POLG_USUV
ID POLG_USUV Reviewed; 3434 AA.
AC Q5WPU5;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
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 Usutu virus (USUV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Flavivirus.
OX NCBI_TaxID=64286;
OH NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OH NCBI_TaxID=41429; Anopheles maculipennis.
OH NCBI_TaxID=653291; Coquillettidia aurites.
OH NCBI_TaxID=864528; Culex neavei.
OH NCBI_TaxID=943103; Culex perexiguus.
OH NCBI_TaxID=7175; Culex pipiens (House mosquito).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=667564; Mansonia africana.
OH NCBI_TaxID=120870; Ochlerotatus caspius.
OH NCBI_TaxID=9187; Turdus merula (Common blackbird).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
RC STRAIN=Vienna 2001 {ECO:0000312|EMBL:AAS59402.1};
RX PubMed=12095429; DOI=10.3201/eid0807.020094;
RA Weissenbock H., Kolodziejek J., Url A., Lussy H., Rebel-Bauder B.,
RA Nowotny N.;
RT "Emergence of Usutu virus, an African mosquito-borne flavivirus of the
RT Japanese encephalitis virus group, central Europe.";
RL Emerg. Infect. Dis. 8:652-656(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
RC STRAIN=Vienna 2001 {ECO:0000312|EMBL:AAS59402.1};
RX PubMed=15464850; DOI=10.1016/j.virol.2004.08.005;
RA Bakonyi T., Gould E.A., Kolodziejek J., Weissenbock H., Nowotny N.;
RT "Complete genome analysis and molecular characterization of Usutu virus
RT that emerged in Austria in 2001: comparison with the South African strain
RT SAAR-1776 and other flaviviruses.";
RL Virology 328:301-310(2004).
CC -!- FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding
CC to the cell membrane and gathering the viral RNA into a nucleocapsid
CC that forms the core of a mature virus particle. During virus entry, may
CC induce genome penetration into the host cytoplasm after hemifusion
CC induced by the surface proteins. Can migrate to the cell nucleus where
CC it modulates host functions. Overcomes the anti-viral effects of host
CC EXOC1 by sequestering and degrading the latter through the proteasome
CC degradation pathway. {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering
CC with host Dicer. {ECO:0000250|UniProtKB:P03314}.
CC -!- FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope
CC proteins in trans-Golgi by binding to envelope protein E at pH6.0.
CC After virion release in extracellular space, gets dissociated from E
CC dimers. {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Protein prM]: Acts as a chaperone for envelope protein E
CC during intracellular virion assembly by masking and inactivating
CC envelope protein E fusion peptide. prM is the only viral peptide
CC matured by host furin in the trans-Golgi network probably to avoid
CC catastrophic activation of the viral fusion activity in acidic Golgi
CC compartment prior to virion release. prM-E cleavage is inefficient, and
CC many virions are only partially matured. These uncleaved prM would play
CC a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Small envelope protein M]: May play a role in virus budding.
CC Exerts cytotoxic effects by activating a mitochondrial apoptotic
CC pathway through M ectodomain. May display a viroporin activity.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and
CC mediates fusion between viral and cellular membranes. Envelope protein
CC is synthesized in the endoplasmic reticulum in the form of heterodimer
CC with protein prM. They play a role in virion budding in the ER, and the
CC newly formed immature particle is covered with 60 spikes composed of
CC heterodimer between precursor prM and envelope protein E. The virion is
CC transported to the Golgi apparatus where the low pH causes dissociation
CC of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is
CC inefficient, and many virions are only partially matured. These
CC uncleaved prM would play a role in immune evasion.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Non-structural protein 1]: Involved in immune evasion,
CC pathogenesis and viral replication. Once cleaved off the polyprotein,
CC is targeted to three destinations: the viral replication cycle, the
CC plasma membrane and the extracellular compartment. Essential for viral
CC replication. Required for formation of the replication complex and
CC recruitment of other non-structural proteins to the ER-derived membrane
CC structures. Excreted as a hexameric lipoparticle that plays a role
CC against host immune response. Antagonizing the complement function.
