcription factor STAT2, preventing its
transcriptional activity. Host TRIM23 is the E3 ligase that
interacts with and polyubiquitinates NS5 to promote its binding to
STAT2 and trigger IFN-I signaling inhibition (PubMed:25211074).
{ECO:0000269|PubMed:19850911, ECO:0000269|PubMed:25211074}.
-!- 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. {ECO:0000269|PubMed:21419753}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539,
ECO:0000269|PubMed:16051820}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
{ECO:0000269|PubMed:16051820}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl
5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-
adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-
triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].
{ECO:0000255|PROSITE-ProRule:PRU00924}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 9. {ECO:0000269|PubMed:21419753};
-!- SUBUNIT: Capsid protein C: Homodimer (PubMed:12768036). Interacts
(via N-terminus) with host EXOC1 (via C-terminus); this
interaction results in EXOC1 degradation through the proteasome
degradation pathway (By similarity). 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. Interacts with protein prM.
Interacts with non-structural protein 1 (By similarity). Non-
structural protein 1: Homodimer; Homohexamer when secreted.
Interacts with envelope protein E (By similarity). Non-structural
protein 2A: Interacts (via N-terminus) with serine protease NS3
(PubMed:25694595). Non-structural protein 2B: Forms a heterodimer
with serine protease NS3. May form homooligomers (By similarity).
Serine protease NS3: Forms a heterodimer with NS2B (By
similarity). Interacts with non-structural protein 2A (via N-
terminus) (PubMed:25694595). Interacts with NS4B (By similarity).
Interacts with unphosphorylated RNA-directed RNA polymerase NS5;
this interaction stimulates RNA-directed RNA polymerase NS5
guanylyltransferase activity (By similarity). NS3 interacts with
host PDCD6IP; this interaction contributes to virion release
(PubMed:21044891). Non-structural protein 4B: Interacts with
serine protease NS3 (By similarity). RNA-directed RNA polymerase
NS5: Homodimer (By similarity). Interacts with host STAT2; this
interaction prevents the establishment of cellular antiviral state
(PubMed:25211074). Interacts with host TRIM23; this interaction
leads to NS5 ubiquitination (PubMed:25211074).
{ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:12768036,
ECO:0000269|PubMed:21044891, ECO:0000269|PubMed:25211074,
ECO:0000269|PubMed:25694595}.
-!- SUBCELLULAR LOCATION: Capsid protein C: Virion
{ECO:0000250|UniProtKB:P17763}. Host nucleus
{ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear
region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Peptide pr: Secreted
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane
{ECO:0000269|PubMed:15507646}; Multi-pass membrane protein
{ECO:0000269|PubMed:15507646}. Host endoplasmic reticulum membrane
{ECO:0000269|PubMed:15507646}; Multi-pass membrane protein
{ECO:0000255}. Note=ER membrane retention is mediated by the
transmembrane domains. {ECO:0000269|PubMed:15507646}.
-!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
{ECO:0000305}; Multi-pass membrane protein
{ECO:0000269|PubMed:15507646}. Host endoplasmic reticulum membrane
{ECO:0000269|PubMed:3008425}; Multi-pass membrane protein
{ECO:0000255}. Note=ER membrane retention is mediated by the
transmembrane domains. {ECO:0000269|PubMed:15507646}.
-!- 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: 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. The nascent capsid protein C contains a C-
terminal hydrophobic domain that act as a signal sequence for
translocation of prM into the lumen of the ER. Mature capsid
protein C is cleaved at a site upstream of this hydrophobic domain
by NS3. prM is cleaved in post-Golgi vesicles by a host furin,
releasing the mature small envelope protein M, and peptide pr.
Non-structural protein 2A-alpha, a C-terminally truncated form of
non-structural protein 2A, results from partial cleavage by NS3.
Specific enzymatic cleavages in vivo yield mature proteins peptide
2K acts as a signal sequence and is removed from the N-terminus of
NS4B by the host signal peptidase in the ER lumen. Signal cleavage
at the 2K-4B site requires a prior NS3 protease-mediated cleavage
at the 4A-2K site. {ECO:0000269|PubMed:1833562,
ECO:0000269|PubMed:21419753, ECO:0000269|PubMed:3008425,
ECO:0000269|PubMed:8116234, ECO:0000269|PubMed:8189517,
ECO:0000269|PubMed:8421901, ECO:0000269|PubMed:8445732}.
-!- 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: Polyubiquitinated; ubiquitination is probably mediated by
host TRIM23 and is prerequisite for NS5-STAT2 interaction. NS5 is
not ISGylated or sumoylated. {ECO:0000269|PubMed:25211074}.
-!- PTM: RNA-directed RNA polymerase NS5: Phosphorylated on serines
residues. This phosphorylation may trigger NS5 nuclear
localization. {ECO:0000269|PubMed:9621090}.
-!- 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; X03700; CAA27332.1; -; Genomic_RNA.
EMBL; X15062; CAB37419.1; -; Genomic_RNA.
EMBL; U17066; AAC54267.1; -; Genomic_RNA.
EMBL; U17067; AAC54268.1; -; Genomic_RNA.
EMBL; AF052437; AAC35899.1; -; Genomic_RNA.
EMBL; AF052438; AAC35900.1; -; Genomic_RNA.
EMBL; AF052439; AAC35901.1; -; Genomic_RNA.
EMBL; AF052444; AAC35906.1; -; Genomic_RNA.
EMBL; AF052445; AAC35907.1; -; Genomic_RNA.
EMBL; AF052446; AAC35908.1; -; Genomic_RNA.
