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Database: UniProt
Entry: Q58HT7
LinkDB: Q58HT7
Original site: Q58HT7 
ID   POLG_DEN4P              Reviewed;        3387 AA.
AC   Q58HT7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   11-DEC-2019, entry version 121.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Capsid protein C;
DE     AltName: Full=Core protein;
DE   Contains:
DE     RecName: Full=Protein prM;
DE   Contains:
DE     RecName: Full=Peptide pr;
DE   Contains:
DE     RecName: Full=Small envelope protein M;
DE     AltName: Full=Matrix protein;
DE   Contains:
DE     RecName: Full=Envelope protein E;
DE   Contains:
DE     RecName: Full=Non-structural protein 1;
DE              Short=NS1;
DE   Contains:
DE     RecName: Full=Non-structural protein 2A;
DE              Short=NS2A;
DE   Contains:
DE     RecName: Full=Serine protease subunit NS2B;
DE     AltName: Full=Flavivirin protease NS2B regulatory subunit;
DE     AltName: Full=Non-structural protein 2B;
DE   Contains:
DE     RecName: Full=Serine protease NS3;
DE              EC=3.4.21.91;
DE              EC=3.6.1.15 {ECO:0000250|UniProtKB:Q9Q6P4};
DE              EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9Q6P4};
DE     AltName: Full=Flavivirin protease NS3 catalytic subunit;
DE     AltName: Full=Non-structural protein 3;
DE   Contains:
DE     RecName: Full=Non-structural protein 4A;
DE              Short=NS4A;
DE   Contains:
DE     RecName: Full=Peptide 2k;
DE   Contains:
DE     RecName: Full=Non-structural protein 4B;
DE              Short=NS4B;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase NS5;
DE              EC=2.1.1.56 {ECO:0000255|PROSITE-ProRule:PRU00924};
DE              EC=2.1.1.57 {ECO:0000255|PROSITE-ProRule:PRU00924};
DE              EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE     AltName: Full=Non-structural protein 5;
OS   Dengue virus type 4 (strain Philippines/H241/1956) (DENV-4).
OC   Viruses; Riboviria; Flaviviridae; Flavivirus.
OX   NCBI_TaxID=408686;
OH   NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OH   NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OH   NCBI_TaxID=188700; Aedes polynesiensis (Polynesian tiger mosquito).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Yip A., Schreiber M., Liu W., Khoo C.A., Wong C., Hibberd M., Vasudevan S.;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding
CC       to the cell membrane and gathering the viral RNA into a nucleocapsid
CC       that forms the core of a mature virus particle. During virus entry, may
CC       induce genome penetration into the host cytoplasm after hemifusion
CC       induced by the surface proteins. Can migrate to the cell nucleus where
CC       it modulates host functions. Overcomes the anti-viral effects of host
CC       EXOC1 by sequestering and degrading the latter through the proteasome
CC       degradation pathway. {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering
CC       with host Dicer. {ECO:0000250|UniProtKB:P03314}.
CC   -!- FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope
CC       proteins in trans-Golgi by binding to envelope protein E at pH6.0.
CC       After virion release in extracellular space, gets dissociated from E
CC       dimers. {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Protein prM]: Acts as a chaperone for envelope protein E
CC       during intracellular virion assembly by masking and inactivating
CC       envelope protein E fusion peptide. prM is the only viral peptide
CC       matured by host furin in the trans-Golgi network probably to avoid
CC       catastrophic activation of the viral fusion activity in acidic Golgi
CC       compartment prior to virion release. prM-E cleavage is inefficient, and
CC       many virions are only partially matured. These uncleaved prM would play
CC       a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Small envelope protein M]: May play a role in virus budding.