CC Binds to the host macrophages and dendritic cells. Inhibits signal
CC transduction originating from Toll-like receptor 3 (TLR3).
CC {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- FUNCTION: [Non-structural protein 2A]: Component of the viral RNA
CC replication complex that functions in virion assembly and antagonizes
CC the host alpha/beta interferon antiviral response.
CC {ECO:0000250|UniProtKB:P14335}.
CC -!- FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the
CC serine protease function of NS3. May have membrane-destabilizing
CC activity and form viroporins (By similarity).
CC {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}.
CC -!- FUNCTION: [Serine protease NS3]: Displays three enzymatic activities:
CC serine protease, NTPase and RNA helicase. NS3 serine protease, in
CC association with NS2B, performs its autocleavage and cleaves the
CC polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-
CC NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and
CC unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE-
CC ProRule:PRU00860}.
CC -!- FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of
CC the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy
CC during unwinding. {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 (-) RNA genome, and performs the capping of genomes in the
CC cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O
CC positions. Besides its role in RNA genome replication, also prevents
CC the establishment of cellular antiviral state by blocking the
CC interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host
CC TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-
CC STAT signaling pathway. {ECO:0000250|UniProtKB:Q9Q6P4}.
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 Evidence={ECO:0000250|UniProtKB:Q9Q6P4};
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 (By similarity). Interacts with envelope protein E (By
CC similarity). NS1 interacts with NS4B (By similarity). Interacts with
CC host complement protein CFH; this interaction leads to the degradation
CC of C3 (By similarity). {ECO:0000250|UniProtKB:Q9Q6P4}.
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). {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.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein C]: Virion
CC {ECO:0000250|UniProtKB:P17763}. Host nucleus
CC {ECO:0000250|UniProtKB:P17763}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region
CC {ECO:0000250|UniProtKB:P06935}.
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}.
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DR EMBL; AY453411; AAS59402.1; -; Genomic_RNA.
DR RefSeq; YP_164264.1; NC_006551.1.
DR PDB; 6A0P; X-ray; 2.00 A; A=294-699.
DR PDB; 6S92; X-ray; 1.93 A; A=591-693.
DR PDB; 6S93; X-ray; 1.67 A; A/B/C=591-693.
DR PDB; 6S94; X-ray; 1.79 A; A/B=591-693.
DR PDBsum; 6A0P; -.
DR PDBsum; 6S92; -.
DR PDBsum; 6S93; -.
DR PDBsum; 6S94; -.
DR SMR; Q5WPU5; -.
DR MEROPS; S07.003; -.
DR ABCD; Q5WPU5; 5 sequenced antibodies.
DR GeneID; 5075863; -.
DR KEGG; vg:5075863; -.
DR Proteomes; UP000170913; 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:0039574; P:suppression by virus of host JAK-STAT cascade via inhibition of host TYK2 activity; 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; 1.10.10.930; -; 1.
DR Gene3D; 1.10.8.970; -; 1.
DR Gene3D; 1.20.1280.260; -; 1.
DR Gene3D; 2.60.260.50; -; 1.
DR Gene3D; 2.60.40.350; -; 1.
DR Gene3D; 2.60.98.10; -; 1.
DR Gene3D; 3.30.387.10; -; 1.
DR Gene3D; 3.30.67.10; -; 1.
DR 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; IPR037172; Flavi_capsidC_sf.
DR InterPro; IPR027287; Flavi_E_Ig-like.
DR InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
DR InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
DR InterPro; IPR001157; Flavi_NS1.
DR InterPro; IPR000752; Flavi_NS2A.
DR InterPro; IPR000487; Flavi_NS2B.
DR InterPro; IPR000404; Flavi_NS4A.
DR InterPro; IPR001528; Flavi_NS4B.