EMBL; DQ118157; AAZ31436.1; -; Genomic_RNA.
EMBL; DQ100292; AAZ07885.1; -; Genomic_RNA.
PIR; A03914; GNWVY.
PIR; S07757; GNWVYP.
RefSeq; NP_041726.1; NC_002031.1.
PDB; 1NA4; EM; -; -.
PDB; 1YKS; X-ray; 1.80 A; A=1671-2107.
PDB; 3EVA; X-ray; 1.50 A; A=2507-2772.
PDB; 3EVB; X-ray; 1.85 A; A=2507-2772.
PDB; 3EVC; X-ray; 1.60 A; A=2507-2772.
PDB; 3EVD; X-ray; 1.50 A; A=2507-2772.
PDB; 3EVE; X-ray; 1.70 A; A=2507-2772.
PDB; 3EVF; X-ray; 1.45 A; A=2507-2772.
PDB; 5FFM; X-ray; 2.60 A; A=1671-2107.
PDBsum; 1NA4; -.
PDBsum; 1YKS; -.
PDBsum; 3EVA; -.
PDBsum; 3EVB; -.
PDBsum; 3EVC; -.
PDBsum; 3EVD; -.
PDBsum; 3EVE; -.
PDBsum; 3EVF; -.
PDBsum; 5FFM; -.
ProteinModelPortal; P03314; -.
SMR; P03314; -.
PRIDE; P03314; -.
GeneID; 1502173; -.
KEGG; vg:1502173; -.
OrthoDB; VOG0900007N; -.
BRENDA; 2.7.7.50; 6740.
BRENDA; 3.6.4.13; 6740.
EvolutionaryTrace; P03314; -.
Proteomes; UP000000360; Genome.
Proteomes; UP000119912; Genome.
Proteomes; UP000138083; Genome.
Proteomes; UP000141075; Genome.
Proteomes; UP000158765; Genome.
Proteomes; UP000158778; Genome.
Proteomes; UP000180827; Genome.
Proteomes; UP000180883; Genome.
Proteomes; UP000180940; Genome.
Proteomes; UP000181442; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IMP:CACAO.
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: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:0046762; P:viral budding from ER membrane; IDA:UniProtKB.
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; cd06174; MFS; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 3.30.387.10; -; 1.
Gene3D; 3.30.67.10; -; 1.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR000069; Env_glycoprot_M_flavivir.
InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
InterPro; IPR001122; Flavi_capsidC.
InterPro; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
InterPro; IPR001157; Flavi_NS1.
InterPro; IPR000752; Flavi_NS2A.
InterPro; IPR000487; Flavi_NS2B.
InterPro; IPR000404; Flavi_NS4A.
InterPro; IPR001528; Flavi_NS4B.
InterPro; IPR002535; Flavi_propep.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR013756; GlyE_cen_dom_subdom2.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR020846; MFS_dom.
InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR000208; RNA-dir_pol_flavivirus.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01003; Flavi_capsid; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF02832; Flavi_glycop_C; 1.
Pfam; PF00869; Flavi_glycoprot; 1.
Pfam; PF01004; Flavi_M; 1.
Pfam; PF00948; Flavi_NS1; 1.
Pfam; PF01005; Flavi_NS2A; 1.
Pfam; PF01002; Flavi_NS2B; 1.
Pfam; PF01350; Flavi_NS4A; 1.
Pfam; PF01349; Flavi_NS4B; 1.
Pfam; PF00972; Flavi_NS5; 1.
Pfam; PF01570; Flavi_propep; 1.
Pfam; PF01728; FtsJ; 1.
Pfam; PF00949; Peptidase_S7; 1.
PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
TIGRFAMs; TIGR04240; flavi_E_stem; 1.
PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; 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;
GTP-binding; 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 STAT2 by virus; Isopeptide bond; Membrane;
Metal-binding; Methyltransferase; mRNA capping; mRNA processing;
Multifunctional enzyme; 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; Ubl conjugation; 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 3411 Genome polyprotein.
/FTId=PRO_0000405153.
CHAIN 1 101 Capsid protein C.
{ECO:0000269|PubMed:8189517}.
/FTId=PRO_0000037754.
PROPEP 102 121 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000269|PubMed:8189517}.
/FTId=PRO_0000261384.
CHAIN 122 285 prM. {ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000261385.
CHAIN 122 210 Peptide pr.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037755.
CHAIN 211 285 Small envelope protein M.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037756.
CHAIN 286 778 Envelope protein E.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037757.
CHAIN 779 1130 Non-structural protein 1.
{ECO:0000269|PubMed:3008425}.
/FTId=PRO_0000037758.
CHAIN 1131 1354 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037759.
CHAIN 1131 1320 Non-structural protein 2A-alpha.
{ECO:0000269|PubMed:8806496}.
/FTId=PRO_0000261386.
CHAIN 1355 1484 Serine protease subunit NS2B.
{ECO:0000269|PubMed:3008425}.
/FTId=PRO_0000037760.
CHAIN 1485 2107 Serine protease NS3.
{ECO:0000269|PubMed:1833562,
ECO:0000269|PubMed:8421901}.
/FTId=PRO_0000037761.
CHAIN 2108 2233 Non-structural protein 4A.
{ECO:0000269|PubMed:8445732}.
/FTId=PRO_0000037762.
PEPTIDE 2234 2256 Peptide 2k. {ECO:0000269|PubMed:2922923}.
/FTId=PRO_0000261387.
CHAIN 2257 2506 Non-structural protein 4B.
{ECO:0000269|PubMed:8421901}.
/FTId=PRO_0000037763.
CHAIN 2507 3411 RNA-directed RNA polymerase NS5.
