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 POLG_DEN3S              Reviewed;        3390 AA.
Q6YMS4; Q6DLV0;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
22-NOV-2017, entry version 114.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Capsid protein C;
AltName: Full=Core protein;
Contains:
RecName: Full=Protein prM;
Contains:
RecName: Full=Peptide pr;
Contains:
RecName: Full=Small envelope protein M;
AltName: Full=Matrix protein;
Contains:
RecName: Full=Envelope protein E;
Contains:
RecName: Full=Non-structural protein 1;
Short=NS1;
Contains:
RecName: Full=Non-structural protein 2A;
Short=NS2A;
Contains:
RecName: Full=Serine protease subunit NS2B;
AltName: Full=Flavivirin protease NS2B regulatory subunit;
AltName: Full=Non-structural protein 2B;
Contains:
RecName: Full=Serine protease NS3;
EC=3.4.21.91;
EC=3.6.1.15 {ECO:0000250|UniProtKB:Q9Q6P4};
EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9Q6P4};
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, ECO:0000269|PubMed:26578813};
EC=2.1.1.57 {ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:26578813};
EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539, ECO:0000269|PubMed:24025331};
AltName: Full=Non-structural protein 5;
Name=pol;
Dengue virus type 3 (strain Sri Lanka/1266/2000) (DENV-3).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; Dengue virus group.
NCBI_TaxID=408692;
NCBI_TaxID=53540; Aedimorphus.
NCBI_TaxID=53539; Diceromyia.
NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=53541; Stegomyia.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=14605161; DOI=10.1128/JCM.41.11.5195-5198.2003;
Peyrefitte C.N., Couissinier-Paris P., Mercier-Perennec V.,
Bessaud M., Martial J., Kenane N., Durand J.-P.A., Tolou H.J.;
"Genetic characterization of newly reintroduced dengue virus type 3 in
Martinique (French West Indies).";
J. Clin. Microbiol. 41:5195-5198(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
Lim S.P., Ooi E.E., Vasudevan S.G.;
"Full length genomic sequence of a Dengue virus of serotype 3 from
Singapore.";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2762-3390 IN COMPLEX WITH
GTP AND ZINC.
PubMed=17301146; DOI=10.1128/JVI.02283-06;
Yap T.L., Xu T., Chen Y.L., Malet H., Egloff M.P., Canard B.,
Vasudevan S.G., Lescar J.;
"Crystal structure of the dengue virus RNA-dependent RNA polymerase
catalytic domain at 1.85-angstrom resolution.";
J. Virol. 81:4753-4765(2007).
[4]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2753-3390 IN COMPLEX WITH
ZINC, CATALYTIC ACTIVITY (RNA-DIRECTED RNA POLYMERASE NS5), AND
SUBUNIT (RNA-DIRECTED RNA POLYMERASE NS5).
PubMed=24025331; DOI=10.1074/JBC.M113.508606;
Lim S.P., Koh J.H., Seh C.C., Liew C.W., Davidson A.D., Chua L.S.,
Chandrasekaran R., Cornvik T.C., Shi P.Y., Lescar J.;
"A crystal structure of the dengue virus non-structural protein 5
(NS5) polymerase delineates interdomain amino acid residues that
enhance its thermostability and de novo initiation activities.";
J. Biol. Chem. 288:31105-31114(2013).
[5]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2496-3385, CATALYTIC
ACTIVITY (RNA-DIRECTED RNA POLYMERASE NS5), MUTAGENESIS OF ARG-2528;
LYS-2532; ARG-2547; LYS-2551; ARG-2574; GLU-2601; ASP-2636; LYS-2670;
ARG-2701 AND GLU-2706, AND ACTIVE SITE (RNA-DIRECTED RNA POLYMERASE
NS5).
PubMed=26578813; DOI=10.1073/pnas.1514978112;
Zhao Y., Soh T.S., Lim S.P., Chung K.Y., Swaminathan K.,
Vasudevan S.G., Shi P.Y., Lescar J., Luo D.;
"Molecular basis for specific viral RNA recognition and 2'-O-ribose
methylation by the dengue virus nonstructural protein 5 (NS5).";
Proc. Natl. Acad. Sci. U.S.A. 112:14834-14839(2015).
-!- FUNCTION: Capsid protein C: Plays a role in virus budding by
binding to the cell membrane and gathering the viral RNA into a
nucleocapsid that forms the core of a mature virus particle.
During virus entry, may induce genome penetration into the host
cytoplasm after hemifusion induced by the surface proteins. Can
migrate to the cell nucleus where it modulates host functions.
Overcomes the anti-viral effects of host EXOC1 by sequestering and
degrading the latter through the proteasome degradation pathway.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Capsid protein C: Inhibits RNA silencing by interfering
with host Dicer. {ECO:0000250|UniProtKB:P03314}.