CC       Exerts cytotoxic effects by activating a mitochondrial apoptotic
CC       pathway through M ectodomain. May display a viroporin activity.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and
CC       mediates fusion between viral and cellular membranes. Envelope protein
CC       is synthesized in the endoplasmic reticulum in the form of heterodimer
CC       with protein prM. They play a role in virion budding in the ER, and the
CC       newly formed immature particle is covered with 60 spikes composed of
CC       heterodimer between precursor prM and envelope protein E. The virion is
CC       transported to the Golgi apparatus where the low pH causes dissociation
CC       of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is
CC       inefficient, and many virions are only partially matured. These
CC       uncleaved prM would play a role in immune evasion.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Non-structural protein 1]: Involved in immune evasion,
CC       pathogenesis and viral replication. Once cleaved off the polyprotein,
CC       is targeted to three destinations: the viral replication cycle, the
CC       plasma membrane and the extracellular compartment. Essential for viral
CC       replication. Required for formation of the replication complex and
CC       recruitment of other non-structural proteins to the ER-derived membrane
CC       structures. Excreted as a hexameric lipoparticle that plays a role
CC       against host immune response. Antagonizing the complement function.
CC       Binds to the host macrophages and dendritic cells. Inhibits signal
CC       transduction originating from Toll-like receptor 3 (TLR3).
CC       {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- FUNCTION: [Non-structural protein 1]: Disrupts the host endothelial
CC       glycocalyx layer of host pulmonary microvascular endothelial cells,
CC       inducing degradation of sialic acid and shedding of heparan sulfate
CC       proteoglycans. NS1 induces expression of sialidases, heparanase, and
CC       activates cathepsin L, which activates heparanase via enzymatic
CC       cleavage. These effects are probably linked to the endothelial
CC       hyperpermeability observed in severe dengue disease.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Non-structural protein 2A]: Component of the viral RNA
CC       replication complex that functions in virion assembly and antagonizes
CC       the host immune response. {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the
CC       serine protease function of NS3. May have membrane-destabilizing
CC       activity and form viroporins (By similarity).
CC       {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}.
CC   -!- FUNCTION: [Serine protease NS3]: Displays three enzymatic activities:
CC       serine protease, NTPase and RNA helicase. NS3 serine protease, in
CC       association with NS2B, performs its autocleavage and cleaves the
CC       polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-
CC       NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and
CC       unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}.
CC   -!- FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of
CC       the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy
CC       during unwinding. Plays a role in the inhibition of the host innate
CC       immune response. Interacts with host MAVS and thereby prevents the
CC       interaction between DDX58 and MAVS. In turn, IFN-beta production is
CC       impaired. {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is
CC       required for the interferon antagonism activity of the latter.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-
CC       derived membrane vesicles where the viral replication takes place.
CC       Inhibits interferon (IFN)-induced host STAT1 phosphorylation and
CC       nuclear translocation, thereby preventing the establishment of cellular
CC       antiviral state by blocking the IFN-alpha/beta pathway.