{ECO:0000269|PubMed:1833562,
ECO:0000269|PubMed:3008425}.
/FTId=PRO_0000037764.
TOPO_DOM 1 104 Cytoplasmic. {ECO:0000255}.
TRANSMEM 105 125 Helical. {ECO:0000255}.
TOPO_DOM 126 244 Extracellular. {ECO:0000255}.
TRANSMEM 245 265 Helical. {ECO:0000255}.
TOPO_DOM 266 270 Cytoplasmic. {ECO:0000255}.
TRANSMEM 271 285 Helical. {ECO:0000255}.
TOPO_DOM 286 730 Extracellular. {ECO:0000255}.
TRANSMEM 731 751 Helical. {ECO:0000255}.
TOPO_DOM 752 757 Extracellular. {ECO:0000255}.
TRANSMEM 758 778 Helical. {ECO:0000255}.
TOPO_DOM 779 1132 Extracellular. {ECO:0000255}.
TRANSMEM 1133 1153 Helical. {ECO:0000255}.
TOPO_DOM 1154 1201 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1202 1222 Helical. {ECO:0000255}.
TOPO_DOM 1223 1287 Lumenal. {ECO:0000255}.
TRANSMEM 1288 1308 Helical. {ECO:0000255}.
TOPO_DOM 1309 1355 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1356 1376 Helical. {ECO:0000255}.
TOPO_DOM 1377 1378 Lumenal. {ECO:0000255}.
TRANSMEM 1379 1399 Helical. {ECO:0000255}.
TOPO_DOM 1400 1456 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1457 1477 Helical. {ECO:0000255}.
TOPO_DOM 1478 2157 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2158 2178 Helical. {ECO:0000255}.
TOPO_DOM 2179 2186 Lumenal. {ECO:0000255}.
INTRAMEM 2187 2207 Helical. {ECO:0000255}.
TOPO_DOM 2208 2209 Lumenal. {ECO:0000255}.
TRANSMEM 2210 2230 Helical. {ECO:0000255}.
TOPO_DOM 2231 2241 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2242 2262 Helical; Note=Signal for NS4B.
{ECO:0000255}.
TOPO_DOM 2263 2293 Lumenal. {ECO:0000255}.
INTRAMEM 2294 2314 Helical. {ECO:0000255}.
TOPO_DOM 2315 2360 Lumenal. {ECO:0000255}.
TRANSMEM 2361 2381 Helical. {ECO:0000255}.
TOPO_DOM 2382 2421 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2422 2442 Helical. {ECO:0000255}.
TOPO_DOM 2443 2445 Lumenal. {ECO:0000255}.
TRANSMEM 2446 2466 Helical. {ECO:0000255}.
TOPO_DOM 2467 3411 Cytoplasmic. {ECO:0000255}.
DOMAIN 1485 1665 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1669 1825 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1820 1997 Helicase C-terminal.
DOMAIN 2507 2771 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3035 3187 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1682 1689 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 38 72 Hydrophobic; homodimerization of capsid
protein C.
{ECO:0000250|UniProtKB:P29990}.
REGION 383 396 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
REGION 1407 1446 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
REGION 1673 1676 Important for RNA-binding.
{ECO:0000250|UniProtKB:P14340}.
MOTIF 1773 1776 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 2878 2911 Nuclear localization signal.
{ECO:0000250}.
COMPBIAS 2656 2660 Poly-Ser.
ACT_SITE 1537 1537 Charge relay system; for serine protease
NS3 activity.
ACT_SITE 1561 1561 Charge relay system; for serine protease
NS3 activity.
ACT_SITE 1622 1622 Charge relay system; for serine protease
NS3 activity.
ACT_SITE 2567 2567 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2652 2652 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2688 2688 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2724 2724 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2945 2945 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 2949 2949 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:P14335}.
METAL 2954 2954 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 2957 2957 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 3222 3222 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:P14335}.
METAL 3238 3238 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
METAL 3357 3357 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
BINDING 2519 2519 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924,
ECO:0000269|PubMed:19101564}.
BINDING 2522 2522 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924,
ECO:0000269|PubMed:19101564}.
BINDING 2523 2523 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924,
ECO:0000269|PubMed:19101564}.
BINDING 2525 2525 mRNA cap; via carbonyl oxygen.
{ECO:0000269|PubMed:19101564}.
BINDING 2534 2534 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924,
ECO:0000269|PubMed:19101564}.
BINDING 2562 2562 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2592 2592 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2593 2593 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2610 2610 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2611 2611 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2637 2637 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2638 2638 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2656 2656 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924,
ECO:0000269|PubMed:19101564}.
BINDING 2719 2719 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924,
ECO:0000269|PubMed:19101564}.
BINDING 2721 2721 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924,
ECO:0000269|PubMed:19101564}.
BINDING 2726 2726 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 101 102 Cleavage; by viral protease NS3.
{ECO:0000269|PubMed:8189517}.
SITE 121 122 Cleavage; by host signal peptidase.
{ECO:0000269|PubMed:8189517}.
SITE 210 211 Cleavage; by host furin.
{ECO:0000250|UniProtKB:P29990}.
SITE 285 286 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 778 779 Cleavage; by host signal peptidase.
{ECO:0000269|PubMed:3008425}.
SITE 1130 1131 Cleavage; by host.
{ECO:0000250|UniProtKB:P29990}.
SITE 1320 1321 Cleavage; by viral protease NS3.
{ECO:0000269|PubMed:8806496}.
SITE 1354 1355 Cleavage; by viral protease NS3.
{ECO:0000269|PubMed:21419753,
ECO:0000269|PubMed:8116234}.