-!- FUNCTION: Peptide pr: Prevents premature fusion activity of
envelope proteins in trans-Golgi by binding to envelope protein E
at pH6.0. After virion release in extracellular space, gets
dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Protein prM: Acts as a chaperone for envelope protein E
during intracellular virion assembly by masking and inactivating
envelope protein E fusion peptide. prM is the only viral peptide
matured by host furin in the trans-Golgi network probably to avoid
catastrophic activation of the viral fusion activity in acidic
Golgi compartment prior to virion release. prM-E cleavage is
inefficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Small envelope protein M: May play a role in virus
budding. Exerts cytotoxic effects by activating a mitochondrial
apoptotic pathway through M ectodomain. May display a viroporin
activity. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Envelope protein E: Binds to host cell surface receptor
and mediates fusion between viral and cellular membranes. Envelope
protein is synthesized in the endoplasmic reticulum in the form of
heterodimer with protein prM. They play a role in virion budding
in the ER, and the newly formed immature particle is covered with
60 spikes composed of heterodimer between precursor prM and
envelope protein E. The virion is transported to the Golgi
apparatus where the low pH causes dissociation of PrM-E
heterodimers and formation of E homodimers. prM-E cleavage is
inefficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 1: Involved in immune evasion,
pathogenesis and viral replication. Once cleaved off the
polyprotein, is targeted to three destinations: the viral
replication cycle, the plasma membrane and the extracellular
compartment. Essential for viral replication. Required for
formation of the replication complex and recruitment of other non-
structural proteins to the ER-derived membrane structures.
Excreted as a hexameric lipoparticle that plays a role against
host immune response. Antagonizing the complement function. Binds
to the host macrophages and dendritic cells. Inhibits signal
transduction originating from Toll-like receptor 3 (TLR3).
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- FUNCTION: Non-structural protein 1: Disrupts the host endothelial
glycocalyx layer of host pulmonary microvascular endothelial
cells, inducing degradation of sialic acid and shedding of heparan
sulfate proteoglycans. NS1 induces expression of sialidases,
heparanase, and activates cathepsin L, which activates heparanase
via enzymatic cleavage. These effects are probably linked to the
endothelial hyperpermeability observed in severe dengue disease.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 2A: Component of the viral RNA
replication complex that functions in virion assembly and
antagonizes the host immune response.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Serine protease subunit NS2B: Required cofactor for the
serine protease function of NS3. May have membrane-destabilizing
activity and form viroporins (By similarity).
{ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00859}.
-!- FUNCTION: Serine protease NS3: Displays three enzymatic
activities: serine protease, NTPase and RNA helicase. NS3 serine
protease, in association with NS2B, performs its autocleavage and
cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM,
NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA
helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.
{ECO:0000255|PROSITE-ProRule:PRU00860}.
-!- FUNCTION: Non-structural protein 4A: Regulates the ATPase activity
of the NS3 helicase activity. NS4A allows NS3 helicase to conserve
energy during unwinding. Plays a role in the inhibition of the
host innate immune response. Interacts with host MAVS and thereby
prevents the interaction between DDX58 and MAVS. In turn, IFN-beta
production is impaired. {ECO:0000250|UniProtKB:P17763,
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.
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- FUNCTION: RNA-directed RNA polymerase NS5: Replicates the viral
(+) and (-) RNA genome, and performs the capping of genomes in the
cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose
2'-O positions. Besides its role in RNA genome replication, also
prevents the establishment of cellular antiviral state by blocking
the interferon-alpha/beta (IFN-alpha/beta) signaling pathway.
Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing
activation of JAK-STAT signaling pathway.
{ECO:0000250|UniProtKB:P17763}.
-!- CATALYTIC ACTIVITY: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds
in which each of the Xaa can be either Arg or Lys and Yaa can be
either Ser or Ala.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539,
ECO:0000269|PubMed:24025331}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. {ECO:0000255|PROSITE-
ProRule:PRU00924, ECO:0000269|PubMed:26578813}.
-!- 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,
ECO:0000269|PubMed:26578813}.
-!- SUBUNIT: Capsid protein C: Homodimer. Interacts (via N-terminus)
with host EXOC1 (via C-terminus); this interaction results in
EXOC1 degradation through the proteasome degradation pathway (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 (By
similarity). Interacts with protein prM. Interacts with non-
structural protein 1 (By similarity). Non-structural protein 1:
Homodimer; Homohexamer when secreted (By similarity). Interacts
with envelope protein E (By similarity). Non-structural protein
2A: Interacts (via N-terminus) with serine protease NS3 (By
similarity). Non-structural protein 2B: Forms a heterodimer with
serine protease NS3 (By similarity). May form homooligomers (By
similarity). Serine protease NS3: Forms a heterodimer with NS2B.
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). Non-structural protein 4A: Interacts
with host MAVS; this interaction inhibits the synthesis of IFN-
beta (By similarity). Non-structural protein 4B: Interacts with
serine protease NS3. RNA-directed RNA polymerase NS5: Homodimer
(PubMed:24025331). Interacts with host STAT2; this interaction
inhibits the phosphorylation of the latter, and, when all viral
proteins are present (polyprotein), targets STAT2 for degradation.
Interacts with serine protease NS3. {ECO:0000250|UniProtKB:P17763,
ECO:0000269|PubMed:24025331}.
-!- SUBCELLULAR LOCATION: Capsid protein C: Virion
{ECO:0000250|UniProtKB:P17763}. Host nucleus
{ECO:0000250|UniProtKB:P17763}. Host cytoplasm
{ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear
region {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Peptide pr: Secreted
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO: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}. Host
mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-
associated vesicles hosting the replication complex. Interacts
with host MAVS in the mitochondrion-associated endoplasmic
reticulum membranes. {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, especially in the DENV 2, 3, 4 serotypes.
