POLG_LANVT
ID POLG_LANVT Reviewed; 3414 AA.
AC P29837;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 173.
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=NS5;
OS Langat virus (strain TP21).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Flavivirus.
OX NCBI_TaxID=31638;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=6935; Ixodida (ticks).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-776.
RX PubMed=1720591; DOI=10.1016/0042-6822(91)90567-u;
RA Mandl C.W., Iacono-Connors L.C., Wallner G., Holzmann H., Kunz C.,
RA Heinz F.X.;
RT "Sequence of the genes encoding the structural proteins of the low-
RT virulence tick-borne flaviviruses Langat TP21 and Yelantsev.";
RL Virology 185:891-895(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 777-3414.
RX PubMed=1316684; DOI=10.1016/0042-6822(92)90545-z;
RA Iacono-Connors L.C., Schmaljohn C.S.;
RT "Cloning and sequence analysis of the genes encoding the nonstructural
RT proteins of Langat virus and comparative analysis with other
RT flaviviruses.";
RL Virology 188:875-880(1992).
RN [3]
RP FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5).
RX PubMed=16188985; DOI=10.1128/jvi.79.20.12828-12839.2005;
RA Best S.M., Morris K.L., Shannon J.G., Robertson S.J., Mitzel D.N.,
RA Park G.S., Boer E., Wolfinbarger J.B., Bloom M.E.;
RT "Inhibition of interferon-stimulated JAK-STAT signaling by a tick-borne
RT flavivirus and identification of NS5 as an interferon antagonist.";
RL J. Virol. 79:12828-12839(2005).
RN [4]
RP STRUCTURE BY NMR OF 580-675, AND DISULFIDE BOND.
RX PubMed=16731969; DOI=10.1110/ps.051844006;
RA Mukherjee M., Dutta K., White M.A., Cowburn D., Fox R.O.;
RT "NMR solution structure and backbone dynamics of domain III of the E
RT protein of tick-borne Langat flavivirus suggests a potential site for
RT molecular recognition.";
RL Protein Sci. 15:1342-1355(2006).
CC -!- FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding
CC to membrane and gathering the viral RNA into a nucleocapsid that forms
CC the core of a mature virus particle. During virus entry, may induce
CC genome penetration in host cytoplasm after hemifusion induced by
CC surface proteins. Can migrate to the cell nucleus where it modulates
CC 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. Presumably to avoid
CC catastrophic activation of the viral fusion activity in acidic GolGi
CC compartment prior to virion release. prM-E cleavage is ineficient, 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 extodomain. 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 ineficient, 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 (By similarity). NS5 methylates viral RNA cap at guanine N-7 and ribose
CC 2'-O positions (By similarity). Besides its role in genome replication,
CC also prevents the establishment of cellular antiviral state by blocking
CC the interferon-alpha/beta (IFN-alpha/beta) signaling pathway
CC (PubMed:16188985). Inhibits host TYK2 and STAT2 phosphorylation,
CC thereby preventing activation of JAK-STAT signaling pathway
CC (PubMed:16188985). {ECO:0000250|UniProtKB:P17763,
CC ECO:0000269|PubMed:16188985}.
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: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]: 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M73835; AAA02740.1; ALT_TERM; Unassigned_RNA.
DR EMBL; S35365; AAB22165.1; -; Genomic_RNA.
DR PIR; A42545; A42545.
DR PDB; 1Z66; NMR; -; A=580-675.
DR PDB; 2GG1; NMR; -; A=580-675.
DR PDBsum; 1Z66; -.
DR PDBsum; 2GG1; -.
DR BMRB; P29837; -.
DR SMR; P29837; -.
DR PRIDE; P29837; -.
DR BRENDA; 3.4.21.91; 9644.
DR EvolutionaryTrace; P29837; -.
DR Proteomes; UP000007766; 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:0039651; P:induction by virus of host cysteine-type endopeptidase activity involved in apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039574; P:suppression by virus of host JAK-STAT cascade via inhibition of host TYK2 activity; IDA:UniProtKB.