DR InterPro; IPR002535; Flavi_propep.
DR InterPro; IPR038688; Flavi_propep_sf.
DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR InterPro; IPR001850; Flavivirus_NS3_S7.
DR InterPro; IPR014412; Gen_Poly_FLV.
DR InterPro; IPR011998; Glycoprot_cen/dimer.
DR InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR InterPro; IPR013756; GlyE_cen_dom_subdom2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR000208; RNA-dir_pol_flavivirus.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002877; 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; PF01002; Flavi_NS2B; 1.
DR Pfam; PF01350; Flavi_NS4A; 1.
DR Pfam; PF01349; Flavi_NS4B; 1.
DR Pfam; PF00972; Flavi_NS5; 1.
DR Pfam; PF01570; Flavi_propep; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF00949; Peptidase_S7; 1.
DR PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF101257; SSF101257; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; 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 Inhibition of host TYK2 by virus; Membrane; Metal-binding;
KW Methyltransferase; mRNA capping; mRNA processing; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Protease; RNA-binding;
KW RNA-directed RNA polymerase; S-adenosyl-L-methionine; Secreted;
KW Serine protease; Suppressor of RNA silencing; Transcription;
KW Transcription regulation; Transferase; Transmembrane; Transmembrane helix;
KW 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..3434
FT /note="Genome polyprotein"
FT /id="PRO_0000441561"
FT CHAIN 1..104
FT /note="Capsid protein C"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441562"
FT PROPEP 105..126
FT /note="ER anchor for the capsid protein C, removed in
FT mature form by serine protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441563"
FT CHAIN 127..293
FT /note="Protein prM"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441564"
FT CHAIN 127..218
FT /note="Peptide pr"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441565"
FT CHAIN 219..293
FT /note="Small envelope protein M"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441566"
FT CHAIN 294..793
FT /note="Envelope protein E"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441567"
FT CHAIN 794..1145
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441568"
FT CHAIN 1146..1372
FT /note="Non-structural protein 2A"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441569"
FT CHAIN 1373..1503
FT /note="Serine protease subunit NS2B"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441570"
FT CHAIN 1504..2122
FT /note="Serine protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441571"
FT CHAIN 2123..2248
FT /note="Non-structural protein 4A"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441572"
FT PEPTIDE 2249..2271
FT /note="Peptide 2k"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441573"
FT CHAIN 2272..2529
FT /note="Non-structural protein 4B"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441574"
FT CHAIN 2530..3434
FT /note="RNA-directed RNA polymerase NS5"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441575"
FT TOPO_DOM 1..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..293
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 294..745
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 746..766
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 767..772
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 794..1218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1219..1239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1240..1249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1250..1270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1271..1286
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1287..1307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1309..1329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1330..1340
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1341..1361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1362..1373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1374..1394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1395..1397
