POLG_TBEVS
ID POLG_TBEVS Reviewed; 3412 AA.
AC P07720; P07721; Q88475; Q88476; Q88477; Q88478; Q88479; Q88877; Q88878;
AC Q88879;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Peptide 2k;
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;
DE EC=3.6.4.13;
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=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 Tick-borne encephalitis virus Far Eastern subtype (strain Sofjin) (SOFV)
OS (Sofjin virus).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Flavivirus.
OX NCBI_TaxID=11087;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=34615; Ixodes persulcatus (Taiga tick).
OH NCBI_TaxID=34613; Ixodes ricinus (Common tick) (Acarus ricinus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2136778; DOI=10.1016/0042-6822(90)90073-z;
RA Pletnev A.G., Yamshchikov V.F., Blinov V.M.;
RT "Nucleotide sequence of the genome and complete amino acid sequence of the
RT polyprotein of tick-borne encephalitis virus.";
RL Virology 174:250-263(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-1190.
RX PubMed=2970626; DOI=10.1093/nar/16.15.7750;
RA Yamshchikov V.F., Pletnev A.G.;
RT "Nucleotide sequence of the genome region encoding the structural proteins
RT and the NS1 protein of the tick borne encephalitis virus.";
RL Nucleic Acids Res. 16:7750-7750(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-683 AND 777-1002.
RX PubMed=3709796; DOI=10.1016/0014-5793(86)81160-7;
RA Pletnev A.G., Yamshchikov V.F., Blinov V.M.;
RT "Tick-borne encephalitis virus genome. The nucleotide sequence coding for
RT virion structural proteins.";
RL FEBS Lett. 200:317-321(1986).
RN [4]
RP GLYCOSYLATION (ENVELOPE PROTEIN E).
RX PubMed=2441520; DOI=10.1016/0042-6822(87)90460-0;
RA Winkler G., Heinz F.X., Kunz C.;
RT "Studies on the glycosylation of flavivirus E proteins and the role of
RT carbohydrate in antigenic structure.";
RL Virology 159:237-243(1987).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (24.0 ANGSTROMS) OF 281-675.
RX PubMed=11893341; DOI=10.1016/s0092-8674(02)00660-8;
RA Kuhn R.J., Zhang W., Rossmann M.G., Pletnev S.V., Corver J., Lenches E.,
RA Jones C.T., Mukhopadhyay S., Chipman P.R., Strauss E.G., Baker T.S.,
RA Strauss J.H.;
RT "Structure of dengue virus: implications for flavivirus organization,
RT maturation, and fusion.";
RL Cell 108:717-725(2002).
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. {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 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 (By similarity). May have membrane-
CC destabilizing 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. {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. Inhibits STAT2
CC translocation in the nucleus after IFN-alpha treatment.
CC {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+)
CC and (-) genome, and performs the capping of genomes in the cytoplasm.
CC NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions.
CC Besides its role in RNA genome replication, also prevents the
CC establishment of cellular antiviral state by blocking the interferon-
CC alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and
CC STAT2 phosphorylation, thereby preventing activation of JAK-STAT
CC 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:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
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)-(ribonucleoside) in mRNA +
CC S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC ChEBI:CHEBI:167617; 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)-ribonucleoside
CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
CC -!- SUBUNIT: [Capsid protein C]: Homodimer (By similarity). Interacts (via
CC N-terminus) with host EXOC1 (via C-terminus); this interaction results
CC in EXOC1 degradation through the proteasome degradation pathway (By
CC similarity). {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Protein prM]: Forms heterodimers with envelope protein E in
CC the endoplasmic reticulum and Golgi. {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Envelope protein E]: Homodimer; in the endoplasmic reticulum
CC and Golgi (By similarity). Interacts with protein prM (By similarity).
CC Interacts with non-structural protein 1 (By similarity).
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Non-structural protein 1]: Homodimer; Homohexamer when
CC secreted. Interacts with envelope protein E.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Non-structural protein 2A]: Interacts (via N-terminus) with
CC serine protease NS3. {ECO:0000250|UniProtKB:P03314}.