{ECO:0000250|UniProtKB:P17763}.
-!- DOMAIN: The transmembrane domains of the small envelope protein M
and envelope protein E contain an endoplasmic reticulum retention
signal. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Genome polyprotein: Specific enzymatic cleavages in vivo
yield mature proteins. Cleavages in the lumen of endoplasmic
reticulum are performed by host signal peptidase, whereas
cleavages in the cytoplasmic side are performed by serine protease
NS3. Signal cleavage at the 2K-4B site requires a prior NS3
protease-mediated cleavage at the 4A-2K site.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: Protein prM: Cleaved in post-Golgi vesicles by a host furin,
releasing the mature small envelope protein M, and peptide pr.
This cleavage is incomplete as up to 30% of viral particles still
carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Envelope protein E: N-glycosylated.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: Non-structural protein 1: N-glycosylated. The excreted form
is glycosylated and this is required for efficient secretion of
the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: RNA-directed RNA polymerase NS5: Sumoylation of RNA-directed
RNA polymerase NS5 increases NS5 protein stability allowing proper
viral RNA replication. {ECO:0000250|UniProtKB:P29990}.
-!- PTM: RNA-directed RNA polymerase NS5: Phosphorylated on serines
residues. This phosphorylation may trigger NS5 nuclear
localization. {ECO:0000250|UniProtKB:P17763}.
-!- SIMILARITY: In the N-terminal section; belongs to the class I-like
SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}.
-!- WEB RESOURCE: Name=Virus Pathogen Resource;
URL="http://www.viprbrc.org/brc/home.do?decorator=flavi_dengue";
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EMBL; AY099336; AAM51537.1; -; Genomic_RNA.
EMBL; AY662691; AAT75224.1; -; Genomic_RNA.
RefSeq; YP_001621843.1; NC_001475.2.
PDB; 2J7U; X-ray; 1.85 A; A=2762-3390.
PDB; 2J7W; X-ray; 2.60 A; A=2763-3390.
PDB; 3VWS; X-ray; 2.10 A; A=2762-3390.
PDB; 4C11; X-ray; 2.60 A; A/B=2753-3390.
PDB; 4HHJ; X-ray; 1.79 A; A=2762-3390.
PDB; 5DTO; X-ray; 2.60 A; A=2496-3385.
PDB; 5EIW; X-ray; 1.61 A; A/C=2491-2766.
PDB; 5F3T; X-ray; 2.05 A; A=2762-3390.
PDB; 5F3Z; X-ray; 2.00 A; A=2762-3390.
PDB; 5F41; X-ray; 2.00 A; A=2762-3390.
PDB; 5HMW; X-ray; 2.15 A; A=2762-3390.
PDB; 5HMX; X-ray; 2.40 A; A=2762-3390.
PDB; 5HMY; X-ray; 2.10 A; A=2762-3390.
PDB; 5HMZ; X-ray; 1.99 A; A=2762-3390.
PDB; 5HN0; X-ray; 2.05 A; A=2762-3390.
PDB; 5I3P; X-ray; 2.45 A; A=2762-3390.
PDB; 5I3Q; X-ray; 1.88 A; A=2762-3390.
PDB; 5IQ6; X-ray; 3.00 A; A=2763-3390.
PDB; 5JJR; X-ray; 1.99 A; A=2494-3385.
PDB; 5JJS; X-ray; 1.65 A; A=2494-3385.
PDBsum; 2J7U; -.
PDBsum; 2J7W; -.
PDBsum; 3VWS; -.
PDBsum; 4C11; -.
PDBsum; 4HHJ; -.
PDBsum; 5DTO; -.
PDBsum; 5EIW; -.
PDBsum; 5F3T; -.
PDBsum; 5F3Z; -.
PDBsum; 5F41; -.
PDBsum; 5HMW; -.
PDBsum; 5HMX; -.
PDBsum; 5HMY; -.
PDBsum; 5HMZ; -.
PDBsum; 5HN0; -.
PDBsum; 5I3P; -.
PDBsum; 5I3Q; -.
PDBsum; 5IQ6; -.
PDBsum; 5JJR; -.
PDBsum; 5JJS; -.
ProteinModelPortal; Q6YMS4; -.
SMR; Q6YMS4; -.
MEROPS; S07.001; -.
GeneID; 5075727; -.
KEGG; vg:5075727; -.
OrthoDB; VOG09000016; -.
BRENDA; 3.4.21.91; 9648.
PRO; PR:Q6YMS4; -.
Proteomes; UP000007537; Genome.
Proteomes; UP000096981; 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:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW.
GO; GO:0039574; P:suppression by virus of host TYK2 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd12149; Flavi_E_C; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 3.30.387.10; -; 1.
Gene3D; 3.30.67.10; -; 1.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR000069; Env_glycoprot_M_flavivir.
InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
InterPro; IPR001122; Flavi_capsidC.
InterPro; IPR037172; Flavi_capsidC_sf.
InterPro; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
InterPro; IPR001157; Flavi_NS1.
InterPro; IPR000752; Flavi_NS2A.
InterPro; IPR000487; Flavi_NS2B.
