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POLG_TBEVH
ID   POLG_TBEVH              Reviewed;        3414 AA.
AC   Q01299;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 161.
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 (strain Hypr) (TBEV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Flavivirus.
OX   NCBI_TaxID=70733;
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].
RA   Wallner G., Mandl C.W., Ecker M., Holzmann H., Stiasny K., Kunz C.,
RA   Heinz F.X.;
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 3357-3414.
RX   PubMed=1712858; DOI=10.1128/jvi.65.8.4070-4077.1991;
RA   Mandl C.W., Kunz C., Heinz F.X.;
RT   "Presence of poly(A) in a flavivirus: significant differences between the
RT   3' noncoding regions of the genomic RNAs of tick-borne encephalitis virus
RT   strains.";
RL   J. Virol. 65:4070-4077(1991).
RN   [3]
RP   FUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), INTERACTION WITH HUMAN SCRIB
RP   (RNA-DIRECTED RNA POLYMERASE NS5), AND MUTAGENESIS OF 2733-TYR-SER-2734.
RX   PubMed=18042258; DOI=10.1111/j.1462-5822.2007.01076.x;
RA   Werme K., Wigerius M., Johansson M.;
RT   "Tick-borne encephalitis virus NS5 associates with membrane protein
RT   scribble and impairs interferon-stimulated JAK-STAT signalling.";
RL   Cell. Microbiol. 10:696-712(2008).
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       (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:18042258). Inhibits host TYK2 and STAT2 phosphorylation,
CC       thereby preventing activation of JAK-STAT signaling pathway
CC       (PubMed:18042258). {ECO:0000250|UniProtKB:P17763,
CC       ECO:0000269|PubMed:18042258}.
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 (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. Interacts with
CC       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). {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.
CC       Interacts with NS4B (By similarity). Interacts with unphosphorylated
CC       RNA-directed RNA polymerase NS5; this interaction stimulates RNA-
CC       directed RNA polymerase NS5 guanylyltransferase activity (By
CC       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 (By similarity).
CC       Interacts with host STAT2; this interaction inhibits the
CC       phosphorylation of the latter, and, when all viral proteins are present
CC       (polyprotein), targets STAT2 for degradation (By similarity). Interacts
CC       with serine protease NS3 (By similarity). Interacts with host SCRIB;
CC       this interaction targets NS5 to the cell membrane periphery and
CC       nucleus, thereby allowing efficient host nuclear STAT1 inhibition
CC       (PubMed:18042258). {ECO:0000250|UniProtKB:P17763,
CC       ECO:0000269|PubMed:18042258}.
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   -!- MISCELLANEOUS: The non-structural protein NS1 presents 2. alternative
CC       cleavage sites for its C-terminus (either at position 1128 or at 1190),
CC       which may define a soluble or a membrane-bound form of NS1.
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; U39292; AAB53095.1; -; Genomic_RNA.
DR   EMBL; M76660; AAA47904.1; -; Genomic_RNA.
DR   PDB; 5O6A; EM; 3.90 A; A/B/C/D=281-776, D/E/F=206-280.
DR   PDB; 5O6V; EM; 3.90 A; A/B/C/D=281-776, D/E/F=206-280.
DR   PDB; 7JNO; X-ray; 1.95 A; A=1676-2110.
DR   PDBsum; 5O6A; -.
DR   PDBsum; 5O6V; -.
DR   PDBsum; 7JNO; -.
DR   SMR; Q01299; -.
DR   ABCD; Q01299; 5 sequenced antibodies.
DR   BRENDA; 2.7.7.48; 17704.
DR   Proteomes; UP000007400; 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; 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; IDA:UniProtKB.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   CDD; cd20761; capping_2-OMTase_Flaviviridae; 1.
DR   CDD; cd12149; Flavi_E_C; 1.
DR   Gene3D; 1.10.8.970; -; 1.
DR   Gene3D; 1.20.1280.260; -; 1.
DR   Gene3D; 2.60.260.50; -; 1.
DR   Gene3D; 2.60.40.350; -; 1.
DR   Gene3D; 2.60.98.10; -; 1.
DR   Gene3D; 3.30.387.10; -; 1.
DR   Gene3D; 3.30.67.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011492; DEAD_Flavivir.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
DR   InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
DR   InterPro; IPR001122; Flavi_capsidC.
DR   InterPro; IPR027287; Flavi_E_Ig-like.
DR   InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
DR   InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
DR   InterPro; IPR001157; Flavi_NS1.
DR   InterPro; IPR000752; Flavi_NS2A.
DR   InterPro; IPR000487; Flavi_NS2B.