CC -!- SUBUNIT: [Serine protease subunit NS2B]: Forms a heterodimer with
CC serine protease NS3 (By similarity). May form homooligomers (By
CC similarity). {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Serine protease NS3]: Forms a heterodimer with NS2B (By
CC similarity). Interacts with non-structural protein 2A (via N-terminus)
CC (By similarity). Interacts with NS4B (By similarity). Interacts with
CC unphosphorylated RNA-directed RNA polymerase NS5; this interaction
CC stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity
CC (By similarity). {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Non-structural protein 4B]: Interacts with serine protease
CC NS3 (By similarity). Interacts with NS1 (By similarity).
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [RNA-directed RNA polymerase NS5]: Homodimer. Interacts with
CC host STAT2; this interaction inhibits the phosphorylation of the
CC latter, and, when all viral proteins are present (polyprotein), targets
CC STAT2 for degradation. Interacts with serine protease NS3. Interacts
CC with host SCRIB; this interaction targets NS5 to the cell membrane
CC periphery and nucleus, thereby allowing efficient host nuclear STAT1
CC inhibition. {ECO:0000250|UniProtKB:Q01299}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein C]: Virion
CC {ECO:0000250|UniProtKB:P17763}. Host nucleus
CC {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region
CC {ECO:0000250|UniProtKB:P17763}. Host cytoplasm
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:P03314}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC {ECO:0000255}. Note=ER membrane retention is mediated by the
CC transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
CC -!- SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane
CC {ECO:0000305}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC {ECO:0000255}. Note=ER membrane retention is mediated by the
CC transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
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:P14335}; 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:P14335}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated
CC vesicles hosting the replication complex.
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:P06935}.
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. {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:0000269|PubMed:2441520}.
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]: 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 Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1k4r";
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DR EMBL; X07755; CAA30581.1; -; Genomic_RNA.
DR EMBL; X03870; CAA27500.1; -; Genomic_RNA.
DR EMBL; X03870; CAA27501.1; ALT_SEQ; Genomic_RNA.
DR EMBL; X03870; CAA27502.1; ALT_SEQ; Genomic_RNA.
DR EMBL; X03870; CAA27503.1; ALT_SEQ; Genomic_RNA.
DR EMBL; X03871; CAA27505.1; -; Genomic_RNA.
DR PIR; A33776; GNWVTB.
DR PDB; 1K4R; EM; 24.00 A; A/B/C=281-675.
DR PDB; 7LSE; X-ray; 2.35 A; E=581-677.
DR PDBsum; 1K4R; -.
DR PDBsum; 7LSE; -.
DR SMR; P07720; -.
DR PRIDE; P07720; -.
DR EvolutionaryTrace; P07720; -.
DR Proteomes; UP000007401; 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: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: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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039563; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW.
DR GO; GO:0039564; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT2 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; cd20761; capping_2-OMTase_Flaviviridae; 1.
DR CDD; cd12149; Flavi_E_C; 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 Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011492; DEAD_Flavivir.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
DR InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
DR InterPro; IPR001122; Flavi_capsidC.
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; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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; PF00948; Flavi_NS1; 1.
DR Pfam; PF01005; Flavi_NS2A; 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; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF56672; SSF56672; 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; Host nucleus;
KW 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 STAT1 by virus; Inhibition of host STAT2 by virus;
KW Membrane; Metal-binding; Methyltransferase; mRNA capping; mRNA processing;
KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW Phosphoprotein; Protease; RNA-binding; RNA-directed RNA polymerase;
KW S-adenosyl-L-methionine; Secreted; Serine protease;
KW Suppressor of RNA silencing; Transcription; Transcription regulation;
KW Transferase; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Viral immunoevasion;
KW Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW Virus endocytosis by host; Virus entry into host cell; Zinc.
