POLG_TBEVW
ID POLG_TBEVW Reviewed; 3414 AA.
AC P14336; Q88493;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 4.
DT 03-AUG-2022, entry version 194.
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 European subtype (strain Neudoerfl) (NEUV)
OS (Neudoerfl virus).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Flavivirus.
OX NCBI_TaxID=11088;
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], AND SEQUENCE REVISION.
RC STRAIN=Neudoerfl;
RX PubMed=7483260; DOI=10.1006/viro.1995.1557;
RA Wallner G., Mandl C.W., Kunz C., Heinz F.X.;
RT "The flavivirus 3'-noncoding region: extensive size heterogeneity
RT independent of evolutionary relationships among strains of tick-borne
RT encephalitis virus.";
RL Virology 213:169-178(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-779.
RC STRAIN=Neudoerfl;
RX PubMed=3413985; DOI=10.1016/0042-6822(88)90161-4;
RA Mandl C.W., Heinz F.X., Kunz C.;
RT "Sequence of the structural proteins of tick-borne encephalitis virus
RT (western subtype) and comparative analysis with other flaviviruses.";
RL Virology 166:197-205(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 767-3414.
RC STRAIN=Neudoerfl;
RX PubMed=2554575; DOI=10.1016/0042-6822(89)90246-8;
RA Mandl C.W., Heinz F.X., Stoeckl E., Kunz C.;
RT "Genome sequence of tick-borne encephalitis virus (Western subtype) and
RT comparative analysis of nonstructural proteins with other flaviviruses.";
RL Virology 173:291-301(1989).
RN [4]
RP PROTEIN SEQUENCE OF 2-18 AND 206-209.
RX PubMed=6305006; DOI=10.1016/s0042-6822(83)80020-8;
RA Boege U., Heinz F.X., Wengler G., Kunz C.;
RT "Amino acid compositions and amino-terminal sequences of the structural
RT proteins of a flavivirus, European Tick-Borne Encephalitis virus.";
RL Virology 126:651-657(1983).
RN [5]
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 [6]
RP FUSION REGION, AND MUTAGENESIS OF LEU-387.
RX PubMed=11287576; DOI=10.1128/jvi.75.9.4268-4275.2001;
RA Allison S.L., Schalich J., Stiasny K., Mandl C.W., Heinz F.X.;
RT "Mutational evidence for an internal fusion peptide in flavivirus envelope
RT protein E.";
RL J. Virol. 75:4268-4275(2001).
RN [7]
RP SUBUNIT (CAPSID PROTEIN C).
RX PubMed=15254179; DOI=10.1128/jvi.78.15.8078-8084.2004;
RA Kiermayr S., Kofler R.M., Mandl C.W., Messner P., Heinz F.X.;
RT "Isolation of capsid protein dimers from the tick-borne encephalitis
RT flavivirus and in vitro assembly of capsid-like particles.";
RL J. Virol. 78:8078-8084(2004).
RN [8]
RP TOPOLOGY (ENVELOPE PROTEIN E).
RX PubMed=17305426; DOI=10.1371/journal.ppat.0030020;
RA Stiasny K., Kossl C., Lepault J., Rey F.A., Heinz F.X.;
RT "Characterization of a structural intermediate of flavivirus membrane
RT fusion.";
RL PLoS Pathog. 3:E20-E20(2007).
RN [9] {ECO:0007744|PDB:1SVB}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 281-675, AND GLYCOSYLATION AT
RP ASN-434.
RX PubMed=7753193; DOI=10.1038/375291a0;
RA Rey F.A., Heinz F.X., Mandl C., Kunz C., Harrison S.C.;
RT "The envelope glycoprotein from tick-borne encephalitis virus at 2 A
RT resolution.";
RL Nature 375:291-298(1995).
RN [10] {ECO:0007744|PDB:1N6G, ECO:0007744|PDB:1NA4}
RP STRUCTURE BY ELECTRON MICROSCOPY (16.00 ANGSTROMS) OF 281-675.