DR   InterPro; IPR000404; Flavi_NS4A.
DR   InterPro; IPR001528; Flavi_NS4B.
DR   InterPro; IPR002535; Flavi_propep.
DR   InterPro; IPR038688; Flavi_propep_sf.
DR   InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR   InterPro; IPR001850; Flavivirus_NS3_S7.
DR   InterPro; IPR014412; Gen_Poly_FLV.
DR   InterPro; IPR011998; Glycoprot_cen/dimer.
DR   InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR   InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR   InterPro; IPR013756; GlyE_cen_dom_subdom2.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR000208; RNA-dir_pol_flavivirus.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01003; Flavi_capsid; 1.
DR   Pfam; PF07652; Flavi_DEAD; 1.
DR   Pfam; PF02832; Flavi_glycop_C; 1.
DR   Pfam; PF00869; Flavi_glycoprot; 1.
DR   Pfam; PF00948; Flavi_NS1; 1.
DR   Pfam; PF01005; Flavi_NS2A; 1.
DR   Pfam; PF01350; Flavi_NS4A; 1.
DR   Pfam; PF01349; Flavi_NS4B; 1.
DR   Pfam; PF00972; Flavi_NS5; 1.
DR   Pfam; PF01570; Flavi_propep; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF00949; Peptidase_S7; 1.
DR   PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   SUPFAM; SSF56983; SSF56983; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   TIGRFAMs; TIGR04240; flavi_E_stem; 1.
DR   PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
DR   PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activation of host autophagy by virus; ATP-binding;
KW   Capsid protein; Clathrin-mediated endocytosis of virus by host;
KW   Cleavage on pair of basic residues; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
KW   Host cytoplasm; Host endoplasmic reticulum; Host membrane; Host nucleus;
KW   Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host STAT1 by virus; Inhibition of host STAT2 by virus;
KW   Membrane; Metal-binding; Methyltransferase; mRNA capping; mRNA processing;
KW   Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW   Phosphoprotein; Protease; RNA-binding; RNA-directed RNA polymerase;
KW   S-adenosyl-L-methionine; Secreted; Serine protease;
KW   Suppressor of RNA silencing; Transcription; Transcription regulation;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Viral attachment to host cell; Viral envelope protein; Viral immunoevasion;
KW   Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW   Virus endocytosis by host; Virus entry into host cell; Zinc.
FT   CHAIN           1..3414
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000405167"
FT   CHAIN           1..96
FT                   /note="Capsid protein C"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT                   /id="PRO_0000037793"
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_0000405168"
FT   CHAIN           118..280
FT                   /note="Protein prM"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000405169"
FT   CHAIN           118..205
FT                   /note="Peptide pr"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000037794"
FT   CHAIN           206..280
FT                   /note="Small envelope protein M"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000037795"
FT   CHAIN           281..776
FT                   /note="Envelope protein E"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000037796"
FT   CHAIN           777..1128
FT                   /note="Non-structural protein 1"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT                   /id="PRO_0000037797"
FT   CHAIN           1129..1358
FT                   /note="Non-structural protein 2A"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000037798"
FT   CHAIN           1359..1489
FT                   /note="Serine protease subunit NS2B"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT                   /id="PRO_0000037799"
FT   CHAIN           1490..2110
FT                   /note="Serine protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT                   /id="PRO_0000037800"
FT   CHAIN           2111..2236
FT                   /note="Non-structural protein 4A"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT                   /id="PRO_0000037801"
FT   PEPTIDE         2237..2259
FT                   /note="Peptide 2k"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT                   /id="PRO_0000405170"
FT   CHAIN           2260..2511
FT                   /note="Non-structural protein 4B"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT                   /id="PRO_0000037802"
FT   CHAIN           2512..3414
FT                   /note="RNA-directed RNA polymerase NS5"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT                   /id="PRO_0000037803"
FT   TOPO_DOM        1..98
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..242
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        281..727
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        728..748
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        749..755
FT                   /note="Extracellular"
FT   TRANSMEM        756..776
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
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..1377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1378..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: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:0000269|PubMed:18042258"
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:0000250|UniProtKB:P14336"
FT   DISULFID        780..791
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        831..920
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        955..1000
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        1057..1106
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        1068..1090
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        1089..1093
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   MUTAGEN         2733..2734
FT                   /note="YS->AA: Relocalizes RNA-directed RNA polymerase NS5
FT                   away from the host cell membrane and nucleus. Reduced JAK-
FT                   STAT signalling inhibition and IFN inhibition."