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1398..1418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1419..1475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1476..1496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1497..2173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2174..2194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2195..2198
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 2199..2219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2220
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2221..2241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2242..2256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2257..2277
FT /note="Helical; Note=Signal for NS4B"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2278..2313
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 2314..2334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2335..2368
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2369..2389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2390..2446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2447..2467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2468..2471
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2472..2492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2493..3434
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1504..1681
FT /note="Peptidase S7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT DOMAIN 1684..1840
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1851..2016
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2530..2795
FT /note="mRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT DOMAIN 3059..3211
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 2..15
FT /note="Interaction with host EXOC1"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT REGION 37..72
FT /note="Hydrophobic; homodimerization of capsid protein C"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT REGION 391..404
FT /note="Fusion peptide"
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT REGION 1426..1465
FT /note="Interacts with and activates NS3 protease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00859"
FT REGION 1688..1691
FT /note="Important for RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P14340"
FT REGION 1956..1980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2167..2171
FT /note="Regulates the ATPase activity of NS3 helicase"
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT REGION 2567..2587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1788..1791
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT ACT_SITE 1554
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 1578
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 1638
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 2590
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2675
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2711
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2747
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT BINDING 1697..1704
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 2585
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 2633
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2634
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2660
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2661
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2676
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2749
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2969
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2973
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2978
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 2981
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 104..105
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 126..127
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 218..219
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 293..294
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 793..794
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1145..1146
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1372..1373
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1503..1504
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1961
FT /note="Involved in NS3 ATPase and RTPase activities"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 1964