SITE 1484 1485 Cleavage; by autolysis.
{ECO:0000269|PubMed:21419753,
ECO:0000269|PubMed:3008425}.
SITE 1945 1945 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 1948 1948 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 2107 2108 Cleavage; by autolysis.
{ECO:0000269|PubMed:21419753,
ECO:0000269|PubMed:8421901,
ECO:0000269|PubMed:8445732}.
SITE 2233 2234 Cleavage; by viral protease NS3.
{ECO:0000269|PubMed:8445732}.
SITE 2256 2257 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 2506 2507 Cleavage; by viral protease NS3.
{ECO:0000269|PubMed:3008425,
ECO:0000269|PubMed:8421901,
ECO:0000269|PubMed:8445732}.
SITE 2530 2530 mRNA cap binding.
SITE 2567 2567 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2652 2652 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU00924,
ECO:0000269|PubMed:18757072}.
SITE 2653 2653 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2688 2688 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2724 2724 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
MOD_RES 2562 2562 Phosphoserine.
{ECO:0000269|PubMed:18757072}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 150 150 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 908 908 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 986 986 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 288 315 {ECO:0000250|UniProtKB:P17763}.
DISULFID 345 406 {ECO:0000250|UniProtKB:P17763}.
DISULFID 345 401 {ECO:0000250|UniProtKB:P06935}.
DISULFID 359 390 {ECO:0000250|UniProtKB:P17763}.
DISULFID 377 406 {ECO:0000250|UniProtKB:P06935}.
DISULFID 377 401 {ECO:0000250|UniProtKB:P17763}.
DISULFID 467 568 {ECO:0000250|UniProtKB:P17763}.
DISULFID 585 615 {ECO:0000250|UniProtKB:P17763}.
DISULFID 782 793 {ECO:0000250|UniProtKB:P17763}.
DISULFID 833 921 {ECO:0000250|UniProtKB:P17763}.
DISULFID 957 1002 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1058 1107 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1069 1091 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1090 1094 {ECO:0000250|UniProtKB:P17763}.
VARIANT 341 341 V -> A (in strain: Isolate Brazil/YF-
VAVD/75 vaccine and Isolate 17DD
vaccine).
VARIANT 438 438 N -> T (in strain: Isolate 17D-204-USA
HONG1 vaccine, Isolate 17D-204-USA HONG2
vaccine and Isolate 17D-204-USA HONG3
vaccine).
VARIANT 440 440 D -> S (in strain: Isolate 17DD vaccine).
VARIANT 610 610 S -> P (in strain: Isolate Brazil/YF-
VAVD/75 vaccine and Isolate 17DD
vaccine).
VARIANT 629 629 I -> V (in strain: Isolate Brazil/YF-
VAVD/75 vaccine).
VARIANT 701 701 T -> V (in strain: Isolate 17DD vaccine).
VARIANT 744 744 A -> V (in strain: Isolate 17D-204-South
Africa vaccine large plaque variant).
VARIANT 764 764 L -> M (in strain: Isolate 17D-204-South
Africa vaccine large plaque variant).
VARIANT 1299 1299 F -> L (in strain: Isolate Brazil/YF-
VAVD/75 vaccine and Isolate 17DD
vaccine).
VARIANT 1666 1666 Q -> R (in strain: Isolate 17DD vaccine).
VARIANT 1669 1669 P -> S (in strain: Isolate Brazil/YF-
VAVD/75 vaccine).
VARIANT 1679 1679 V -> I (in strain: Isolate Brazil/YF-
VAVD/75 vaccine and Isolate 17DD
vaccine).
VARIANT 2214 2214 V -> I (in strain: Isolate 17D-204-USA
HONG1 vaccine, Isolate 17D-204-USA HONG2
vaccine, Isolate 17D-204-USA HONG3
vaccine, Isolate Spain/AVD2791-93F/04
vaccine, Isolate Brazil/YF-VAVD/75
vaccine, Isolate 17DD vaccine and Isolate
Pasteur 17D-204 vaccine).
VARIANT 2277 2277 P -> S (in strain: Isolate Brazil/YF-
VAVD/75 vaccine).
VARIANT 2401 2401 E -> K (in strain: Isolate 17D-204-South
Africa vaccine large plaque variant,
Isolate 17D-204-South Africa vaccine
medium plaque variant, Isolate 17D-204-
South Africa vaccine, Isolate 17D-204-USA
HONG1 vaccine, Isolate 17D-204-USA HONG2
vaccine, Isolate 17D-204-USA HONG3
vaccine, Isolate Brazil/YF-VAVD/75
vaccine, Isolate Spain/AVD2791-93F/04
vaccine, Isolate 17DD vaccine and Isolate
Pasteur 17D-204 vaccine).
VARIANT 2460 2460 L -> S (in strain: Isolate 17D-204-USA
HONG vaccine1, Isolate 17D-204-USA HONG2
vaccine and Isolate 17D-204-USA HONG3
vaccine).
VARIANT 2528 2528 R -> Q (in strain: Isolate Brazil/YF-
VAVD/75 vaccine and Isolate 17DD
vaccine).
VARIANT 2643 2643 P -> S (in strain: Isolate 17D-204-South
Africa vaccine medium plaque variant).
VARIANT 2661 2661 V -> I (in strain: Isolate Brazil/YF-
VAVD/75 vaccine).
VARIANT 2897 2897 N -> S (in strain: Isolate Brazil/YF-
VAVD/75 vaccine and Isolate 17DD
vaccine).
VARIANT 3110 3110 G -> R (in strain: Isolate 17D-204-USA
HONG2 vaccine).