FT CHAIN 1..3412
FT /note="Genome polyprotein"
FT /id="PRO_0000405171"
FT CHAIN 1..96
FT /note="Capsid protein C"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037804"
FT PROPEP 97..117
FT /note="ER anchor for the capsid protein C, removed in
FT mature form by serine protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000405172"
FT CHAIN 118..280
FT /note="Protein prM"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000405173"
FT CHAIN 118..205
FT /note="Peptide pr"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037805"
FT CHAIN 206..280
FT /note="Small envelope protein M"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037806"
FT CHAIN 281..776
FT /note="Envelope protein E"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037807"
FT CHAIN 777..1128
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037808"
FT CHAIN 1129..1358
FT /note="Non-structural protein 2A"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037809"
FT CHAIN 1359..1489
FT /note="Serine protease subunit NS2B"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037810"
FT CHAIN 1490..2110
FT /note="Serine protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037811"
FT CHAIN 2111..2236
FT /note="Non-structural protein 4A"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037812"
FT PEPTIDE 2237..2259
FT /note="Peptide 2k"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000405174"
FT CHAIN 2260..2510
FT /note="Non-structural protein 4B"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037813"
FT CHAIN 2511..3412
FT /note="RNA-directed RNA polymerase NS5"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037814"
FT TOPO_DOM 1..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..727
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 728..748
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 749..755
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 756..776
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 777..1187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1188..1208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1209..1236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1237..1257
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P17763, ECO:0000255"
FT TOPO_DOM 1258..1293
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P17763, ECO:0000255"
FT TRANSMEM 1294..1314
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P17763, ECO:0000255"
FT TOPO_DOM 1315..1327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P17763, ECO:0000255"
FT TRANSMEM 1328..1348
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P17763, ECO:0000255"
FT TOPO_DOM 1349..1359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P17763, ECO:0000255"
FT TRANSMEM 1360..1378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1379..1382
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1383..1403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1404..1454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1455..1475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1476..2160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2161..2181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2182..2189
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 2190..2210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2211
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2212..2232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2233..2244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2245..2265
FT /note="Helical; Note=Signal for NS4B"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2266..2299
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 2300..2320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2321..2343
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 2344..2364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2365..2368
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2369..2389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2390..2430
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2431..2451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2452..2476
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2477..2497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2498..3412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1490..1669
FT /note="Peptidase S7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT DOMAIN 1675..1831
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1841..2000
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2511..2775
FT /note="mRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT DOMAIN 3038..3187