FT /note="Involved in NS3 ATPase and RTPase activities"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 2122..2123
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 2248..2249
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 2271..2272
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 2529..2530
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 2542
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2545
FT /note="mRNA cap binding; via carbonyl oxygen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2546
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2548
FT /note="mRNA cap binding; via carbonyl oxygen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2553
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2557
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2590
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2675
FT /note="Essential for 2'-O-methyltransferase and N-7
FT methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2679
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2711
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2742
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2744
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2747
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT MOD_RES 2585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT CARBOHYD 923
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT CARBOHYD 968
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT CARBOHYD 1000
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 296..323
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT DISULFID 353..414
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 353..409
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT DISULFID 367..398
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT DISULFID 385..414
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT DISULFID 385..409
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 483..580
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT DISULFID 597..628
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT DISULFID 797..808
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 848..936
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 972..1016
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1073..1122
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1084..1106
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1084..1105
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 1105..1109
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1106..1109
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 334..345
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 347..366
FT /evidence="ECO:0007829|PDB:6A0P"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 383..392
FT /evidence="ECO:0007829|PDB:6A0P"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 402..422
FT /evidence="ECO:0007829|PDB:6A0P"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 428..436
FT /evidence="ECO:0007829|PDB:6A0P"
FT TURN 442..446
FT /evidence="ECO:0007829|PDB:6A0P"
FT HELIX 448..453
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 456..462
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 468..472
FT /evidence="ECO:0007829|PDB:6A0P"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 477..486
FT /evidence="ECO:0007829|PDB:6A0P"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:6A0P"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 494..499
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 502..507
FT /evidence="ECO:0007829|PDB:6A0P"
FT HELIX 508..512
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:6A0P"
FT TURN 529..532
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 533..535
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 545..547
FT /evidence="ECO:0007829|PDB:6A0P"
FT HELIX 552..559
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 562..565
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 575..583
FT /evidence="ECO:0007829|PDB:6A0P"
FT STRAND 601..609
FT /evidence="ECO:0007829|PDB:6S93"
FT STRAND 611..613
FT /evidence="ECO:0007829|PDB:6S93"
FT STRAND 615..621
FT /evidence="ECO:0007829|PDB:6S93"