DR GO; GO:0039576; P:suppression by virus of host JAK-STAT cascade via inhibition of JAK1 activity; IDA:UniProtKB.
DR GO; GO:0039563; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IDA:UniProtKB.
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; 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; 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; PF01004; Flavi_M; 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;
KW Activation of host caspases by virus; ATP-binding; Capsid protein;
KW 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 JAK1 by virus; Inhibition of host STAT1 by virus;
KW Inhibition of host STAT2 by virus; Inhibition of host TYK2 by virus;
KW Membrane; Metal-binding; Methyltransferase;
KW Modulation of host cell apoptosis by virus; 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..3414
FT /note="Genome polyprotein"
FT /id="PRO_0000405129"
FT CHAIN 1..96
FT /note="Capsid protein C"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037688"
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_0000405130"
FT CHAIN 118..280
FT /note="Protein prM"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000405131"
FT CHAIN 118..205
FT /note="Peptide pr"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037689"
FT CHAIN 206..280
FT /note="Small envelope protein M"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037690"
FT CHAIN 281..776
FT /note="Envelope protein E"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037691"
FT CHAIN 777..1128
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037692"
FT CHAIN 1129..1358
FT /note="Non-structural protein 2A"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037693"
FT CHAIN 1359..1489
FT /note="Serine protease subunit NS2B"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037694"
FT CHAIN 1490..2110
FT /note="Serine protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037695"
FT CHAIN 2111..2236
FT /note="Non-structural protein 4A"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037696"
FT PEPTIDE 2237..2259
FT /note="Peptide 2k"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000405132"
FT CHAIN 2260..2511
FT /note="Non-structural protein 4B"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037697"
FT CHAIN 2512..3414
FT /note="RNA-directed RNA polymerase NS5"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037698"
FT TOPO_DOM 1..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..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:0000255"
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..1232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1233..1253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1254..1267
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1268..1288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1289..1300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1301..1319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1320..1325
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1326..1346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1347..1359
FT /note="Cytoplasmic"
FT /evidence="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..2209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2210
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2211..2231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2232..2238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2239..2259
FT /note="Helical; Note=Signal for NS4B"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2260..2296