InterPro; IPR000404; Flavi_NS4A.
InterPro; IPR001528; Flavi_NS4B.
InterPro; IPR002535; Flavi_propep.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
InterPro; IPR013756; GlyE_cen_dom_subdom2.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR000208; RNA-dir_pol_flavivirus.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01003; Flavi_capsid; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF02832; Flavi_glycop_C; 1.
Pfam; PF00869; Flavi_glycoprot; 1.
Pfam; PF01004; Flavi_M; 1.
Pfam; PF00948; Flavi_NS1; 1.
Pfam; PF01005; Flavi_NS2A; 1.
Pfam; PF01002; Flavi_NS2B; 1.
Pfam; PF01350; Flavi_NS4A; 1.
Pfam; PF01349; Flavi_NS4B; 1.
Pfam; PF00972; Flavi_NS5; 1.
Pfam; PF01570; Flavi_propep; 1.
Pfam; PF01728; FtsJ; 1.
Pfam; PF00949; Peptidase_S7; 1.
PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF101257; SSF101257; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
TIGRFAMs; TIGR04240; flavi_E_stem; 1.
PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus; ATP-binding;
Capsid protein; Clathrin-mediated endocytosis of virus by host;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
Host cytoplasm; Host endoplasmic reticulum; Host membrane;
Host mitochondrion; 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 MAVS by virus;
Inhibition of host RLR pathway by virus;
Inhibition of host STAT2 by virus; Inhibition of host TYK2 by virus;
Ion channel; Ion transport; Membrane; Metal-binding;
Methyltransferase; mRNA capping; mRNA processing;
Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
Phosphoprotein; Protease; RNA-binding; RNA-directed RNA polymerase;
S-adenosyl-L-methionine; Secreted; Serine protease;
Suppressor of RNA silencing; Transcription; Transcription regulation;
Transferase; Transmembrane; Transmembrane helix; Transport;
Ubl conjugation; Viral attachment to host cell;
Viral envelope protein; Viral immunoevasion; Viral ion channel;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus endocytosis by host; Virus entry into host cell; Zinc.
CHAIN 1 3390 Genome polyprotein.
/FTId=PRO_0000405225.
CHAIN 1 100 Capsid protein C.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000268088.
PROPEP 101 114 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000268089.
CHAIN 115 280 Protein prM.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000268090.
CHAIN 115 205 Peptide pr.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000268091.
CHAIN 206 280 Small envelope protein M.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000268092.
CHAIN 281 773 Envelope protein E.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000268093.
CHAIN 774 1125 Non-structural protein 1.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000268094.
CHAIN 1126 1343 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000268095.
CHAIN 1344 1473 Serine protease subunit NS2B.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000268097.
CHAIN 1474 2092 Serine protease NS3.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000268098.
CHAIN 2093 2219 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000268099.
PEPTIDE 2220 2242 Peptide 2k.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000268100.
CHAIN 2243 2490 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000268101.
CHAIN 2491 3390 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000268102.
TOPO_DOM 1 100 Cytoplasmic. {ECO:0000255}.
TRANSMEM 101 120 Helical. {ECO:0000255}.
TOPO_DOM 121 243 Extracellular. {ECO:0000255}.
TRANSMEM 244 264 Helical. {ECO:0000255}.
TOPO_DOM 265 265 Cytoplasmic. {ECO:0000255}.
TRANSMEM 266 280 Helical. {ECO:0000255}.
TOPO_DOM 281 723 Extracellular. {ECO:0000255}.
TRANSMEM 724 744 Helical. {ECO:0000255}.
TOPO_DOM 745 750 Cytoplasmic. {ECO:0000255}.
TRANSMEM 751 771 Helical. {ECO:0000255}.
TOPO_DOM 772 1193 Extracellular. {ECO:0000255}.
TRANSMEM 1194 1218 Helical. {ECO:0000255}.
TOPO_DOM 1219 1224 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1225 1243 Helical. {ECO:0000255}.
TOPO_DOM 1244 1267 Lumenal. {ECO:0000255}.
TRANSMEM 1268 1288 Helical. {ECO:0000255}.
TOPO_DOM 1289 1289 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1290 1308 Helical. {ECO:0000255}.
TOPO_DOM 1309 1315 Lumenal. {ECO:0000255}.
TRANSMEM 1316 1336 Helical. {ECO:0000255}.
TOPO_DOM 1337 1344 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1345 1365 Helical. {ECO:0000255}.
TOPO_DOM 1366 1368 Lumenal. {ECO:0000255}.
TRANSMEM 1369 1389 Helical. {ECO:0000255}.
TOPO_DOM 1390 1443 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1444 1464 Helical. {ECO:0000255}.
TOPO_DOM 1465 2146 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2147 2167 Helical. {ECO:0000255}.
TOPO_DOM 2168 2169 Lumenal. {ECO:0000255}.
INTRAMEM 2170 2190 Helical. {ECO:0000255}.
TOPO_DOM 2191 2191 Lumenal. {ECO:0000255}.
TRANSMEM 2192 2212 Helical. {ECO:0000255}.
TOPO_DOM 2213 2227 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2228 2248 Helical; Note=Signal for NS4B.
{ECO:0000255}.
TOPO_DOM 2249 2273 Lumenal. {ECO:0000255}.