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..391
FT /note="Fusion peptide"
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT REGION 1410..1449
FT /note="Interacts with and activates NS3 protease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00859"
FT REGION 2729..2733
FT /note="Interaction with host SCRIB"
FT /evidence="ECO:0000250|UniProtKB:Q01299"
FT MOTIF 1779..1782
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT ACT_SITE 1543
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 1567
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 1627
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 2571
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2656
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2693
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2729
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT BINDING 1688..1695
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 2566
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2596
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2597
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2615
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2641
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2642
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2657
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2731
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2948
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2952
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2957
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2960
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 96..97
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT SITE 117..118
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT SITE 205..206
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 280..281
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 776..777
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT SITE 1128..1129
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1358..1359
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1489..1490
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT SITE 1949
FT /note="Involved in NS3 ATPase and RTPase activities"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 1952
FT /note="Involved in NS3 ATPase and RTPase activities"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 2110..2111
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT SITE 2236..2237
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT SITE 2259..2260
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT SITE 2510..2511
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT SITE 2523
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2526
FT /note="mRNA cap binding; via carbonyl oxygen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2527
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2529
FT /note="mRNA cap binding; via carbonyl oxygen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2534
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2538
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2571
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2656
FT /note="Essential for 2'-O-methyltransferase and N-7
FT methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2660
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2693
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2724
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2726
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2729
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT MOD_RES 2566
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P14336,
FT ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 861
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 983
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 999
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 283..310
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT DISULFID 340..401
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 340..396
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT DISULFID 354..385
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT DISULFID 372..401
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT DISULFID 372..396
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 466..570
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT DISULFID 587..618
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT DISULFID 780..791
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 831..920
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 955..1000