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 2297..2315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2316..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..2432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2433..2453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2454..2477
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2478..2498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2499..3414
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 2512..2776
FT /note="mRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT DOMAIN 3040..3189
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 1..27
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 2730..2734
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 2572
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2657
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2694
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2730
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 2567
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 2598
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 2616
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 2643
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2658
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2732
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2950
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2954
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2959
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2962
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3359
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 2511..2512
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT SITE 2524
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2527
FT /note="mRNA cap binding; via carbonyl oxygen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2528
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2530
FT /note="mRNA cap binding; via carbonyl oxygen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2535
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2539
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2572
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2657
FT /note="Essential for 2'-O-methyltransferase and N-7
FT methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2661
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2694
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2725
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2727
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2730
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT MOD_RES 2567
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:0000269|PubMed:16731969"
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 TURN 589..591
FT /evidence="ECO:0007829|PDB:1Z66"
FT STRAND 593..600
FT /evidence="ECO:0007829|PDB:1Z66"
FT STRAND 602..611
FT /evidence="ECO:0007829|PDB:1Z66"
FT STRAND 616..619
FT /evidence="ECO:0007829|PDB:1Z66"
FT STRAND 622..626
FT /evidence="ECO:0007829|PDB:1Z66"
FT STRAND 629..633
FT /evidence="ECO:0007829|PDB:2GG1"
FT STRAND 643..645
FT /evidence="ECO:0007829|PDB:1Z66"
FT STRAND 648..654
FT /evidence="ECO:0007829|PDB:1Z66"
FT STRAND 657..665
FT /evidence="ECO:0007829|PDB:1Z66"
FT STRAND 668..674
FT /evidence="ECO:0007829|PDB:1Z66"
SQ SEQUENCE 3414 AA; 378023 MW; 59CB7E95DD70D82E CRC64;
MAGKAVLKGK GGGPPRRASK VAPKKTRQLR VQMPNGLVLM RMLGVLWHAL TGTARSPVLK
AFWKVVPLKQ ATLALRKIKR TVSTLMVGLH RRGSRRTTID WMTPLLITVM LGMCLTATVR
RERDGSMVIR AEGRDAATQV RVENGTCVIL ATDMGSWCDD SLAYECVTID QGEEPVDVDC