RX PubMed=12773377; DOI=10.1093/emboj/cdg270;
RA Zhang Y., Corver J., Chipman P.R., Zhang W., Pletnev S.V., Sedlak D.,
RA Baker T.S., Strauss J.H., Kuhn R.J., Rossmann M.G.;
RT "Structures of immature flavivirus particles.";
RL EMBO J. 22:2604-2613(2003).
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 (PubMed:15254179). Interacts
CC (via N-terminus) with host EXOC1 (via C-terminus); this interaction
CC results in EXOC1 degradation through the proteasome degradation pathway
CC (By similarity). {ECO:0000250|UniProtKB:P17763,
CC ECO:0000269|PubMed:15254179}.
CC -!- SUBUNIT: [Protein prM]: Forms heterodimers with envelope protein E in
CC the endoplasmic reticulum and Golgi (By similarity).
CC {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 (By similarity).
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 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. {ECO:0000269|PubMed:2441520,
CC ECO:0000269|PubMed:7753193}.
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=1na4";
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DR EMBL; U27495; AAA86870.1; -; Genomic_RNA.
DR PIR; A31052; GNWVNE.
DR RefSeq; NP_043135.1; NC_001672.1.
DR PDB; 1N6G; EM; 16.00 A; A/B/C=281-675.
DR PDB; 1NA4; EM; -; A/B/C=281-675.
DR PDB; 1SVB; X-ray; 1.90 A; A=281-675.
DR PDB; 1URZ; X-ray; 2.70 A; A/B/C/D/E/F=281-681.
DR PDB; 6J5G; X-ray; 3.29 A; A=281-681.
DR PDB; 6S8C; X-ray; 2.57 A; A/B/C=281-684, A/B/C=707-728.
DR PDB; 7LSF; X-ray; 2.24 A; E=579-677.
DR PDB; 7LSG; X-ray; 1.86 A; C=581-677.
DR PDBsum; 1N6G; -.
DR PDBsum; 1NA4; -.
DR PDBsum; 1SVB; -.
DR PDBsum; 1URZ; -.
DR PDBsum; 6J5G; -.
DR PDBsum; 6S8C; -.
DR PDBsum; 7LSF; -.
DR PDBsum; 7LSG; -.
DR SMR; P14336; -.
DR TCDB; 1.G.3.1.1; the viral pore-forming membrane fusion protein-3 (vmfp3) family.
DR iPTMnet; P14336; -.
DR ABCD; P14336; 1 sequenced antibody.
DR GeneID; 1489719; -.
DR KEGG; vg:1489719; -.
DR EvolutionaryTrace; P14336; -.
DR Proteomes; UP000007402; 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; Direct protein sequencing;
KW Disulfide bond; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6305006"
FT CHAIN 2..3414
FT /note="Genome polyprotein"
FT /id="PRO_0000405175"
FT CHAIN 2..96
FT /note="Capsid protein C"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037815"
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_0000405176"
FT CHAIN 118..280
FT /note="Protein prM"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000405177"
FT CHAIN 118..205
FT /note="Peptide pr"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037816"
FT CHAIN 206..280
FT /note="Small envelope protein M"
FT /evidence="ECO:0000269|PubMed:6305006"
FT /id="PRO_0000037817"
FT CHAIN 281..776
FT /note="Envelope protein E"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037818"
FT CHAIN 777..1128
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037819"
FT CHAIN 1129..1358
FT /note="Non-structural protein 2A"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037820"
FT CHAIN 1359..1489
FT /note="Serine protease subunit NS2B"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037821"
FT CHAIN 1490..2110
FT /note="Serine protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037822"
FT CHAIN 2111..2236
FT /note="Non-structural protein 4A"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037823"
FT PEPTIDE 2237..2259
FT /note="Peptide 2k"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000405178"
FT CHAIN 2260..2511
FT /note="Non-structural protein 4B"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037824"
FT CHAIN 2512..3414
FT /note="RNA-directed RNA polymerase NS5"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT /id="PRO_0000037825"
FT TOPO_DOM 2..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="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 756..776
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 777..1132
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1133..1153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1154..1158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1159..1179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1180..1187
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1188..1208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1209..1293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1294..1314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1315..1327
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1328..1348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1349..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..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..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..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..391
FT /note="Fusion peptide"
FT /evidence="ECO:0000269|PubMed:11287576"
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:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:7753193"
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:0000269|PubMed:7753193"
FT DISULFID 340..401
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 340..396
FT /evidence="ECO:0000269|PubMed:7753193"
FT DISULFID 354..385
FT /evidence="ECO:0000269|PubMed:7753193"
FT DISULFID 372..401
FT /evidence="ECO:0000269|PubMed:7753193"
FT DISULFID 372..396
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 466..570
FT /evidence="ECO:0000269|PubMed:7753193"
FT DISULFID 587..618
FT /evidence="ECO:0000269|PubMed:7753193"
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 MUTAGEN 387
FT /note="L->D: Complete loss of envelope protein E fusion
FT activity."