INTRAMEM 2274 2294 Helical. {ECO:0000255}.
TOPO_DOM 2295 2305 Lumenal. {ECO:0000255}.
INTRAMEM 2306 2326 Helical. {ECO:0000255}.
TOPO_DOM 2327 2346 Lumenal. {ECO:0000255}.
TRANSMEM 2347 2367 Helical. {ECO:0000255}.
TOPO_DOM 2368 2412 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2413 2433 Helical. {ECO:0000255}.
TOPO_DOM 2434 2458 Lumenal. {ECO:0000255}.
TRANSMEM 2459 2479 Helical. {ECO:0000255}.
TOPO_DOM 2480 3390 Cytoplasmic. {ECO:0000255}.
DOMAIN 1474 1651 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1654 1810 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1820 1986 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2492 2753 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3018 3168 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1667 1674 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 1 15 Interaction with host EXOC1.
{ECO:0000250|UniProtKB:P17763}.
REGION 37 72 Hydrophobic; homodimerization of capsid
protein C.
{ECO:0000250|UniProtKB:P29990}.
REGION 378 391 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
REGION 1396 1435 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
REGION 1658 1661 Important for RNA-binding.
{ECO:0000250|UniProtKB:P14340}.
MOTIF 1758 1761 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 2567 2570 SUMO-interacting motif.
{ECO:0000250|UniProtKB:P29990}.
ACT_SITE 1524 1524 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1548 1548 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1608 1608 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 2551 2551 For 2'-O-MTase activity.
{ECO:0000269|PubMed:26578813}.
ACT_SITE 2636 2636 For 2'-O-MTase activity.
{ECO:0000269|PubMed:26578813}.
ACT_SITE 2670 2670 For 2'-O-MTase activity.
{ECO:0000269|PubMed:26578813}.
ACT_SITE 2706 2706 For 2'-O-MTase activity.
{ECO:0000269|PubMed:26578813}.
METAL 2927 2927 Zinc 1. {ECO:0000269|PubMed:17301146}.
METAL 2931 2931 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:17301146}.
METAL 2936 2936 Zinc 1. {ECO:0000269|PubMed:17301146}.
METAL 2939 2939 Zinc 1. {ECO:0000269|PubMed:17301146}.
METAL 3202 3202 Zinc 2; via tele nitrogen.
{ECO:0000269|PubMed:17301146}.
METAL 3218 3218 Zinc 2. {ECO:0000269|PubMed:17301146}.
METAL 3337 3337 Zinc 2. {ECO:0000269|PubMed:17301146}.
BINDING 2504 2504 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2507 2507 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2508 2508 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2510 2510 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2519 2519 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2546 2546 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2576 2576 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2577 2577 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2594 2594 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2595 2595 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2621 2621 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2622 2622 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2640 2640 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2701 2701 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2703 2703 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2708 2708 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 100 101 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P29990}.
SITE 114 115 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 205 206 Cleavage; by host furin.
{ECO:0000250|UniProtKB:P29990,
ECO:0000255}.
SITE 280 281 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 773 774 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 1125 1126 Cleavage; by host.
{ECO:0000250|UniProtKB:P29990}.
SITE 1343 1344 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P29990}.
SITE 1473 1474 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P29990}.
SITE 1931 1931 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 1934 1934 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 2092 2093 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P29990}.
SITE 2219 2220 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P29990}.
SITE 2242 2243 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 2490 2491 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P29990}.
SITE 2515 2515 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2551 2551 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2636 2636 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2637 2637 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2670 2670 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2706 2706 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
MOD_RES 2546 2546 Phosphoserine.
{ECO:0000250|UniProtKB:P03314}.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 347 347 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 433 433 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 903 903 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 980 980 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1132 1132 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1188 1188 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2300 2300 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2304 2304 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2456 2456 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 283 310 {ECO:0000250|UniProtKB:P17763}.
DISULFID 340 401 {ECO:0000250|UniProtKB:P17763}.
DISULFID 354 385 {ECO:0000250|UniProtKB:P17763}.
DISULFID 372 396 {ECO:0000250|UniProtKB:P17763}.
DISULFID 463 563 {ECO:0000250|UniProtKB:P17763}.
DISULFID 580 611 {ECO:0000250|UniProtKB:P17763}.
DISULFID 777 788 {ECO:0000250|UniProtKB:P17763}.
DISULFID 828 916 {ECO:0000250|UniProtKB:P17763}.
DISULFID 952 996 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1053 1102 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1064 1086 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1085 1089 {ECO:0000250|UniProtKB:P17763}.
VARIANT 97 97 Q -> K.
VARIANT 684 684 E -> A.
VARIANT 867 867 L -> I.
VARIANT 1006 1006 T -> S.
VARIANT 1148 1148 L -> M.
VARIANT 1252 1252 V -> I.
VARIANT 1400 1400 P -> A.
VARIANT 1585 1585 T -> M.
VARIANT 1871 1871 T -> S.
VARIANT 2063 2063 K -> R.
VARIANT 2128 2128 D -> H.
VARIANT 2239 2239 T -> I.
VARIANT 2399 2399 S -> P.
VARIANT 2402 2402 F -> Y.
VARIANT 2856 2856 M -> L.
VARIANT 2862 2862 A -> V.