VARIANT 3135 3135 M -> N (in strain: Isolate Brazil/YF-
VAVD/75 vaccine).
VARIANT 3163 3163 D -> N (in strain: Isolate 17D-204-South
Africa vaccine large plaque variant,
Isolate 17D-204-South Africa vaccine
medium plaque variant, Isolate 17D-204-
South Africa vaccine, Isolate 17D-204-USA
HONG1 vaccine, Isolate 17D-204-USA HONG2
vaccine, Isolate 17D-204-USA HONG3
vaccine, Isolate Brazil/YF-VAVD/75
vaccine, Isolate Spain/AVD2791-93F/04
vaccine, Isolate 17DD vaccine and Isolate
Pasteur 17D-204 vaccine).
VARIANT 3222 3222 H -> R (in strain: Isolate Brazil/YF-
VAVD/75 vaccine).
MUTAGEN 98 101 RKRR->AAAA: Complete loss of NS2B-NS3
cleavage.
MUTAGEN 98 101 RKRR->AKAA: Complete loss of NS2B-NS3
cleavage.
MUTAGEN 98 101 RKRR->AKRA: Reduces NS2B-NS3 cleavage
efficiency.
MUTAGEN 98 100 RKR->AAA: Complete loss of NS2B-NS3
cleavage.
MUTAGEN 98 100 RKR->AKA: Complete loss of NS2B-NS3
cleavage.
MUTAGEN 98 99 RK->AA: Reduces NS2B-NS3 cleavage
efficiency.
MUTAGEN 99 101 KRR->ARA: Complete loss of NS2B-NS3
cleavage. {ECO:0000269|PubMed:10482557}.
MUTAGEN 99 100 KR->AA: Complete loss of NS2B-NS3
cleavage.
MUTAGEN 100 101 RR->AA: Reduces NS2B-NS3 cleavage
efficiency.
MUTAGEN 116 121 LLMTGG->VPQAQA: Complete loss of
infectious virus production. Enhances
signal peptidase cleavage in vitro of
nascent capsid protein C.
{ECO:0000269|PubMed:10590087}.
MUTAGEN 908 908 N->A: Reduces viral RNA accumulation and
NS1 secretion.
{ECO:0000269|PubMed:8806496}.
MUTAGEN 910 910 S->A: Reduces viral RNA accumulation and
NS1 secretion.
{ECO:0000269|PubMed:8806496}.
MUTAGEN 986 986 N->A: No effect.
{ECO:0000269|PubMed:8806496}.
MUTAGEN 988 988 T->A: No effect.
{ECO:0000269|PubMed:8806496}.
MUTAGEN 1077 1077 R->A: Blocks RNA replication.
{ECO:0000269|PubMed:8985349}.
MUTAGEN 1152 1154 RKR->AAA: Defective in infectious
particle production; almost no effect on
viral replication.
{ECO:0000269|PubMed:25694595}.
MUTAGEN 1229 1231 RER->AAA: Defective in infectious
particle production; almost no effect on
viral replication.
{ECO:0000269|PubMed:25694595}.
MUTAGEN 1319 1321 QKT->RRS: Increases NS2A-alpha
processing, complete loss of NS2A.
MUTAGEN 1319 1319 Q->A: Almost no effect on viral
replication.
{ECO:0000269|PubMed:25694595}.
MUTAGEN 1319 1319 Q->S: Complete loss of cleavage and NS2A
alpha. Complete loss of infectivity.
{ECO:0000269|PubMed:11967294}.
MUTAGEN 1320 1320 K->E,I,Q,S: Complete loss of cleavage and
NS2A-alpha processing. Complete loss of
infectivity.
{ECO:0000269|PubMed:11967294}.
MUTAGEN 1320 1320 K->R: No effect on NS2A-alpha processing.
{ECO:0000269|PubMed:11967294}.
MUTAGEN 1321 1321 T->V: Complete loss of cleavage and NS2A
alpha synthesis. Complete loss of
infectivity.
{ECO:0000269|PubMed:11967294}.
MUTAGEN 1351 1351 F->C,I,V: Enhances NS2A-NS2B cleavage
efficiency. {ECO:0000269|PubMed:8116234}.
MUTAGEN 1351 1351 F->G: No effect on NS2A-NS2B cleavage
efficiency. {ECO:0000269|PubMed:8116234}.
MUTAGEN 1352 1352 G->A,K: Enhances NS2A-NS2B cleavage
efficiency. {ECO:0000269|PubMed:8116234}.
MUTAGEN 1352 1352 G->E,V: Reduces NS2A-NS2B cleavage
efficiency. {ECO:0000269|PubMed:8116234}.
MUTAGEN 1353 1353 R->H,K,R,T: Reduces NS2A-NS2B cleavage
efficiency. {ECO:0000269|PubMed:8116234}.
MUTAGEN 1353 1353 R->L,P: Complete loss of NS2A-NS2B
cleavage. {ECO:0000269|PubMed:8116234}.
MUTAGEN 1354 1354 R->I,N,S,T: Complete loss of NS2A-NS2B
cleavage. {ECO:0000269|PubMed:8116234}.
MUTAGEN 1354 1354 R->K: Reduces of NS2A-NS2B cleavage
efficiency. {ECO:0000269|PubMed:8116234}.
MUTAGEN 1355 1355 S->D,K,R,V: Complete loss of NS2A-NS2B
cleavage. {ECO:0000269|PubMed:8116234}.
MUTAGEN 1355 1355 S->G: Reduces of NS2A-NS2B cleavage
efficiency. {ECO:0000269|PubMed:8116234}.