FT /evidence="ECO:0000269|PubMed:11287576"
FT MUTAGEN 387
FT /note="L->F: About 50% loss of envelope protein E fusion
FT activity."
FT /evidence="ECO:0000269|PubMed:11287576"
FT MUTAGEN 387
FT /note="L->T: About 70% loss of envelope protein E fusion
FT activity."
FT /evidence="ECO:0000269|PubMed:11287576"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 318..332
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 334..352
FT /evidence="ECO:0007829|PDB:1SVB"
FT HELIX 363..366
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 370..380
FT /evidence="ECO:0007829|PDB:1SVB"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 389..401
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:1SVB"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 418..425
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:1SVB"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 460..467
FT /evidence="ECO:0007829|PDB:1SVB"
FT HELIX 468..470
FT /evidence="ECO:0007829|PDB:1SVB"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:6S8C"
FT STRAND 477..482
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:1SVB"
FT HELIX 497..501
FT /evidence="ECO:0007829|PDB:1SVB"
FT HELIX 518..521
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 529..533
FT /evidence="ECO:0007829|PDB:6S8C"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:1SVB"
FT HELIX 541..547
FT /evidence="ECO:0007829|PDB:1SVB"
FT TURN 548..550
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 553..557
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 567..573
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 591..600
FT /evidence="ECO:0007829|PDB:7LSG"
FT STRAND 602..604
FT /evidence="ECO:0007829|PDB:7LSG"
FT STRAND 606..612
FT /evidence="ECO:0007829|PDB:7LSG"
FT STRAND 614..619
FT /evidence="ECO:0007829|PDB:7LSG"
FT STRAND 622..626
FT /evidence="ECO:0007829|PDB:7LSG"
FT STRAND 629..633
FT /evidence="ECO:0007829|PDB:7LSG"
FT STRAND 636..641
FT /evidence="ECO:0007829|PDB:7LSG"
FT STRAND 643..645