FT STRAND 627..629
FT /evidence="ECO:0007829|PDB:6S93"
FT STRAND 632..637
FT /evidence="ECO:0007829|PDB:6S93"
FT STRAND 640..649
FT /evidence="ECO:0007829|PDB:6S93"
FT STRAND 662..668
FT /evidence="ECO:0007829|PDB:6S93"
FT STRAND 671..679
FT /evidence="ECO:0007829|PDB:6S93"
FT HELIX 681..683
FT /evidence="ECO:0007829|PDB:6S93"
FT STRAND 685..691
FT /evidence="ECO:0007829|PDB:6S93"
SQ SEQUENCE 3434 AA; 380313 MW; F05864FD02780251 CRC64;
MSKKPGGPGR NRAINMLKRG IPRVFPLVGV KRVVMGLLDG RGPVRFVLAL MTFFKFTALA
PTKALLGRWK RINKTTAMKH LTSFKKELGT MINVVNNRGT KKKRGNNGPG LVMIITLMTV
VSMVSSLKLS NFQGKVMMTI NATDMADVIV VPTQHGKNQC WIRAMDVGYM CDDTITYECP
KLDAGNDPED IDCWCDKQPM YVHYGRCTRT RHSKRSRRSI AVQTHGESML ANKKDAWLDS
TKASRYLMKT ENWIIRNPGY AFVAVLLGWM LGSNNGQRVV FVVLLLLVAP AYSFNCLGMS
NRDFLEGVSG ATWVDVVLEG DSCITIMAKD KPTIDIKMME TEATNLAEVR SYCYLATVSD
VSTVSNCPTT GEAHNPKRAE DTYVCKSGVT DRGWGNGCGL FGKGSIDTCA NFTCSLKAMG
RMIQPENVKY EVGIFIHGST SSDTHGNYSS QLGASQAGRF TITPNSPAIT VKMGDYGEIS
VECEPRNGLN TEAYYIMSVG TKHFLVHREW FNDLALPWTS PASSNWRNRE ILLEFEEPHA
TKQSVVALGS QEGALHQALA GAVPVSFSGS VKLTSGHLKC RVKMEKLTLK GTTYGMCTEK
FSFAKNPADT GHGTVVLELQ YTGSDGPCKI PISIVASLSD LTPIGRMVTA NPYVASSEAN
AKVLVEMEPP FGDSYIVVGR GDKQINHHWH KAGSSIGKAF ITTIKGAQRL AALGDTAWDF
GSVGGIFNSV GKAVHQVFGG AFRTLFGGMS WITQGLMGAL LLWMGVNARD RSIALVMLAT
GGVLLFLATN VHADSGCAID VGRRELRCGQ GIFIHNDVEA WVDRYKFMPE TPKQLAKVIE
QAHAKGICGL RSVSRLEHVM WENIRDELNT LLRENAVDLS VVVEKPKGMY KSAPQRLALT
SEEFEIGWKA WGKSLVFAPE LANHTFVVDG PETKECPDAK RAWNSLEIED FGFGIMSTRV
WLKVREHNTT DCDSSIIGTA VKGDIAVHSD LSYWIESHKN TTWRLERAVF GEIKSCTWPE
THTLWSDGVV ESDLVVPVTL AGPKSNHNRR EGYKVQSQGP WDEEDIVLDF DYCPGTTVTI
TEACGKRGPS IRTTTSSGRL VTDWCCRSCT LPPLRYRTKN GCWYGMEIRP MKHDETTLVK
SSVSAHRSDM IDPFQLGLLV MFLATQEVLR KRWTARLTVP AIVGALLVLI LGGITYTDLL
RYVLLVGAAF AEANSGGDVV HLALIAAFKI QPGFLAMTFL RGKWTNQENI LLALGAAFFQ
MAATDLNFSL PGILNATATA WMLLRAATQP STSAIVMPLL CLLAPGMRLL YLDTYRITLI
IIGICSLIGE RRRAAAKKKG AVLLGLALTS TGQFSASVMA AGLMACNPNK KRGWPATEVL
TAVGLMFAIV GGLAELDVDS MSIPFVLAGL MAVSYTISGK STDLWLERAA DITWETDAAI
TGTSQRLDVK LDDDGDFHLI NDPGVPWKIW VIRMTALGFA AWTPWAIIPA GIGYWLTVKY
AKRGGVFWDT PAPRTYPKGD TSPGVYRIMS RYILGTYQAG VGVMYEGVLH TLWHTTRGAA
IRSGEGRLTP YWGSVKEDRI TYGGPWKFDR KWNGLDDVQL IIVAPGKAAI NIQTKPGIFK
TPQGEIGAVS LDYPEGTSGS PILDKNGDIV GLYGNGVILG NGSYVSAIVQ GEREEEPVPE
AYNADMLRKK QLTVLDLHPG AGKTRRILPQ IIKDAIQRRL RTAVLAPTRV VAAEMAEALK
GLPVRYLTPA VNREHSGTEI VDVMCHATLT HRLMSPLRAP NYNLFVMDEA HFTDPASIAA
RGYIATKVEL GEAAAIFMTA TPPGTHDPFP DTNAPVTDIQ AEVPDRAWSS GFEWITEYTG
KTVWFVASVK MGNEIAQCLQ RAGKKVIQLN RKSYDTEYPK CKNGDWDFVI TTDISEMGAN
FGASRVIDCR KSVKPTILEE GEGRVILSNP SPITSASAAQ RRGRVGRNPS QIGDEYHYGG
GTSEDDTIAA HWTEAKIMLD NIHLPNGLVA QMYGPERDKA FTMDGEYRLR GEERKTFLEL
LRTADLPVWL AYKVASNGIQ YTDRKWCFDG PRSNIILEDN NEVEIVTRTG ERKMLKPRWL
DARVYADHQS LKWFKDFAAG KRSAVGFLEV LGRMPEHFAG KTREAFDTMY LVATAEKGGK
AHRMALEELP DALETITLIV ALAVMTAGVF LLLVQRRGIG KLGLGGMVLG LATFFLWMAD
VSGTKIAGTL LLALLMMIVL IPEPEKQRSQ TDNQLAVFLI CVLLVVGVVA ANEYGMLERT
KSDLGKIFSS TRQPQSALPL PSMNALALDL RPATAWALYG GSTVVLTPLI KHLVTSEYIT
TSLASISAQA GSLFNLPRGL PFTELDFTVV LVFLGCWGQV SLTTLITAAA LATLHYGYML
PGWQAEALRA AQRRTAAGIM KNAVVDGLVA TDVPELERTT PLMQKKVGQI LLIGVSAAAL
LVNPCVTTVR EAGILISAAL LTLWDNGAIA VWNSTTATGL CHVIRGNWLA GASIAWTLIK
NADKPACKRG RPGGRTLGEQ WKEKLNGLSK EDFLKYRKEA ITEVDRSAAR KARRDGNKTG
GHPVSRGSAK LRWMVERQFV KPIGKVVDLG CGRGGWSYYA ATLKGVQEVR GYTKGGPGHE
EPMLMQSYGW NLVTMKSGVD VYYKPSEPCD TLFCDIGESS SSAEVEEQRT LRILEMVSDW
LQRGPREFCI KVLCPYMPRV MERLEVLQRR YGGGLVRVPL SRNSNHEMYW VSGAAGNIVH
AVNMTSQVLI GRMEKRTWHG PKYEEDVNLG SGTRAVGKPQ PHTNQEKIKA RIQRLKEEYA
ATWHHDKDHP YRTWTYHGSY EVKPTGSASS LVNGVVRLMS KPWDAILNVT TMAMTDTTPF
GQQRVFKEKV DTKAPEPPSG VREVMDETTN WLWAFLAREK KPRLCTREEF KRKVNSNAAL
GAMFEEQNQW SSAREAVEDP RFWEMVDEER ENHLKGECHT CIYNMMGKRE KKLGEFGKAK
GSRAIWFMWL GARFLEFEAL GFLNEDHWLG RKNSGGGVEG LGVQKLGYIL REMSHHSGGK
MYADDTAGWD TRITRADLDN EAKVLELMEG EHRQLARAII ELTYKHKVVK VMRPGTDGKT
VMDVISREDQ RGSGQVVTYA LNTFTNIAVQ LIRLMEAEGV IGQEHLESLP RKTKYAVRTW
LFENGEERVT RMAVSGDDCV VKPLDDRFAN ALHFLNSMSK VRKDVPEWKP SSGWHDWQQV
PFCSNHFQEL IMKDGRTLVV PCRGQDELIG RARVSPGSGW NVRDTACLAK AYAQMWLLLY
FHRRDLRLMA NAICSAVPSN WVPTGRTSWS VHATGEWMTT DDMLEVWNKV WIQDNEWMLD
KTPVQSWTDI PYTGKREDIW CGSLIGTRTR ATWAENIYAA INQVRAIIGQ EKYRDYMLSL
RRYEEVNVQE DRVL