MUTAGEN 1406 1409 ELKK->ALAA: Complete loss of polyprotein
cleavage. {ECO:0000269|PubMed:10998334}.
MUTAGEN 1537 1537 H->A: Complete loss NS3 protease
activity. {ECO:0000269|PubMed:2147282}.
MUTAGEN 1561 1561 D->A,N: Complete loss NS3 protease
activity. {ECO:0000269|PubMed:2147282}.
MUTAGEN 1622 1622 S->A: Complete loss NS3 protease
activity. {ECO:0000269|PubMed:2147282}.
MUTAGEN 1622 1622 S->C: Diminishes NS3 protease activity.
{ECO:0000269|PubMed:2147282}.
MUTAGEN 1833 1833 W->A: Complete loss of production of
infectious virus particles.
{ECO:0000269|PubMed:18199634}.
MUTAGEN 2107 2107 R->A,L,M,T,V: Reduces NS4A-NS4B cleavage
efficiency. {ECO:0000269|PubMed:8421901}.
MUTAGEN 2107 2107 R->E: Complete loss of NS4A-NS4B
cleavage. {ECO:0000269|PubMed:8421901,
ECO:0000269|PubMed:8445732}.
MUTAGEN 2107 2107 R->K: No effect on NS4A-NS4B cleavage
efficiency. {ECO:0000269|PubMed:8421901}.
MUTAGEN 2107 2107 R->P: Complete loss of NS4A-NS4B
cleavage. {ECO:0000269|PubMed:8421901}.
MUTAGEN 2234 2234 S->A,T: No effect on NS4A-NS4B cleavage.
{ECO:0000269|PubMed:8445732}.
MUTAGEN 2234 2234 S->I,P: No effect on NS4A-NS4B cleavage.
{ECO:0000269|PubMed:8445732}.
MUTAGEN 2505 2505 R->A,I,L,Q,S,T: No effect on NS4B-NS5
cleavage efficiency.
{ECO:0000269|PubMed:8421901}.
MUTAGEN 2505 2505 R->P: Reduces NS4B-NS5 cleavage
efficiency. {ECO:0000269|PubMed:8421901}.
MUTAGEN 2506 2506 R->E: Complete loss of NS4B-NS5 cleavage.
{ECO:0000269|PubMed:8421901,
ECO:0000269|PubMed:8445732}.
MUTAGEN 2506 2506 R->H,N,Q: Reduces NS4B-NS5 cleavage
efficiency. {ECO:0000269|PubMed:8421901}.
MUTAGEN 2506 2506 R->K: No effect on NS4B-NS5 cleavage
efficiency. {ECO:0000269|PubMed:8421901}.
MUTAGEN 2506 2506 R->Y: Complete loss of NS4B-NS5 cleavage.
{ECO:0000269|PubMed:8421901}.
MUTAGEN 2507 2507 G->A,S: Reduces NS4B-NS5 cleavage
efficiency.
MUTAGEN 2507 2507 G->E,K,L,M,N,V: Reduces NS4B-NS5 cleavage
efficiency.
MUTAGEN 2512 2512 K->R: Completet loss of NS5 binding to
STAT2 after IFN-I stimulation.
{ECO:0000269|PubMed:25211074}.
MUTAGEN 2562 2562 S->A: Complete loss of 2'-O-MTase
activity. {ECO:0000269|PubMed:18757072}.
STRAND 1677 1680 {ECO:0000244|PDB:1YKS}.
TURN 1688 1691 {ECO:0000244|PDB:1YKS}.
HELIX 1692 1702 {ECO:0000244|PDB:1YKS}.
STRAND 1707 1713 {ECO:0000244|PDB:1YKS}.
HELIX 1714 1723 {ECO:0000244|PDB:1YKS}.
TURN 1724 1726 {ECO:0000244|PDB:1YKS}.
STRAND 1729 1731 {ECO:0000244|PDB:1YKS}.
STRAND 1746 1750 {ECO:0000244|PDB:1YKS}.
HELIX 1751 1758 {ECO:0000244|PDB:1YKS}.
STRAND 1760 1762 {ECO:0000244|PDB:1YKS}.
STRAND 1768 1772 {ECO:0000244|PDB:1YKS}.
TURN 1773 1776 {ECO:0000244|PDB:1YKS}.
HELIX 1780 1794 {ECO:0000244|PDB:1YKS}.
STRAND 1799 1803 {ECO:0000244|PDB:1YKS}.
STRAND 1821 1825 {ECO:0000244|PDB:1YKS}.
STRAND 1834 1836 {ECO:0000244|PDB:1YKS}.
HELIX 1839 1842 {ECO:0000244|PDB:1YKS}.
STRAND 1847 1850 {ECO:0000244|PDB:1YKS}.
HELIX 1854 1866 {ECO:0000244|PDB:1YKS}.
STRAND 1871 1873 {ECO:0000244|PDB:1YKS}.
STRAND 1876 1878 {ECO:0000244|PDB:1YKS}.
STRAND 1892 1899 {ECO:0000244|PDB:1YKS}.
STRAND 1909 1913 {ECO:0000244|PDB:1YKS}.
STRAND 1916 1923 {ECO:0000244|PDB:1YKS}.
TURN 1924 1927 {ECO:0000244|PDB:1YKS}.
STRAND 1928 1936 {ECO:0000244|PDB:1YKS}.
HELIX 1939 1946 {ECO:0000244|PDB:1YKS}.
STRAND 1958 1962 {ECO:0000244|PDB:1YKS}.
HELIX 1974 1983 {ECO:0000244|PDB:1YKS}.