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1057..1106
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1068..1090
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1089..1093
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT CONFLICT 381
FT /note="W -> S (in Ref. 3; CAA27500)"
FT /evidence="ECO:0000305"
FT STRAND 591..600
FT /evidence="ECO:0007829|PDB:7LSE"
FT STRAND 602..612
FT /evidence="ECO:0007829|PDB:7LSE"
FT STRAND 614..619
FT /evidence="ECO:0007829|PDB:7LSE"
FT STRAND 622..626
FT /evidence="ECO:0007829|PDB:7LSE"
FT STRAND 636..641
FT /evidence="ECO:0007829|PDB:7LSE"
FT STRAND 643..645
FT /evidence="ECO:0007829|PDB:7LSE"
FT STRAND 651..655
FT /evidence="ECO:0007829|PDB:7LSE"
FT STRAND 658..665
FT /evidence="ECO:0007829|PDB:7LSE"
FT STRAND 668..674
FT /evidence="ECO:0007829|PDB:7LSE"
SQ SEQUENCE 3412 AA; 377981 MW; 0F61CE6DCCDC5965 CRC64;
MAGKAILKGK GGGPPRRVSK ETAKKTRQSR VQMPNGLVLM RMMGILWHAV AGTARSPVLK
SFWKSVPLKQ ATAALRKIKK AVSTLMVGLQ RRGKRRSAVD WTGWLLVVVL LGVTLAATVR
KERDGTTVIR AEGKDAATQV RVENGTCVIL ATDMGSWCDD SLTYECVTID QGEEPVDVDC
SCRNVDGVYL EYGRCGKQEG SRTRRSVLIP SHAQGDLTGR GHKWLEGDSL RTHLTRVEGW
VWKNKVLTLA VIAVVWLTVE SVVTRVAVVV VLLCLAPVYA SRCTHLENRD FVTGTQGTTR
VTLVLELGGC VTITAEGKPS MDVWLDSIYQ ENPAKTREYC LHAKLSDTKV AARCPTMGPA
TLAEEHQSGT VCKRDQSDRG WGNHCGLFGK GSIVTCVKAS CEAKKKATGH VYDANKIVYT
VKVEPHTGDY VAANETHSGR KTASFTVSSE RTILTMGDYG DVSLLCRVAS GVDLAQTVIL
ELDKTSEHLP TAWQVHRDWF NDLALPWKHE GAQNWNNAER LVEFGAPHAV KMDVYNLGDQ
TGVLLKSLAG VPVAHIDGTK YHLKSGHVTC EVGLEKLKMK GLTYTMCDKT KFTWKRIPTD
SGHDTVVMEV AFSGTKPCRI PVRAVAHGSP DVNVAMLMTP NPTIENNGGG FIEMQLPPGD
NIIYVGELSH QWFQKGSSIG RVFQKTRKGI ERLTVIGEHA WDFGSTGGFL TSVGKALHTV
LGGAFNSLFG GVGFLPKILV GVVLAWLGLN MRNPTMSMSF LLAGGLVLAM TLGVGADVGC
AVDTERMELR CGEGLVVWRE VSEWYDNYAY YPETLGALAS AIKETFEEGT CGIVPQNRLE
MAMWRSSATE LNLALVEGDA NLTVVVDKLD PTDYRGGIPS LLKKGKDIKV SWKSWGHSMI
WSVPEAPRLF MVGTEGSSEC PLERRKTGVF TVAEFGVGLR TKVFLDFRQE STHECDTGVM
GAAVKNGMAV HTDQSLWMKS VRNDTGTYIV ELLVTDLRNC SWPASHTIDN AEVVDSELFL
PASLAGPRSW YNRIPGYSEQ VKGPWKYSPI RVTREECPGT RVTINADCDK RGASVRSTTE
SGKVIPEWCC RTCTLPPVTF RTGTDCWYAM EIRPVHDQGG LVRSMVVADN GELLSEGGIP
GIVALFVVLE YVIRRRPATG TTAMWGGIVV LALLVTGLVK IESLVRYVVA VGITFHLELG
PEIVALTLLQ AVFELRVGLL SAFALRSNLT VREMVTIYFL LLVLELGLPS EGLGALWKWG
DALAMGALIF RACTAEEKTG VGLLLMALMT QQDLATVHYG LMLFLGVASC CSIWKLIRGH
REQKGLTWIV PLAGLLGGEG SGVRLVAFWE LTVHGRRRSF SEPLTVVGVM LTLASGMIRH
TSQEALCALA VASFLLLMLV LGTRKMQLVA EWSGCVEWHP ELMNEGGEVS LRVRQDSMGN
FHLTELEKEE RVMAFWLLAG LAASAFHWSG ILGVMGLWTL SEMLRTARRS GLVFSGQGGR
ERGDRPFEVK DGVYRIFSPG LLWGQRQVGV GYGSKGVLHT MWHVTRGAAL SIDDAVAGPY
WADVKEDVVC YGGAWSLEEK WKGETVQVHA FPPGRAHEVH QCQPGELLLD TGRRIGAVPI
DLAKGTSGSP ILNSQGVVVG LYGNGLKTNE TYVSSIAQGE AEKSRPNLPP AVTGTGWTAK
GQITVLDMHP GSGKTHRVLP ELIRQCIDRR LRTLVLAPTR VVLKEMERAL NGKRVRFHSP
AVGDQQVGGS IVDVMCHATY VNRRLLPQGR QNWEVAIMDE AHWTDPHSIA ARGHLYTLAK
ENKCALVLMT ATPPGKSEPF PESNGAISSE EKQIPDGEWR DGFDWITEYE GRTAWFVPSS
AKGGIIARTL IQKGKSVICL NSKTFEKDYS RVRDEKPDFV VTTDISEMGA NLDVSRVIDG
RTNIKPEEVD GRVELTGTRR VTTASAAQRR GRVGRQEGRT DEYIYSGQCD DDDSGLVQWK
EAQILLDNIT TLRGPVATFY GPEQDKMPEV AGHFRLTEEK RKHFRHLLTH CDFTPWLAWH
VAANVSSVTS RNWTWEGPEE NTVDEANGDL VTFRSPNGAE RTLRPVWRDA RMFREGRDIR
EFVAYASGRR SFGDVLSGMS GVPELLRHRC VSAMDVFYTL MHEEPGSRAM KMAERDAPEA
FLTVVEMMVL GLATLGVVWC FVVRTSISRM MLGTLVLLAS LALLWAGGVS YGNMAGVALI
FYTLLTVLQP EAGKQRSSDD NKLAYFLLTL CSLAGLVAAN EMGFLEKTKA DLSTVLWSEH
EELRSWEEWT NIDIQPARSW GTYVLVVSLF TPYIIHQLQT KIQQLVNSAV ATGAQAMRDL
GGGAPFFGVA GHVMALGVVS LVGATPTSLV VGVGLAAFHL AIVVSGLEAE LTQRAHKVFF
SAMVRNPMVD GDVINPFGEG EAKPALYERK MSLVLAIVLC LMSVVMNRTV PSTPRLLLWD
WRQRDNCSNQ RRTPFGRCQA CGLSGVVRGS LWGFCPLGHR LWLRASGSRR GGSEGDTLGD
LWKRKLNGCT KEEFFAYRRT GILETERDKA RELLKRGETN MGLAVSRGTA KLAWLEERGY
ATLKGEVVDL GCGRGGWSYY AASRPAVMSV KACAIAGKGH ETPKMVTSLG WNLIKFRAGM
DVFSMQPHRA DTIMCDIGES NPDAVVEGER TRKVILLMEQ WKNRNPTATC VFKALAPYRP
EVTEALHRFQ LQWGGGLVRT PFSRNSTHEM YYSTAITGNI VNSVNIQSRK LLARFGDQRG
PTRVPELDLG VGTRCVVLAE DKVKEKDVQE RISALREQYG ETWHMDREHP YRTWQYWAAT
ACANRVGGAL INGVVKLLSW PWNAREDVVR MAMTDTTAFG QQRVFKEKVD TKAQEPQPGT
KVIMRAVNDW ILERLARKSK PRMCSREEFI AKVKSNAALG AWSDEQNRWS SAKEAVEDPA
FWQLVDEERE RHLAGRCAHC VYNMMGKREK KLGEFGVAKG SRAIWYMWLG SRFLEFEALG
FLNEDHWASR GSSGSGVEGI SLNYLGWHLK GLSTLEGGLF YADDTAGWDT KVTNADLEDE
EQLLRYMEGE HKQLAATIMQ KAYHAKVVKV ARPSRDGGCI MDVITRRDQR GSGQVVTYAL
NTLTNIKVQL IRMMEGEGVI EASDAHNPRL LRVERWLRDH GEERLGRMLV SGDDCVVRPV
DDRFSGALYF LNDMAKTRKD IGEWDHSVGF SNWEEVPFCS HHFHELVMKD GRTLIVPCRD
QDELVGRARV SPGCGRSVRE TACLSKAYGQ MWLLSYFHRR DLRTLGLAIC SAVPVDWVPA
GRTTWSIHAS GAWMTTEDML DVWNRVWILD NPFMHSKEKI AEWRDVPYLP KSHDMLCSSL
VGRKERAEWA KNIWGAVEKV RKMIGQEKFK DYLSCMDRHD LHWESKLESS II