FT /evidence="ECO:0007829|PDB:1SVB"
FT STRAND 651..655
FT /evidence="ECO:0007829|PDB:7LSG"
FT STRAND 658..665
FT /evidence="ECO:0007829|PDB:7LSG"
FT STRAND 668..674
FT /evidence="ECO:0007829|PDB:7LSG"
SQ SEQUENCE 3414 AA; 378322 MW; 35DBCE014B310B79 CRC64;
MVKKAILKGK GGGPPRRVSK ETATKTRQPR VQMPNGLVLM RMMGILWHAV AGTARNPVLK
AFWNSVPLKQ ATAALRKIKR TVSALMVGLQ KRGKRRSATD WMSWLLVITL LGMTLAATVR
KERDGSTVIR AEGKDAATQV RVENGTCVIL ATDMGSWCDD SLSYECVTID QGEEPVDVDC
FCRNVDGVYL EYGRCGKQEG SRTRRSVLIP SHAQGELTGR GHKWLEGDSL RTHLTRVEGW
VWKNKLLALA MVTVVWLTLE SVVTRVAVLV VLLCLAPVYA SRCTHLENRD FVTGTQGTTR
VTLVLELGGC VTITAEGKPS MDVWLDAIYQ ENPAKTREYC LHAKLSDTKV AARCPTMGPA
TLAEEHQGGT VCKRDQSDRG WGNHCGLFGK GSIVACVKAA CEAKKKATGH VYDANKIVYT
VKVEPHTGDY VAANETHSGR KTASFTISSE KTILTMGEYG DVSLLCRVAS GVDLAQTVIL
ELDKTVEHLP TAWQVHRDWF NDLALPWKHE GAQNWNNAER LVEFGAPHAV KMDVYNLGDQ
TGVLLKALAG VPVAHIEGTK YHLKSGHVTC EVGLEKLKMK GLTYTMCDKT KFTWKRAPTD
SGHDTVVMEV TFSGTKPCRI PVRAVAHGSP DVNVAMLITP NPTIENNGGG FIEMQLPPGD
NIIYVGELSH QWFQKGSSIG RVFQKTKKGI ERLTVIGEHA WDFGSAGGFL SSIGKAVHTV
LGGAFNSIFG GVGFLPKLLL GVALAWLGLN MRNPTMSMSF LLAGGLVLAM TLGVGADVGC
AVDTERMELR CGEGLVVWRE VSEWYDNYAY YPETPGALAS AIKETFEEGS CGVVPQNRLE
MAMWRSSVTE LNLALAEGEA NLTVVVDKFD PTDYRGGVPG LLKKGKDIKV SWKSWGHSMI
WSIPEAPRRF MVGTEGQSEC PLERRKTGVF TVAEFGVGLR TKVFLDFRQE PTHECDTGVM
GAAVKNGMAI HTDQSLWMRS MKNDTGTYIV ELLVTDLRNC SWPASHTIDN ADVVDSELFL
PASLAGPRSW YNRIPGYSEQ VKGPWKYTPI RVIREECPGT TVTINAKCDK RGASVRSTTE
SGKVIPEWCC RACTMPPVTF RTGTDCWYAM EIRPVHDQGG LVRSMVVADN GELLSEGGVP
GIVALFVVLE YIIRRRPSTG TTVVWGGIVV LALLVTGMVR IESLVRYVVA VGITFHLELG
PEIVALMLLQ AVFELRVGLL SAFALRRSLT VREMVTTYFL LLVLELGLPG ASLEEFWKWG
DALAMGALIF RACTAEGKTG AGLLLMALMT QQDVVTVHHG LVCFLSVASA CSVWRLLKGH
REQKGLTWVV PLAGLLGGEG SGIRLLAFWE LSAHRGRRSF SEPLTVVGVM LTLASGMMRH
TSQEALCALA VASFLLLMLV LGTRKMQLVA EWSGCVEWYP ELVNEGGEVS LRVRQDAMGN
FHLTELEKEE RMMAFWLIAG LAASAIHWSG ILGVMGLWTL TEMLRSSRRS DLVFSGQGGR
ERGDRPFEVK DGVYRIFSPG LFWGQNQVGV GYGSKGVLHT MWHVTRGAAL SIDDAVAGPY
WADVREDVVC YGGAWSLEEK WKGETVQVHA FPPGRAHEVH QCQPGELILD TGRKLGAIPI