HELIX 1989 1991 {ECO:0000244|PDB:1YKS}.
HELIX 2000 2003 {ECO:0000244|PDB:1YKS}.
STRAND 2004 2006 {ECO:0000244|PDB:1YKS}.
TURN 2008 2011 {ECO:0000244|PDB:1YKS}.
HELIX 2015 2026 {ECO:0000244|PDB:1YKS}.
HELIX 2032 2040 {ECO:0000244|PDB:1YKS}.
HELIX 2049 2051 {ECO:0000244|PDB:1YKS}.
HELIX 2056 2058 {ECO:0000244|PDB:1YKS}.
STRAND 2063 2065 {ECO:0000244|PDB:5FFM}.
STRAND 2069 2071 {ECO:0000244|PDB:1YKS}.
STRAND 2077 2079 {ECO:0000244|PDB:1YKS}.
STRAND 2083 2086 {ECO:0000244|PDB:1YKS}.
HELIX 2087 2089 {ECO:0000244|PDB:1YKS}.
STRAND 2090 2092 {ECO:0000244|PDB:1YKS}.
HELIX 2093 2103 {ECO:0000244|PDB:1YKS}.
TURN 2104 2106 {ECO:0000244|PDB:1YKS}.
HELIX 2514 2524 {ECO:0000244|PDB:3EVF}.
HELIX 2527 2534 {ECO:0000244|PDB:3EVF}.
STRAND 2536 2541 {ECO:0000244|PDB:3EVF}.
HELIX 2544 2551 {ECO:0000244|PDB:3EVF}.
HELIX 2564 2573 {ECO:0000244|PDB:3EVF}.
STRAND 2581 2586 {ECO:0000244|PDB:3EVF}.
HELIX 2592 2598 {ECO:0000244|PDB:3EVF}.
STRAND 2603 2609 {ECO:0000244|PDB:3EVF}.
HELIX 2627 2629 {ECO:0000244|PDB:3EVF}.
STRAND 2630 2633 {ECO:0000244|PDB:3EVF}.
TURN 2638 2640 {ECO:0000244|PDB:3EVF}.
STRAND 2647 2651 {ECO:0000244|PDB:3EVF}.
HELIX 2660 2678 {ECO:0000244|PDB:3EVF}.
TURN 2679 2681 {ECO:0000244|PDB:3EVD}.
STRAND 2683 2690 {ECO:0000244|PDB:3EVF}.
HELIX 2695 2708 {ECO:0000244|PDB:3EVF}.
STRAND 2711 2713 {ECO:0000244|PDB:3EVF}.
STRAND 2725 2730 {ECO:0000244|PDB:3EVF}.
HELIX 2735 2751 {ECO:0000244|PDB:3EVF}.
STRAND 2757 2760 {ECO:0000244|PDB:3EVF}.
SEQUENCE 3411 AA; 379518 MW; 680E0FACD23DCFA6 CRC64;
MSGRKAQGKT LGVNMVRRGV RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF FLFNILTGKK
ITAHLKRLWK MLDPRQGLAV LRKVKRVVAS LMRGLSSRKR RSHDVLTVQF LILGMLLMTG
GVTLVRKNRW LLLNVTSEDL GKTFSVGTGN CTTNILEAKY WCPDSMEYNC PNLSPREEPD
DIDCWCYGVE NVRVAYGKCD SAGRSRRSRR AIDLPTHENH GLKTRQEKWM TGRMGERQLQ
KIERWFVRNP FFAVTALTIA YLVGSNMTQR VVIALLVLAV GPAYSAHCIG ITDRDFIEGV
HGGTWVSATL EQDKCVTVMA PDKPSLDISL ETVAIDRPAE VRKVCYNAVL THVKINDKCP
STGEAHLAEE NEGDNACKRT YSDRGWGNGC GLFGKGSIVA CAKFTCAKSM SLFEVDQTKI
QYVIRAQLHV GAKQENWNTD IKTLKFDALS GSQEVEFIGY GKATLECQVQ TAVDFGNSYI
AEMETESWIV DRQWAQDLTL PWQSGSGGVW REMHHLVEFE PPHAATIRVL ALGNQEGSLK
TALTGAMRVT KDTNDNNLYK LHGGHVSCRV KLSALTLKGT SYKICTDKMF FVKNPTDTGH
GTVVMQVKVS KGAPCRIPVI VADDLTAAIN KGILVTVNPI ASTNDDEVLI EVNPPFGDSY
IIVGRGDSRL TYQWHKEGSS IGKLFTQTMK GVERLAVMGD TAWDFSSAGG FFTSVGKGIH
TVFGSAFQGL FGGLNWITKV IMGAVLIWVG INTRNMTMSM SMILVGVIMM FLSLGVGADQ
GCAINFGKRE LKCGDGIFIF RDSDDWLNKY SYYPEDPVKL ASIVKASFEE GKCGLNSVDS
LEHEMWRSRA DEINAIFEEN EVDISVVVQD PKNVYQRGTH PFSRIRDGLQ YGWKTWGKNL
VFSPGRKNGS FIIDGKSRKE CPFSNRVWNS FQIEEFGTGV FTTRVYMDAV FEYTIDCDGS
ILGAAVNGKK SAHGSPTFWM GSHEVNGTWM IHTLEALDYK ECEWPLTHTI GTSVEESEMF