VARIANT 2864 2864 E -> G.
VARIANT 2970 2970 A -> V.
VARIANT 3093 3093 L -> V.
MUTAGEN 2528 2528 R->A: 90% loss of 2'-O-MTase activity.
{ECO:0000269|PubMed:26578813}.
MUTAGEN 2532 2532 K->A: 25% loss of 2'-O-MTase activity.
{ECO:0000269|PubMed:26578813}.
MUTAGEN 2547 2547 R->A: Complete loss of 2'-O-MTase
activity. {ECO:0000269|PubMed:26578813}.
MUTAGEN 2551 2551 K->A: Complete loss of 2'-O-MTase
activity. {ECO:0000269|PubMed:26578813}.
MUTAGEN 2574 2574 R->A: 40% loss of 2'-O-MTase activity.
{ECO:0000269|PubMed:26578813}.
MUTAGEN 2601 2601 E->R: Complete loss of 2'-O-MTase
activity. Decreased thermostability both
in the presence and absence of the RNA
ligand. {ECO:0000269|PubMed:26578813}.
MUTAGEN 2636 2636 D->A: Complete loss of 2'-O-MTase
activity. {ECO:0000269|PubMed:26578813}.
MUTAGEN 2670 2670 K->A: Complete loss of 2'-O-MTase
activity. {ECO:0000269|PubMed:26578813}.
MUTAGEN 2701 2701 R->A: 98% loss of 2'-O-MTase activity.
{ECO:0000269|PubMed:26578813}.
MUTAGEN 2706 2706 E->A: Complete loss of 2'-O-MTase
activity. {ECO:0000269|PubMed:26578813}.
HELIX 2499 2509 {ECO:0000244|PDB:5EIW}.
HELIX 2512 2519 {ECO:0000244|PDB:5EIW}.
TURN 2520 2522 {ECO:0000244|PDB:5EIW}.
STRAND 2524 2527 {ECO:0000244|PDB:5EIW}.
HELIX 2529 2536 {ECO:0000244|PDB:5EIW}.
HELIX 2548 2557 {ECO:0000244|PDB:5EIW}.
STRAND 2565 2570 {ECO:0000244|PDB:5EIW}.
HELIX 2576 2581 {ECO:0000244|PDB:5EIW}.
STRAND 2587 2593 {ECO:0000244|PDB:5EIW}.
HELIX 2611 2613 {ECO:0000244|PDB:5EIW}.
STRAND 2614 2617 {ECO:0000244|PDB:5EIW}.
HELIX 2622 2624 {ECO:0000244|PDB:5EIW}.
STRAND 2631 2635 {ECO:0000244|PDB:5EIW}.
HELIX 2644 2658 {ECO:0000244|PDB:5EIW}.
HELIX 2659 2661 {ECO:0000244|PDB:5EIW}.
STRAND 2666 2672 {ECO:0000244|PDB:5EIW}.
HELIX 2677 2690 {ECO:0000244|PDB:5EIW}.
STRAND 2693 2695 {ECO:0000244|PDB:5EIW}.
STRAND 2707 2712 {ECO:0000244|PDB:5EIW}.
HELIX 2717 2730 {ECO:0000244|PDB:5EIW}.
STRAND 2733 2735 {ECO:0000244|PDB:5EIW}.
STRAND 2740 2743 {ECO:0000244|PDB:5EIW}.
HELIX 2754 2756 {ECO:0000244|PDB:5JJS}.
HELIX 2763 2776 {ECO:0000244|PDB:5JJS}.
TURN 2777 2780 {ECO:0000244|PDB:5JJS}.
STRAND 2790 2800 {ECO:0000244|PDB:5JJS}.
HELIX 2812 2816 {ECO:0000244|PDB:5JJS}.
HELIX 2819 2823 {ECO:0000244|PDB:5JJS}.
HELIX 2825 2830 {ECO:0000244|PDB:5JJS}.
HELIX 2837 2847 {ECO:0000244|PDB:5JJS}.
HELIX 2857 2874 {ECO:0000244|PDB:5JJS}.
TURN 2875 2877 {ECO:0000244|PDB:5IQ6}.
HELIX 2885 2893 {ECO:0000244|PDB:5JJS}.
HELIX 2909 2916 {ECO:0000244|PDB:5JJS}.
HELIX 2918 2932 {ECO:0000244|PDB:5JJS}.
STRAND 2941 2944 {ECO:0000244|PDB:4HHJ}.
HELIX 2961 2978 {ECO:0000244|PDB:5JJS}.
HELIX 2980 2983 {ECO:0000244|PDB:5JJS}.
TURN 2984 2987 {ECO:0000244|PDB:5JJS}.
HELIX 2989 2992 {ECO:0000244|PDB:5JJS}.
STRAND 2993 2995 {ECO:0000244|PDB:5JJS}.
TURN 2997 2999 {ECO:0000244|PDB:5JJS}.
HELIX 3001 3012 {ECO:0000244|PDB:5JJS}.
STRAND 3014 3017 {ECO:0000244|PDB:4HHJ}.
HELIX 3027 3030 {ECO:0000244|PDB:5JJS}.
HELIX 3033 3039 {ECO:0000244|PDB:5JJS}.