DLVKGTSGSP ILNAQGVVVG LYGNGLKTNE TYVSSIAQGE AEKSRPNLPQ AVVGTGWTSK
GQITVLDMHP GSGKTHRVLP ELIRQCIDRR LRTLVLAPTR VVLKEMERAL NGKRVRFHSP
AVSDQQAGGA IVDVMCHATY VNRRLLPQGR QNWEVAIMDE AHWTDPHSIA ARGHLYTLAK
ENKCALVLMT ATPPGKSEPF PESNGAITSE ERQIPDGEWR DGFDWITEYE GRTAWFVPSI
AKGGAIARTL RQKGKSVICL NSKTFEKDYS RVRDEKPDFV VTTDISEMGA NLDVSRVIDG
RTNIKPEEVD GKVELTGTRR VTTASAAQRR GRVGRQDGRT DEYIYSGQCD DDDSGLVQWK
EAQILLDNIT TLRGPVATFY GPEQDKMPEV AGHFRLTEEK RKHFRHLLTH CDFTPWLAWH
VAANVSSVTD RSWTWEGPEA NAVDEASGDL VTFRSPNGAE RTLRPVWKDA RMFKEGRDIK
EFVAYASGRR SFGDVLTGMS GVPELLRHRC VSALDVFYTL MHEEPGSRAM RMAERDAPEA
FLTMVEMMVL GLATLGVIWC FVVRTSISRM MLGTLVLLAS LLLLWAGGVG YGNMAGVALI
FYTLLTVLQP EAGKQRSSDD NKLAYFLLTL CSLAGLVAAN EMGFLEKTKA DLSTALWSER
EEPRPWSEWT NVDIQPARSW GTYVLVVSLF TPYIIHQLQT KIQQLVNSAV ASGAQAMRDL
GGGAPFFGVA GHVMTLGVVS LIGATPTSLM VGVGLAALHL AIVVSGLEAE LTQRAHKVFF
SAMVRNPMVD GDVINPFGEG EAKPALYERK MSLVLATVLC LMSVVMNRTV ASITEASAVG
LAAAGQLLRP EADTLWTMPV ACGMSGVVRG SLWGFLPLGH RLWLRASGGR RGGSEGDTLG
DLWKRRLNNC TREEFFVYRR TGILETERDK ARELLRRGET NVGLAVSRGT AKLAWLEERG
YATLKGEVVD LGCGRGGWSY YAASRPAVMS VRAYTIGGKG HEAPKMVTSL GWNLIKFRSG
MDVFSMQPHR ADTVMCDIGE SSPDAAVEGE RTRKVILLME QWKNRNPTAA CVFKVLAPYR
PEVIEALHRF QLQWGGGLVR TPFSRNSTHE MYYSTAVTGN IVNSVNVQSR KLLARFGDQR
GPTKVPELDL GVGTRCVVLA EDKVKEQDVQ ERIRALREQY SETWHMDEEH PYRTWQYWGS
YRTAPTGSAA SLINGVVKLL SWPWNAREDV VRMAMTDTTA FGQQRVFKDK VDTKAQEPQP
GTRVIMRAVN DWILERLAQK SKPRMCSREE FIAKVKSNAA LGAWSDEQNR WASAREAVED
PAFWRLVDEE RERHLMGRCA HCVYNMMGKR EKKLGEFGVA KGSRAIWYMW LGSRFLEFEA
LGFLNEDHWA SRESSGAGVE GISLNYLGWH LKKLSTLNGG LFYADDTAGW DTKVTNADLE
DEEQILRYME GEHKQLATTI MQKAYHAKVV KVARPSRDGG CIMDVITRRD QRGSGQVVTY
ALNTLTNIKV QLIRMMEGEG VIEAADAHNP RLLRVERWLK EHGEERLGRM LVSGDDCVVR
PLDDRFGKAL YFLNDMAKTR KDIGEWEHSA GFSSWEEVPF CSHHFHELVM KDGRTLVVPC
RDQDELVGRA RISPGCGWSV RETACLSKAY GQMWLLSYFH RRDLRTLGLA INSAVPADWV
PTGRTTWSIH ASGAWMTTED MLDVWNRVWI LDNPFMQNKE RVMEWRDVPY LPKAQDMLCS
SLVGRRERAE WAKNIWGAVE KVRKMIGPEK FKDYLSCMDR HDLHWELRLE SSII