CC       {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+)
CC       and (-) RNA genome, and performs the capping of genomes in the
CC       cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O
CC       positions. Besides its role in RNA genome replication, also prevents
CC       the establishment of cellular antiviral state by blocking the
CC       interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host
CC       TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-
CC       STAT signaling pathway. {ECO:0000250|UniProtKB:P17763}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of
CC         the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.;
CC         EC=3.4.21.91;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
CC         EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-guanosine in mRNA + S-
CC         adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-guanosine in mRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:60856, Rhea:RHEA-COMP:15681, Rhea:RHEA-COMP:15683,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143971,
CC         ChEBI:CHEBI:143975; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00924};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-adenosine in mRNA + S-
CC         adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-adenosine in mRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:60852, Rhea:RHEA-COMP:15680, Rhea:RHEA-COMP:15682,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143973,
CC         ChEBI:CHEBI:143974; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00924};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-guanosine in
CC         mRNA + S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-
CC         triphosphoguanosine)-(2'-O-methyl-guanosine) in mRNA + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:60864, Rhea:RHEA-COMP:15683,
CC         Rhea:RHEA-COMP:15685, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:143975, ChEBI:CHEBI:143977;
CC         EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-adenosine in
CC         mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-(2'-O-methyl-adenosine) in mRNA + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:60860, Rhea:RHEA-COMP:15682,
CC         Rhea:RHEA-COMP:15684, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:143974, ChEBI:CHEBI:143976;
CC         EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
CC   -!- SUBUNIT: Capsid protein C: Homodimer. Interacts (via N-terminus) with
CC       host EXOC1 (via C-terminus); this interaction results in EXOC1
CC       degradation through the proteasome degradation pathway. Protein prM:
CC       Forms heterodimers with envelope protein E in the endoplasmic reticulum
CC       and Golgi. Envelope protein E: Homodimer; in the endoplasmic reticulum
CC       and Golgi. Interacts with protein prM. Interacts with non-structural
CC       protein 1. Non-structural protein 1: Homodimer; Homohexamer when
CC       secreted. Interacts with envelope protein E. Non-structural protein 2A:
CC       Interacts (via N-terminus) with serine protease NS3. Non-structural
CC       protein 2B: Forms a heterodimer with serine protease NS3. May form
CC       homooligomers. Serine protease NS3: Forms a heterodimer with NS2B.
CC       Interacts with NS4B. Interacts with unphosphorylated RNA-directed RNA
CC       polymerase NS5; this interaction stimulates RNA-directed RNA polymerase
CC       NS5 guanylyltransferase activity. Non-structural protein 4A: Interacts
CC       with host MAVS; this interaction inhibits the synthesis of IFN-beta.
CC       Non-structural protein 4B: Interacts with serine protease NS3. RNA-
CC       directed RNA polymerase NS5: Homodimer. Interacts with host STAT2; this
CC       interaction inhibits the phosphorylation of the latter, and, when all
CC       viral proteins are present (polyprotein), targets STAT2 for
CC       degradation. Interacts with serine protease NS3.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein C]: Virion
CC       {ECO:0000250|UniProtKB:P17763}. Host nucleus
CC       {ECO:0000250|UniProtKB:P17763}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Peptide pr]: Secreted
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane
CC       {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
CC       {ECO:0000255}. Host endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane
CC       {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
CC       {ECO:0000255}. Host endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted
CC       {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane;
CC       Peripheral membrane protein; Lumenal side
CC       {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles
CC       hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic
CC       reticulum membrane; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum
CC       membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane
CC       protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side
CC       {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently
CC       associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion
CC       {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles
CC       hosting the replication complex. Interacts with host MAVS in the
CC       mitochondrion-associated endoplasmic reticulum membranes.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived
CC       vesicles hosting the replication complex.
CC       {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host
CC       endoplasmic reticulum membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}.
CC       Note=Located in RE-associated vesicles hosting the replication complex.
CC       NS5 protein is mainly localized in the nucleus rather than in ER
CC       vesicles, especially in the DENV 2, 3, 4 serotypes.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- DOMAIN: The transmembrane domains of the small envelope protein M and
CC       envelope protein E contain an endoplasmic reticulum retention signal.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield
CC       mature proteins. Cleavages in the lumen of endoplasmic reticulum are
CC       performed by host signal peptidase, whereas cleavages in the
CC       cytoplasmic side are performed by serine protease NS3. Signal cleavage
CC       at the 2K-4B site requires a prior NS3 protease-mediated cleavage at
CC       the 4A-2K site. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin,
CC       releasing the mature small envelope protein M, and peptide pr. This
CC       cleavage is incomplete as up to 30% of viral particles still carry
CC       uncleaved prM. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: [Envelope protein E]: N-glycosylated.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is
CC       glycosylated and this is required for efficient secretion of the
CC       protein from infected cells. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: [RNA-directed RNA polymerase NS5]: Sumoylation of RNA-directed RNA
CC       polymerase NS5 increases NS5 protein stability allowing proper viral
CC       RNA replication. {ECO:0000250|UniProtKB:P29990}.