HELIX 3040 3045 {ECO:0000244|PDB:5JJS}.
HELIX 3048 3060 {ECO:0000244|PDB:5JJS}.
STRAND 3063 3073 {ECO:0000244|PDB:5JJS}.
STRAND 3076 3087 {ECO:0000244|PDB:5JJS}.
STRAND 3090 3092 {ECO:0000244|PDB:5HMZ}.
HELIX 3095 3114 {ECO:0000244|PDB:5JJS}.
HELIX 3120 3124 {ECO:0000244|PDB:5JJS}.
HELIX 3131 3145 {ECO:0000244|PDB:5JJS}.
STRAND 3148 3151 {ECO:0000244|PDB:5JJS}.
STRAND 3154 3157 {ECO:0000244|PDB:5JJS}.
HELIX 3162 3166 {ECO:0000244|PDB:5JJS}.
HELIX 3169 3173 {ECO:0000244|PDB:5JJS}.
STRAND 3178 3181 {ECO:0000244|PDB:5F41}.
STRAND 3190 3192 {ECO:0000244|PDB:5JJS}.
HELIX 3193 3195 {ECO:0000244|PDB:5JJS}.
STRAND 3201 3207 {ECO:0000244|PDB:5JJS}.
STRAND 3213 3218 {ECO:0000244|PDB:5JJS}.
HELIX 3221 3228 {ECO:0000244|PDB:5JJS}.
STRAND 3230 3234 {ECO:0000244|PDB:4HHJ}.
HELIX 3238 3255 {ECO:0000244|PDB:5JJS}.
HELIX 3260 3272 {ECO:0000244|PDB:5JJS}.
STRAND 3294 3297 {ECO:0000244|PDB:5JJS}.
HELIX 3299 3307 {ECO:0000244|PDB:5JJS}.
TURN 3308 3310 {ECO:0000244|PDB:5F41}.
HELIX 3323 3325 {ECO:0000244|PDB:5JJS}.
HELIX 3331 3336 {ECO:0000244|PDB:5JJS}.
HELIX 3344 3364 {ECO:0000244|PDB:5JJS}.
HELIX 3373 3375 {ECO:0000244|PDB:5HMY}.
SEQUENCE 3390 AA; 377923 MW; 14C0E2C0C9189CCB CRC64;
MNNQRKKTGK PSINMLKRVR NRVSTGSQLA KRFSKGLLNG QGPMKLVMAF IAFLRFLAIP
PTAGVLARWG TFKKSGAIKV LKGFKKEISN MLSIINQRKK TSLCLMMILP AALAFHLTSR
DGEPRMIVGK NERGKSLLFK TASGINMCTL IAMDLGEMCD DTVTYKCPHI TEVEPEDIDC
WCNLTSTWVT YGTCNQAGEH RRDKRSVALA PHVGMGLDTR TQTWMSAEGA WRQVEKVETW
ALRHPGFTIL ALFLAHYIGT SLTQKVVIFI LLMLVTPSMT MRCVGVGNRD FVEGLSGATW
VDVVLEHGGC VTTMAKNKPT LDIELQKTEA TQLATLRKLC IEGKITNITT DSRCPTQGEA
VLPEEQDQNY VCKHTYVDRG WGNGCGLFGK GSLVTCAKFQ CLEPIEGKVV QYENLKYTVI
ITVHTGDQHQ VGNETQGVTA EITPQASTTE AILPEYGTLG LECSPRTGLD FNEMILLTMK
NKAWMVHRQW FFDLPLPWAS GATTETPTWN RKELLVTFKN AHAKKQEVVV LGSQEGAMHT
ALTGATEIQN SGGTSIFAGH LKCRLKMDKL ELKGMSYAMC TNTFVLKKEV SETQHGTILI
KVEYKGEDAP CKIPFSTEDG QGKAHNGRLI TANPVVTKKE EPVNIEAEPP FGESNIVIGI
GDNALKINWY KKGSSIGKMF EATERGARRM AILGDTAWDF GSVGGVLNSL GKMVHQIFGS
AYTALFSGVS WVMKIGIGVL LTWIGLNSKN TSMSFSCIAI GIITLYLGAV VQADMGCVIN
WKGKELKCGS GIFVTNEVHT WTEQYKFQAD SPKRLATAIA GAWENGVCGI RSTTRMENLL
WKQIANELNY ILWENNIKLT VVVGDTLGVL EQGKRTLTPQ PMELKYSWKT WGKAKIVTAE
TQNSSFIIDG PNTPECPSAS RAWNVWEVED YGFGVFTTNI WLKLREVYTQ LCDHRLMSAA
VKDERAVHAD MGYWIESQKN GSWKLEKASL IEVKTCTWPK SHTLWTNGVL ESDMIIPKSL
AGPISQHNYR PGYHTQTAGP WHLGKLELDF NYCEGTTVVI TESCGTRGPS LRTTTVSGKL
IHEWCCRSCT LPPLRYMGED GCWYGMEIRP ISEKEENMVK SLVSAGSGKV DNFTMGVLCL
AILFEEVLRG KFGKKHMIAG VFFTFVLLLS GQITWRDMAH TLIMIGSNAS DRMGMGVTYL