FCRGVEKVTL EYGRCGRREG SRSRRSVLIP SHAQRDLTGR GHQWLEGEAV KAHLTRVEGW
VWKNKLFTLS LVMVAWLMVD GLLPRILIVV VALALVPAYA SRCTHLENRD FVTGVQGTTR
LTLVLELGGC VTVTADGKPS LDVWLDSIYQ ESPAQTREYC LHAKLTGTKV AARCPTMGPA
TLPEEHQSGT VCKRDQSDRG WGNHCGLFGK GSIVTCVKFT CEDKKKATGH VYDVNKITYT
IKVEPHTGEF VAANETHSGR KSASFTVSSE KTILTLGDYG DVSLLCRVAS GVDLAQTVVL
ALDKTHEHLP TAWQVHRDWF NDLALPWKHD GAEAWNEAGR LVEFGTPHAV KMDVFNLGDQ
TGVLLKSLAG VPVASIEGTK YHLKSGHVTC EVGLEKLKMK GLTYTVCDKT KFTWKRAPTD
SGHDTVVMEV GFSGTRPCRI PVRAVAHGVP EVNVAMLITP NPTMENNGGG FIEMQLPPGD
NIIYVGDLNH QWFQKGSSIG RVLQKTRKGI ERLTVLGEHA WDFGSVGGVM TSIGRAMHTV
LGGAFNTLLG GVGFLPKILL GVAMAWLGLN MRNPTLSMGF LLSGGLVLAM TLGVGADVGC
AVDTERMELR CGEGLVVWRE VSEWYDNYVF HPETPAVLAS AVQRAYEEEI CGIVPQNRLE
MAMWRSSLVE LNLALAEGEA NLTVVVDKAD PSDYRGGVPG LLNKGKDIKV SWRSWGRSML
WSVPEAPRRF MIGVEGGREC PFARRKTGVM TVAEFGIGLR TKVFMDLRQE LTTECDTGVM
GAAVKNGMAV HTDQSLWMKS IKNDTTVTIV ELIVTDLRNC TWPASHTIDN AGVVNSKLFL
PASLAGPRST YNVIPGYAEQ VRGPWAHTPV RIKREECPGT RVTIDKACDK RGASVRSTTE
SGKVIPEWCC RTCELPPVTY RTGTDCWYAM EIRPVHTQGG LVRSMVVADN GALLSEGGVP
GVVALFVVLE LVIRRRPATG GTVIWGGIAI LALLVTGLVS VESLFRYLVA VGLVFQLELG
PEAVAMVLLQ AVFEMRTCLL SGFVLRRSIT TREIVTVYFL LLVLEMGIPV KGLEHLWRWT
DALAMGAIIF RACTAEGKTG IGLLLAAFMT QSDMNIIHDG LTAFLCVATT MAIWRYIRGQ
GERKGLTWIV PLAGILGGEG SGVRLLAFWE LAASRGRRSF NEPMTVIGVM LTLASGMMRH
TSQEAVCAMA LAAFLLLMLT LGTRKMQLLA EWSGNIEWNP ELTSEGGEVS LRVRQDALGN
LHLTELEKEE RMMAFWLVVG LIASAFHWSG ILIVMGLWTI SEMLGSPRRT DLVFSGCSEG
RSDSRPLDVK NGVYRIYTPG LLWGQRQIGV GYGAKGVLHT MWHVTRGAAL LVDGVAVGPY
WADVREDVVC YGGAWSLESR WRGETVQVHA FPPGRAHETH QCQPGELILE NGRKMGAIPI
DLAKGTSGSP IMNSQGEVVG LYGNGLKTND TYVSSIAQGE VEKSRPNLPQ SVVGTGWTAK
GQITVLDMHP GSGKTHRVLP ELIRQCVERR LRTLVLAPTR VVLREMERAL SGKNVRFHSP
AVTEQHANGA IVDVMCHATY VNRRLLPQGR QNWEVAIMDE AHWTDPHSIA ARGHLYSLAK
ENRCAFVLMT ATPPGKSEPF PESNGAIASE ERQIPDGEWR DGFDWITEYE GRTAWFVPSI
ARGGAIARAL RQRGKSVICL NSKTFDKEYS RVKDEKPDFV VTTDISEMGA NLDVTRVIDG
RTNIKPEEVD GRIELTGTRR VTTASAAQRR GRVGRQGGRT DEYIYSGQCD DDDSGLVQWK
EAQILLDNIT TARGPVATFY GPEQERMTET AGHYRLPEEK RKHFRHLLAQ CDFTPWLAWH
VAANVASVTD RSWTWEGPEE NAVDENNGEL VTFRSPNGAE RTLRPVWRDA RMFREGRDIR
EFVSYASGRR SVGDVLMGMS GVPALLRQRC TSAMDVFYTL MHEEPGSRAM RIGERDAPEA
FLTAVEMLVL GLATLGVVWC FVVRTSVSRM VLGTLVLATS LIFLWAGGVG YGNMAGVALV
FYTLLTVLQP ETGKQRSSDD NKLAYFLLTL CGLAGMVAAN EMGLLEKTKA DLAALFARDQ
GETVRWGEWT NLDIQPARSW GTYVLVVSLF TPYMLHQLQT RIQQLVNSAV ASGAQAMRDL
GGGTPFFGVA GHVLALGVAS LVGATPTSLI LGVGLAAFHL AIVVSGLEAE LTQRAHKVFF
SAMVRNPMVD GDVINPFGDG EAKPALYERK LSLILALVLC LASVVMNRTF VAVTEAGAVG
VAAAMQLLRP EMDVLWTMPV ACGMSGVVRG SLWGLLPLGH RLWLRTTGTR RGGSEGDTLG
DMWKARLNSC TKEEFFAYRR AGVMETDREK ARELLKRGET NMGLAVSRGT SKLAWMEERG
YVTLKGEVVD LGCGRGGWSY YAASRPAVMS VRAYTIGGKG HESPRMVTSL GWNLIKFRAG
MDVFSMEPHR ADAILCDIGE SNPDAVVEGE RSRRVILLME QWKNRNPTAT CVFKVLAPYR
PEVIEALHRF QLQWGGGLVR TPFSRNSTHE MYFSTAITGN IVNSVNIQSR KLLARFGDQR
GPTRVPEIDL GVGTRSVVLA EDKVKEKDVM ERIQALKDQY CDTWHEDHEH PYRTWQYWGS
YKTAATGSSA SLLNGVVKLL SWPWNAREDV VRMAMTDTTA FGQQRVFKDK VDTKAQEPQP
GTKIIMRAVN DWLLERLVKK SRPRMCSREE FIAKVRSNAA LAAWSDEQNK WKSAREAVED
PEFWSLVEAE RERHLQGRCA HCVYNMMGKR EKKLGEFGVA KGSRAIWYMW LGSRFLEFEA
LGFLNEDHWA SRASSGAGVE GISLNYLGWH LKKLASLSGG LFYADDTAGW DTRITNADLD
DEEQILRYMD GDHKKLAATV LRKAYHAKVV RVARPSREGG CVMDIITRRD QRGSGQVVTY
ALNTITNIKV QLVRMMEGEG VIEVADSHNP RLLRVEKCVE EHGEERLSRM LVSGDDCVVR
PVDDRFSKAL YFLNDMAKTR KDTGEWEPST GFASWEEVPF CSHHFHELVM KDGRALVVPC
RDQDELVGRA RVSPGCGWSV RETACLSKAY GQMWLLSYFH RRDLRTLGFA ICSAVPVDWV
PTGRTTWSIH ASGAWMTTED MLEVWNRVWI YDNPFMEDKT RVDEWRDTPY LPKSQDILCS
SLVGRGERAE WAKNIWGAVE KVRRMIGPEH YRDYLSSMDR HDLHWELKLE SSIF