CC   -!- PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines
CC       residues. This phosphorylation may trigger NS5 nuclear localization.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the class I-like SAM-
CC       binding methyltransferase superfamily. mRNA cap 0-1 NS5-type
CC       methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}.
CC   -!- WEB RESOURCE: Name=Virus Pathogen Resource;
CC       URL="http://www.viprbrc.org/brc/home.do?decorator=flavi_dengue";
DR   EMBL; AY947539; AAX48017.1; -; Genomic_RNA.
DR   PDB; 4AM0; X-ray; 3.02 A; Q/R/S/T=574-674.
DR   PDBsum; 4AM0; -.
DR   SMR; Q58HT7; -.
DR   PRIDE; Q58HT7; -.
DR   ABCD; Q58HT7; -.
DR   PRO; PR:Q58HT7; -.
DR   Proteomes; UP000000275; Genome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR   GO; GO:0039545; P:suppression by virus of host MAVS activity; IEA:UniProtKB-KW.
DR   GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039574; P:suppression by virus of host TYK2 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   CDD; cd12149; Flavi_E_C; 1.
DR   Gene3D; 1.10.10.930; -; 1.
DR   Gene3D; 1.10.8.970; -; 1.
DR   Gene3D; 1.20.1280.260; -; 1.
DR   Gene3D; 2.60.260.50; -; 1.
DR   Gene3D; 2.60.40.350; -; 1.
DR   Gene3D; 2.60.98.10; -; 1.
DR   Gene3D; 3.30.387.10; -; 1.
DR   Gene3D; 3.30.67.10; -; 1.
DR   InterPro; IPR011492; DEAD_Flavivir.
DR   InterPro; IPR000069; Env_glycoprot_M_flavivir.
DR   InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
DR   InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
DR   InterPro; IPR001122; Flavi_capsidC.
DR   InterPro; IPR037172; Flavi_capsidC_sf.
DR   InterPro; IPR027287; Flavi_E_Ig-like.
DR   InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
DR   InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
DR   InterPro; IPR001157; Flavi_NS1.
DR   InterPro; IPR000752; Flavi_NS2A.
DR   InterPro; IPR000487; Flavi_NS2B.
DR   InterPro; IPR000404; Flavi_NS4A.
DR   InterPro; IPR001528; Flavi_NS4B.
DR   InterPro; IPR002535; Flavi_propep.
DR   InterPro; IPR038688; Flavi_propep_sf.
DR   InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR   InterPro; IPR001850; Flavivirus_NS3_S7.
DR   InterPro; IPR014412; Gen_Poly_FLV.
DR   InterPro; IPR011998; Glycoprot_cen/dimer.
DR   InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR   InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR   InterPro; IPR013756; GlyE_cen_dom_subdom2.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR000208; RNA-dir_pol_flavivirus.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF01003; Flavi_capsid; 1.
DR   Pfam; PF07652; Flavi_DEAD; 1.
DR   Pfam; PF02832; Flavi_glycop_C; 1.
DR   Pfam; PF00869; Flavi_glycoprot; 1.
DR   Pfam; PF01004; Flavi_M; 1.
DR   Pfam; PF00948; Flavi_NS1; 1.
DR   Pfam; PF01005; Flavi_NS2A; 1.
DR   Pfam; PF01002; Flavi_NS2B; 1.
DR   Pfam; PF01350; Flavi_NS4A; 1.
DR   Pfam; PF01349; Flavi_NS4B; 1.
DR   Pfam; PF00972; Flavi_NS5; 1.
DR   Pfam; PF01570; Flavi_propep; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF00949; Peptidase_S7; 1.
DR   PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF101257; SSF101257; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF56983; SSF56983; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   TIGRFAMs; TIGR04240; flavi_E_stem; 1.