FT                   /evidence="ECO:0000269|PubMed:18042258"
FT   STRAND          1683..1686
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   TURN            1694..1697
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   HELIX           1698..1708
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          1713..1719
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   HELIX           1720..1729
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   TURN            1730..1732
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          1735..1737
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          1752..1756
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   HELIX           1757..1764
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          1774..1780
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   HELIX           1786..1800
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          1805..1809
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          1824..1831
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   HELIX           1844..1848
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          1853..1856
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   HELIX           1860..1872
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          1877..1881
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   TURN            1882..1884
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   HELIX           1885..1895
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          1898..1902
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   HELIX           1904..1907
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          1915..1919
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          1922..1924
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          1927..1929
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          1932..1934
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          1937..1940
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   HELIX           1943..1950
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          1960..1965
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   HELIX           1977..1987
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          1992..1994
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   HELIX           2001..2006
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   TURN            2011..2014
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   HELIX           2018..2030
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   HELIX           2035..2044
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   HELIX           2052..2054
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   HELIX           2059..2061
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          2068..2070
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          2072..2074
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   STRAND          2080..2082
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   HELIX           2090..2093
FT                   /evidence="ECO:0007829|PDB:7JNO"
FT   HELIX           2099..2106
FT                   /evidence="ECO:0007829|PDB:7JNO"
SQ   SEQUENCE   3414 AA;  378545 MW;  EC0B1A5325A08C19 CRC64;
     MVKKAILKGK GGGPPRRVSK ETATKTRQPR VQMPNGLVLM RMMGILWHAV AGTARNPVLK
     AFWNSVPLKQ ATAALRKIKR TVSALMVGLQ KRGKRRSATD WMSWLLVITL LGMTIAATVR
     KERDGSTVIR AEGKDAATQV RVENGTCVIL ATDMGSWCDD SLSYECVTID QGEEPVDVDC