ALIATFKIQP FLALGFFLRK LTSRENLLLG VGLAMATTLQ LPEDIEQMAN GVALGLMALK
LITQFETYQL WTALVSLTCS NTIFTLTVAW RTATLILAGV SLLPVCQSSS MRKTDWLPMT
VAAMGVPPLP LFIFSLKDTL KRRSWPLNEG VMAVGLVSIL ASSLLRNDVP MAGPLVAGGL
LIACYVITGT SADLTVEKAP DVTWEEEAEQ TGVSHNLMIT VDDDGTMRIK DDETENILTV
LLKTALLIVS GIFPYSIPAT LLVWHTWQKQ TQRSGVLWDV PSPPETQKAE LEEGVYRIKQ
QGIFGKTQVG VGVQKEGVFH TMWHVTRGAV LTHNGKRLEP NWASVKKDLI SYGGGWRLSA
QWQKGEEVQV IAVEPGKNPK NFQTTPGTFQ TTTGEIGAIA LDFKPGTSGS PIINREGKVV
GLYGNGVVTK NGGYVSGIAQ TNAEPDGPTP ELEEEMFKKR NLTIMDLHPG SGKTRKYLPA
IVREAIKRRL RTLILAPTRV VAAEMEEALK GLPIRYQTTA TKSEHTGREI VDLMCHATFT
MRLLSPVRVP NYNLIIMDEA HFTDPASIAA RGYISTRVGM GEAAAIFMTA TPPGTADAFP
QSNAPIQDEE RDIPERSWNS GNEWITDFAG KTVWFVPSIK AGNDIANCLR KNGKKVIQLS
RKTFDTEYQK TKLNDWDFVV TTDISEMGAN FKADRVIDPR RCLKPVILTD GPERVILAGP
MPVTAASAAQ RRGRVGRNPQ KENDQYIFTG QPLNNDEDHA HWTEAKMLLD NINTPEGIIP
ALFEPEREKS AAIDGEYRLK GESRKTFVEL MRRGDLPVWL AHKVASEGIK YTDRKWCFDG
QRNNQILEEN MDVEIWTKEG EKKKLRPRWL DARTYSDPLA LKEFKDFAAG RKSIALDLVT
EIGRVPSHLA HRTRNALDNL VMLHTSEDGG RAYRHAVEEL PETMETLLLL GLMILLTGGA
MLFLISGKGI GKTSIGLICV IASSGMLWMA EVPLQWIASA IVLEFFMMVL LIPEPEKQRT
PQDNQLAYVV IGILTLAATI AANEMGLLET TKRDLGMSKE PGVVSPTSYL DVDLHPASAW
TLYAVATTVI TPMLRHTIEN STANVSLAAI ANQAVVLMGL DKGWPISKMD LGVPLLALGC
YSQVNPLTLT AAVLLLITHY AIIGPGLQAK ATREAQKRTA AGIMKNPTVD GIMTIDLDSV
IFDSKFEKQL GQVMLLVLCA VQLLLMRTSW ALCEALTLAT GPITTLWEGS PGKFWNTTIA
VSMANIFRGS YLAGAGLAFS IMKSVGTGKR GTGSQGETLG EKWKKKLNQL SRKEFDLYKK
SGITEVDRTE AKEGLKRGET THHAVSRGSA KLQWFVERNM VVPEGRVIDL GCGRGGWSYY
CAGLKKVTEV RGYTKGGPGH EEPVPMSTYG WNIVKLMSGK DVFYLPPEKC DTLLCDIGES
SPSPTVEESR TIRVLKMVEP WLKNNQFCIK VLNPYMPTVI EHLERLQRKH GGMLVRNPLS
RNSTHEMYWI SNGTGNIVSS VNMVSRLLLN RFTMTHRRPT IEKDVDLGAG TRHVNAEPET
PNMDVIGERI KRIKEEHNST WHYDDENPYK TWAYHGSYEV KATGSASSMI NGVVKLLTKP
WDVVPMVTQM AMTDTTPFGQ QRVFKEKVDT RTPRPMPGTR KAMEITAEWL WRTLGRNKRP
RLCTREEFTK KVRTNAAMGA VFTEENQWDS AKAAVEDEEF WKLVDREREL HKLGKCGSCV
YNMMGKREKK LGEFGKAKGS RAIWYMWLGA RYLEFEALGF LNEDHWFSRE NSYSGVEGEG
LHKLGYILRD ISKIPGGAMY ADDTAGWDTR ITEDDLHNEE KIIQQMDPEH RQLANAIFKL
TYQNKVVKVQ RPTPTGTVMD IISRKDQRGS GQLGTYGLNT FTNMEAQLVR QMEGEGVLTK
ADLENPHLLE KKITQWLETK GVERLKRMAI SGDDCVVKPI DDRFANALLA LNDMGKVRKD
IPQWQPSKGW HDWQQVPFCS HHFHELIMKD GRKLVVPCRP QDELIGRARI SQGAGWSLRE
TACLGKAYAQ MWSLMYFHRR DLRLASNAIC SAVPVHWVPT SRTTWSIHAH HQWMTTEDML
TVWNRVWIEE NPWMEDKTPV TTWENVPYLG KREDQWCGSL IGLTSRATWA QNIPTAIQQV
RSLIGNEEFL DYMPSMKRFR KEEESEGAIW


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