DR   PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
DR   PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activation of host autophagy by virus; ATP-binding;
KW   Capsid protein; Clathrin-mediated endocytosis of virus by host;
KW   Cleavage on pair of basic residues; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
KW   Host cytoplasm; Host endoplasmic reticulum; Host membrane;
KW   Host mitochondrion; Host nucleus; Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host MAVS by virus; Inhibition of host RLR pathway by virus;
KW   Inhibition of host STAT2 by virus; Inhibition of host TYK2 by virus;
KW   Ion channel; Ion transport; Membrane; Metal-binding; Methyltransferase;
KW   mRNA capping; mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW   Nucleotidyltransferase; Phosphoprotein; Protease; RNA-binding;
KW   RNA-directed RNA polymerase; S-adenosyl-L-methionine; Secreted;
KW   Serine protease; Suppressor of RNA silencing; Transcription;
KW   Transcription regulation; Transferase; Transmembrane; Transmembrane helix;
KW   Transport; Ubl conjugation; Viral attachment to host cell;
KW   Viral envelope protein; Viral immunoevasion; Viral ion channel;
KW   Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW   Virus endocytosis by host; Virus entry into host cell; Zinc.
FT   CHAIN           1..3387
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000405227"
FT   CHAIN           1..99
FT                   /note="Capsid protein C"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000268103"
FT   PROPEP          100..113
FT                   /note="ER anchor for the capsid protein C, removed in
FT                   mature form by serine protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000268104"
FT   CHAIN           114..279
FT                   /note="Protein prM"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000268105"
FT   CHAIN           114..204
FT                   /note="Peptide pr"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000268106"
FT   CHAIN           205..279
FT                   /note="Small envelope protein M"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000268107"
FT   CHAIN           280..774
FT                   /note="Envelope protein E"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000268108"
FT   CHAIN           775..1126
FT                   /note="Non-structural protein 1"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000268109"
FT   CHAIN           1127..1344
FT                   /note="Non-structural protein 2A"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000268110"
FT   CHAIN           1345..1474
FT                   /note="Serine protease subunit NS2B"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000268111"
FT   CHAIN           1475..2092
FT                   /note="Serine protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000268112"
FT   CHAIN           2093..2219
FT                   /note="Non-structural protein 4A"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000268113"
FT   PEPTIDE         2220..2242
FT                   /note="Peptide 2k"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000268114"
FT   CHAIN           2243..2487
FT                   /note="Non-structural protein 4B"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000268115"
FT   CHAIN           2488..3387
FT                   /note="RNA-directed RNA polymerase NS5"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT                   /id="PRO_0000268116"
FT   TOPO_DOM        1..100
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        118..237
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        259..265
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        280..723
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        724..746
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        747..750
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        751..771
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        772..1194
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1195..1218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1219..1224
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1225..1243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1244..1267
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1268..1288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1289
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1290..1308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1309..1316