     FCRNVDGVYL EYGRCGKQEG SRTRRSVLIP SHAQGELTGR GHKWLEGDSL RTHLTRVEGW
     VWKNRLLALA MVTVVWLTLE SVVTRVAVLV VLLCLAPVYA SRCTHLENRD FVTGTQGTTR
     VTLVLELGGC VTITAEGKPS MDVWLDAIYQ ENPAQTREYC LHAKLSDTKV AARCPTMGPA
     TLAEEHQGGT VCKRDQSDRG WGNHCGLFGK GSIVACVKAA CEAKKKATGH VYDANKIVYT
     VKVEPHTGDY VAANETHSGR KTASFTVSSE KTILTMGEYG DVSLLCRVAS GVDLAQTVIL
     ELDKTVEHLP TAWQVHRDWF NDLALPWKHE GARNWNNAER LVEFGAPHAV KMDVYNLGDQ
     TGVLLKALAG VPVAHIEGTK YHLKSGHVTC EVGLEKLKMK GLTYTMCDKT KFTWKRAPTD
     SGHDTVVMEV TFSGTKPCRI PVRAVAHGSP DVNVAMLITP NPTIENNGGG FIEMQLPPGD
     NIIYVGELSY QWFQKGSSIG RVFQKTKKGI ERLTVIGEHA WDFGSAGGFL SSIGKALHTV
     LGGAFNSIFG GVGFLPKLLL GVALAWLGLN MRNPTMSMSF LLAGVLVLAM TLGVGADVGC
     AVDTERMELR CGEGLVVWRE VSEWYDNYAY YPETPGALAS AIKETFEEGS CGVVPQNRLE
     MAMWRSSVTE LNLALAEGEA NLTVMVDKFD PTDYRGGVPG LLKKGKDIKV SWKSWGHSMI
     WSIPEAPRRF MVGTEGQSEC PLERRKTGVF TVAEFGVGLR TKVFLDFRQE PTHECDTGVM
     GAAVKNGMAI HTDQSLWMRS MKNDTGTYIV ELLVTDLRNC SWPASHTIDN ADVVDSELFL
     PASLAGPRSW YNRIPGYSEQ VKGPWKHTPI RVIREECPGT TVTINAKCDK RGASVRSTTE
     SGKVIPEWCC RACTMPPVTF RTGTDCWYAM EIRPVHDQGG LVRSMVVADN GELLSEGGVP
     GIVALFVVLE YIIRRRPSTG STVVWGGIVV LALLVTGMVR MESLVRYVVA VGITFHLELG
     PEIVALMLLQ AVFELRVGLL SAFALRRSLT VREMVTTYFL LLVLELGLPS ANLEDFWKWG
     DALAMGALIF RACTAEGKTG AGLLLMALMT QQDVVTVHHG LVCFLSAASA CSIWRLLRGH
     REQKGLTWIV PLARLLGGEG SGIRLLAFWE LSAHRGRRSF SEPLTVVGVM LTLASGMMRH
     TSQEALCALA VASFLLLMLV LGTRKMQLVA EWSGCVEWHP ELVNEGGEVS LRVRQDAMGN
     FHLTELEKEE RMMAFWLIAG LAASAIHWSG IIGVMGLWTL TKMLRSSRRS DLVFSGQGGR
     ERGDRPFEVK DGVYRIFSPG LFWGQNQVGV GYGSKGVLHT MWHVTRGAAL SIDDAVAGPY
     WADVREDVVC YGGAWSLEEK WKGETVQVHA FPPGKAHEVH QCQPGELILD TGRKLGAIPI
     DLVKGTSGSP ILNAQGVVVG LYGNGLKTNE TYVSSIAQGE AEKSRPNLPQ AVVGTGWTSK
     GQITVLDMHP GSGKTHRVLP ELIRQCIDRR LRTLVLAPTR VVLKEMERAL NGKRVRFHSP
     AVSDQQAGGA IVDVMCHATY VNRRLLPQGR QNWEVAIMDE AHWTDPHSIA ARGHLYTLAK
     ENKCALVLMT ATPPGKSEPF PESNGAITSE ERQIPNGEWR DGFDWITEYE GRTAWFVPSI
     AKGGAIARTL RQKGKSVICL NSKTFEKDYS RVRDEKPDFV VTTDISEMGA NLDVSRVIDG
     RTNIKPEEVD GKVELTGTRR VTTASAAQRR GRVGRQDGRT DEYIYSGQCD DDDSGLVQWK
     EAQILLDNIT TLRGPVATFY GPEQDKMPEV AGHFRLTEEK RKHFRHLLTH CDFTPWLAWH
     VAANVSSVTD RSWTWEGPEA NAVDEASGGL VTFRSPNGAE RTLRPVWKDA RMFKEGRDIK
     EFVAYASGRR SFGDVLTGMS GVPELLRHRC VSALDVFYTL MHEKPDSRAM RMAERDAPEA
     FLTMVEMMVL GLATLGVIWC FVVRTSISRM MLGTLVLLAS LLLLWAGGVG YGNMAGVALI
     FYTLLTVLQP EAGKQRSSDD NKLAYFLLTL CSLAGLVAAN EMGFLEKTKA DLSTVLWSER
     EEPRPWSEWT NVDIQPARSW GTYVLVVSLF TPYIIHQLQT KIQQLVNSAV ASGAQAMRDL
     GGGAPFFGVA GHVMTLGVVS LIGATPTSLM VGVGLAALHL AIVVSGLEAE LTQRAHKVFF
     SAMVRNPMVD GDVINPFGEG EAKPALYERR MSLVLAIVLC LMSVVMNRTV ASITEASAVG
     LAAAGQLLRP EADTLWTMPV ACGMSGVVRG SLWGFLPLGH RLWLRASGGR RGGSEGDTLG
     DLWKRRLNNC TREEFFVYRR TGILETERDK ARELLRRGET NMGLAVSRGT AKLAWLEERG
     YATLKGEVVD LGCGRGGWSY YAASRPAVMS VRAYTIGGRG HEAPKMVTSL GWNLIKFRSG
     MDVFSMQPHR ADTVMCDIGE SSPDAAVEGE RTRKVILLME QWKNRNPTAA CVFKVLAPYR
     PEVIEALHRF QLQWGGGLVR TPFSRNSTHE MYYSTAVTGN IVNSVNVQSR KLLARFGDQR
     GPTRVPELDL GVGTRCVVLA EDKVKEQDVQ ERIKALREQY SETWHMDEEH PYRTWQYWGS
     YRTAPTGSAA SLINGVVKLL SWPWNAREDV VRMAMTDTTA FGQQRVFKDK VDTKAQEPQP
     GTRVIMRAVN DWILERLAQK SKPRMCSREE FIAKVKSNAA LGAWSDEQNR WASAREAVED
     PAFWHLVDEE 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 GLSSWEEVPF CSHHFHELVM KDGRTLVVPC
     RDQDELVGRA RISPGCGWSV RETACLSKAY GQMWLLSYFH RRDLRTLGLA INSAVPVDWV
     PTGRTTWSIH ASGAWMTTED MLDVWNRVWI LDNPFMQNKG KVMEWRDVPY LPKAQDMLCS
     SLVGRKERAE WAKNIWGAVE KVRKMIGPEK FKDYLSCMDR HDLHWELRLE SSII
 
 
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