MPRSIGGPVS SHNHIPGYKV QTNGPWMQVP LEVKREACPG TSVIIDGNCD GRGKSTRSTT
DSGKVIPEWC CRSCTMPPVS FHGSDGCWYP MEIRPRKTHE SHLVRSWVTA GEIHAVPFGL
VSMMIAMEVV LRKRQGPKQM LVGGVVLLGA MLVGQVTLLD LLKLTVAVGL HFHEMNNGGD
AMYMALIAAF SIRPGLLIGF GLRTLWSPRE RLVLTLGAAM VEIALGGVMG GLWKYLNAVS
LCILTINAVA SRKASNTILP LMALLTPVTM AEVRLAAMFF CAVVIIGVLH QNFKDTSMQK
TIPLVALTLT SYLGLTQPFL GLCAFLATRI FGRRSIPVNE ALAAAGLVGV LAGLAFQEME
NFLGPIAVGG LLMMLVSVAG RVDGLELKKL GEVSWEEEAE ISGSSARYDV ALSEQGEFKL
LSEEKVPWDQ VVMTSLALVG AALHPFALLL VLAGWLFHVR GARRSGDVLW DIPTPKIIEE
CEHLEDGIYG IFQSTFLGAS QRGVGVAQGG VFHTMWHVTR GAFLVRNGKK LIPSWASVKE
DLVAYGGSWK LEGRWDGEEE VQLIAAVPGK NVVNVQTKPS LFKVRNGGEI GAVALDYPSG
TSGSPIVNRN GEVIGLYGNG ILVGDNSFVS AISQTEVKEE GKEELQEIPT MLKKGMTTVL
DFHPGAGKTR RFLPQILAEC ARRRLRTLVL APTRVVLSEM KEAFHGLDVK FHTQAFSAHG
SGREVIDAMC HATLTYRMLE PTRVVNWEVI IMDEAHFLDP ASIAARGWAA HRARANESAT
ILMTATPPGT SDEFPHSNGE IEDVQTDIPS EPWNTGHDWI LADKRPTAWF LPSIRAANVM
AASLRKAGKS VVVLNRKTFE REYPTIKQKK PDFILATDIA EMGANLCVER VLDCRTAFKP
VLVDEGRKVA IKGPLRISAS SAAQRRGRIG RNPNRDGDSY YYSEPTSENN AHHVCWLEAS
MLLDNMEVRG GMVAPLYGVE GTKTPVSPGE MRLRDDQRKV FRELVRNCDL PVWLSWQVAK
AGLKTNDRKW CFEGPEEHEI LNDSGETVKC RAPGGAKKPL RPRWCDERVS SDQSALSEFI
KFAEGRRGAA EVLVVLSELP DFLAKKGGEA MDTISVFLHS EEGSRAYRNA LSMMPEAMTI
VMLFILAGLL TSGMVIFFMS PKGISRMSMA MGTMAGCGYL MFLGGVKPTH ISYVMLIFFV
LMVVVIPEPG QQRSIQDNQV AYLIIGILTL VSAVAANELG MLEKTKEDLF GKKNLIPSSA
SPWSWPDLDL KPGAAWTVYV GIVTMLSPML HHWIKVEYGN LSLSGIAQSA SVLSFMDKGI
PFMKMNISVI MLLVSGWNSI TVMPLLCGIG CAMLHWSLIL PGIKAQQSKL AQRRVFHGVA
ENPVVDGNPT VDIEEAPEMP ALYEKKLALY LLLALSLASV AMCRTPFSLA EGIVLASAAL
GPLIEGNTSL LWNGPMAVSM TGVMRGNHYA FVGVMYNLWK MKTGRRGSAN GKTLGEVWKR
ELNLLDKRQF ELYKRTDIVE VDRDTARRHL AEGKVDTGVA VSRGTAKLRW FHERGYVKLE
GRVIDLGCGR GGWCYYAAAQ KEVSGVKGFT LGRDGHEKPM NVQSLGWNII TFKDKTDIHR
LEPVKCDTLL CDIGESSSSS VTEGERTVRV LDTVEKWLAC GVDNFCVKVL APYMPDVLEK
LELLQRRFGG TVIRNPLSRN STHEMYYVSG ARSNVTFTVN QTSRLLMRRM RRPTGKVTLE
ADVILPIGTR SVETDKGPLD KEAIEERVER IKSEYMTSWF YDNDNPYRTW HYCGSYVTKT
SGSAASMVNG VIKILTYPWD RIEEVTRMAM TDTTPFGQQR VFKEKVDTRA KDPPAGTRKI
MKVVNRWLFR HLAREKNPRL CTKEEFIAKV RSHAAIGAYL EEQEQWKTAN EAVQDPKFWE
LVDEERKLHQ QGRCRTCVYN MMGKREKKLS EFGKAKGSRA IWYMWLGARY LEFEALGFLN
EDHWASRENS GGGVEGIGLQ YLGYVIRDLA AMDGGGFYAD DTAGWDTRIT EADLDDEQEI
LNYMSPHHKK LAQAVMEMTY KNKVVKVLRP APGGKAYMDV ISRRDQRGSG QVVTYALNTI
TNLKVQLIRM AEAEMVIHHQ HVQDCDESVL TRLEAWLTEH GCDRLKRMAV SGDDCVVRPI
DDRFGLALSH LNAMSKVRKD ISEWQPSKGW NDWENVPFCS HHFHELQLKD GRRIVVPCRE
QDELIGRGRV SPGNGWMIKE TACLSKAYAN MWSLMYFHKR DMRLLSLAVS SAVPTSWVPQ
GRTTWSIHGK GEWMTTEDML EVWNRVWITN NPHMQDKTMV KKWRDVPYLT KRQDKLCGSL
IGMTNRATWA SHIHLVIHRI RTLIGQEKYT DYLTVMDRYS VDADLQLGEL I


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