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1317..1337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1338..1345
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1346..1366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1367..1369
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1370..1390
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1391..1437
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        1438..1458
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1459..2146
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2147..2167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2168..2169
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        2170..2190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2191
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2192..2212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2213..2225
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2226..2246
FT                   /note="Helical; Note=Signal for NS4B"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2247..2270
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        2271..2291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2292..2301
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        2302..2322
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2323..2343
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2344..2364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2365..2409
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2410..2430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2431..2455
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2456..2476
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2477..3387
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1475..1652
FT                   /note="Peptidase S7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT   DOMAIN          1654..1810
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1820..1987
FT                   /note="Helicase C-terminal"
FT   DOMAIN          2489..2751
FT                   /note="mRNA cap 0-1 NS5-type MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   DOMAIN          3016..3166
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   NP_BIND         1667..1674
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   REGION          36..71
FT                   /note="Hydrophobic; homodimerization of capsid protein C"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   REGION          377..390
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000250|UniProtKB:P14336"
FT   REGION          1397..1436
FT                   /note="Interacts with and activates NS3 protease"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00859"
FT   REGION          1658..1661
FT                   /note="Important for RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P14340"
FT   MOTIF           1758..1761
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           2564..2567
FT                   /note="SUMO-interacting motif"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   ACT_SITE        1525
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT   ACT_SITE        1549
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT   ACT_SITE        1609
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT   ACT_SITE        2548
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   ACT_SITE        2633
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   ACT_SITE        2668
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   ACT_SITE        2704
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   METAL           2925
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   METAL           2929
FT                   /note="Zinc 1; via tele nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   METAL           2934
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   METAL           2937
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   METAL           3200
FT                   /note="Zinc 2; via tele nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   METAL           3216
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   METAL           3335
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   BINDING         2543
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2573
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2574
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2591
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2592
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2618
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2619
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2634
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2706
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            99..100
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            113..114
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            204..205
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000250|UniProtKB:P29990, ECO:0000255"
FT   SITE            279..280
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            774..775
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            1126..1127
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            1344..1345
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            1474..1475
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            1931
FT                   /note="Involved in NS3 ATPase and RTPase activities"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   SITE            1934
FT                   /note="Involved in NS3 ATPase and RTPase activities"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   SITE            2092..2093
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            2219..2220
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            2242..2243
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            2487..2488
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P29990"
FT   SITE            2501
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2504
FT                   /note="mRNA cap binding; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2505
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2507
FT                   /note="mRNA cap binding; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2512
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2516
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2548
FT                   /note="Essential for 2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2633
FT                   /note="Essential for 2'-O-methyltransferase and N-7
FT                   methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2637
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2668
FT                   /note="Essential for 2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2699
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2701
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2704
FT                   /note="Essential for 2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   MOD_RES         2543
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        346
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        751
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        904
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        981
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2297
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2301
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        2453
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        282..309
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        339..400
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        353..384
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        371..395
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        464..564
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        581..612
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        778..789
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        829..917
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        953..997
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        1054..1103
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        1065..1087
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        1086..1090
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   STRAND          585..593
FT                   /evidence="ECO:0000244|PDB:4AM0"
FT   STRAND          599..605
FT                   /evidence="ECO:0000244|PDB:4AM0"
FT   STRAND          607..609
FT                   /evidence="ECO:0000244|PDB:4AM0"
FT   STRAND          611..613
FT                   /evidence="ECO:0000244|PDB:4AM0"
FT   STRAND          616..620
FT                   /evidence="ECO:0000244|PDB:4AM0"
FT   STRAND          632..634
FT                   /evidence="ECO:0000244|PDB:4AM0"
FT   STRAND          643..648
FT                   /evidence="ECO:0000244|PDB:4AM0"
FT   STRAND          652..661
FT                   /evidence="ECO:0000244|PDB:4AM0"
FT   HELIX           662..664
FT                   /evidence="ECO:0000244|PDB:4AM0"
FT   STRAND          666..672
FT                   /evidence="ECO:0000244|PDB:4AM0"
SQ   SEQUENCE   3387 AA;  378408 MW;  83A0CECAB088E1A8 CRC64;
     MNQRKKVVRP PFNMLKRERN RVSTPQGLVK RFSTGLFSGK GPLRMVLAFI TFLRVLSIPP
     TAGILKRWGQ LKKNKAIKIL TGFRKEIGRM LNILNGRKRS TMTLLCLIPT AMAFHLSTRD
     GEPLMIVARH ERGRPLLFKT TEGINKCTLI AMDLGEMCED TVTYECPLLV NTEPEDIDCW
     CNLTSAWVMY GTCTQSGERR REKRSVALTP HSGMGLETRA ETWMSSEGAW KHAQRVESWI
     LRNPGFALLA GFMAYMIGQT GIQRTVFFVL MMLVAPSYGM RCVGVGNRDF VEGVSGGAWV
     DLVLEHGGCV TTMAQGKPTL DFELIKTTAK EVALLRTYCI EASISNITTA TRCPTQGEPY
     LKEEQDQQYI CRRDVVDRGW GNGCGLFGKG GVVTCAKFSC SGKITGNLVQ IENLEYTVVV
     TVHNGDTHAV GNDIPNHGVT ATITPRSPSV EVKLPDYGEL TLDCEPRSGI DFNEMILMKM
     KKKTWLVHKQ WFLDLPLPWA AGADTSEVHW NYKERMVTFK VPHAKRQDVT VLGSQEGAMH
     SALTGATEVD SGDGNHMFAG HLKCKVRMEK LRIKGMSYTM CSGKFSIDKE MAETQHGTTV
     VKVKYEGAGA PCKVPIEIRD VNKEKVVGRI ISSTPFAEYT NSVTNIELEP PFGDSYIVIG
     VGDSALTLHW FRKGSSIGKM LESTYRGAKR MAILGETAWD FGSVGGLLTS LGKAVHQVFG
     SVYTTMFGGV SWMVRILIGF LVLWIGTNSR NTSMAMTCIA VGGITLFLGF TVHADTGCAV
     SWSGKELKCG SGIFVIDNVH TWTEQYKFQP ESPARLASAI LNAHEDGVCG IRSTTRLENI
     MWKQITNELN YVLWEGGHDL TVVAGDVKGV LSKGKRALAP PVNDLKYSWK TWGKAKIFTP
     EAKNSTFLID GPDTSECPNE RRAWNFLEVE DYGFGMFTTN IWMKFREGSS EVCDHRLMSA
     AIKDQKAVHA DMGYWIESSK NQTWQIEKAS LIEVKTCLWP KTHTLWSNGV LESQMLIPKA
     YAGPFSQHNY RQGYATQTVG PWHLGKLEID FGECPGTTVT IQEDCDHRGP SLRTTTASGK
     LVTQWCCRSC TMPPLRFLGE DGCWYGMEIR PLSEKEENMV KSQVSAGQGT SETFSMGLLC
     LTLFVEECLR RRVTRKHMIL VVVTTLCAII LGGLTWMDLL RALIMLGDTM SGRMGGQIHL
     AIMAVFKMSP GYVLGIFLRK LTSRETALMV IGMAMTTVLS IPHDLMEFID GISLGLILLK
     MVTHFDNTQV GTLALSLTFI RSTMPLVMAW RTIMAVLFVV TLIPLCRTSC LQKQSHWVEI
     TALILGAQAL PVYLMTLMKG ASKRSWPLNE GIMAVGLVSL LGSALLKNDV PLAGPMVAGG
     LLLAAYVMSG SSADLSLEKA ANVQWDEMAD ITGSSPIIEV KQDEDGSFSI RDIEETNMIT
     LLVKLALITV SGLYPLAIPV TMTLWYMWQV KTQRSGALWD VPSPAAAQKA TLTEGVYRIM
     QRGLFGKTQV GVGIHMEGVF HTMWHVTRGS VICHETGRLE PSWADVRNDM ISYGGGWRLG
     DKWDKEEDVQ VLAIEPGKNP KHVQTKPGLF KTLTGEIGAV TLDFKPGTSG SPIINRKGKV
     IGLYGNGVVT KSGDYVSAIT QAERTGEPDY EVDEDIFRKK RLTIMDLHPG AGKTKRILPS
     IVREALKRRL RTLILAPTRV VAAEMEEALR GLPIRYQTPA VKSEHTGREI VDLMCHATFT
     TRLLSSTRVP NYNLIVMDEA HFTDPSSVAA RGYISTRVEM GEAAAIFMTA TPPGATDPFP
     QSNSPIEDIE REIPERSWNT GFDWITDYQG KTVWFVPSIK AGNDIANCLR KSGKKVIQLS
     RKTFDTEYPK TKLTDWDFVV TTDISEMGAN FRAGRVIDPR RCLKPVISTD GPERVILAGP
     IPVTPASAAQ RRGRIGRNPA QEDDQYVFSG DPLKNDEDHA HWTEAKMLLD NIYTPEGIIP
     TLFGPEREKN QAIDGEFRLR GEQRKTFVEL MRRGDLPVWL SYKVASAGIS YKDREWCFTG
     ERNNQILEEN MEVEIWTREG EKKKLRPKWL DARVYADPMA LKDFKEFASG RKSITLDILT
     EIASLPTYLS SRAKLALDNI VMLHTTERGG KAYQHALNEL PESLETLMLV ALLGAMTAGI
     FLFFMQGKGI GKLSMGLIAI AVASGLLWVA EIQPQWIAAS IILEFFLMVL LIPEPEKQRT
     PQDNQLIYVI LTILTIIGLI AANEMGLIEK TKTDFGFYQV KTETTILDVD LRPASAWTLY
     AVATTILTPM LRHTIENTSA NLSLAAIANQ AAVLMGLGKG WPLHRMDLGV PLLAMGCYSQ
     VNPTTLIASL VMLLVHYAII GPGLQAKATR EAQKRTAAGI MKNPTVDGIT VIDLEPISYD
     PKFEKQLGQV MLLVLCAGQL LLMRTTWAFC EVLTLATGPV LTLWEGNPGR FWNTTIAVST
     ANIFRGSYLA GAGLAFSLIK NAQTPRRGTG TTGETLGEKW KRQLNSLDRK EFEEYKRSGI
     LEVDRTEAKS ALKDGSKIKH AVSRGSSKIR WIVERGMVKP KGKVVDLGCG RGGWSYYMAT
     LKNVTEVKGY TKGGPGHEEP IPMATYGWNL VKLHSGVDVF YKPTEQVDTL LCDIGESSSN
     PTIEEGRTLR VLKMVEPWLS SKPEFCIKVL NPYMPTVIEE LEKLQRKHGG SLVRCPLSRN
     STHEMYWVSG VSGNIVSSVN TTSKMLLNRF TTRHRKPTYE KDVDLGAGTR SVSTETEKPD
     MTIIGRRLQR LQEEHKETWH YDQENPYRTW AYHGSYEAPS TGSASSMVNG VVKLLTKPWD
     VIPMVTQLAM TDTTPFGQQR VFKEKVDTRT PQPKPGTRMV MTTTANWLWA LLGKKKNPRL
     CTREEFISKV RSNAAIGAVF QEEQGWTSAS EAVNDSRFWE LVDKERALHQ EGKCESCVYN
     MMGKREKKLG EFGRAKGSRA IWYMWLGARF LEFEALGFLN EDHWFGRENS WSGVEGEGLH
     RLGYILEDID KKDGDLIYAD DTAGWDTRIT EDDLLNEELI TEQMAPHHKI LAKAIFKLTY
     QNKVVKVLRP TPKGAVMDII SRKDQRGSGQ VGTYGLNTFT NMEVQLIRQM EAEGVITQDD
     MHNPKGLKER VEKWLKECGV DRLKRMAISG DDCVVKPLDE RFSTSLLFLN DMGKVRKDIP
     QWEPSKGWKN WQEVPFCSHH FHKIFMKDGR SLVVPCRNQD ELIGRARISQ GAGWSLRETA
     CLGKAYAQMW SLMYFHRRDL RLASMAICSA VPTEWFPTSR TTWSIHAHHQ WMTTEDMLKV
     WNRVWIEDNP NMTDKTPVHS WEDIPYLGKR EDLWCGSLIG LSSRATWAKN IHTAITQVRN
     LIGKEEYVDY MPVMKRYSAP FESEGVL
//
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