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POLG_POWVL
ID   POLG_POWVL              Reviewed;        3415 AA.
AC   Q04538;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Peptide 2k;
DE   Contains:
DE     RecName: Full=Capsid protein C;
DE     AltName: Full=Core protein;
DE   Contains:
DE     RecName: Full=Protein prM;
DE   Contains:
DE     RecName: Full=Peptide pr;
DE   Contains:
DE     RecName: Full=Small envelope protein M;
DE     AltName: Full=Matrix protein;
DE   Contains:
DE     RecName: Full=Envelope protein E;
DE   Contains:
DE     RecName: Full=Non-structural protein 1;
DE              Short=NS1;
DE   Contains:
DE     RecName: Full=Non-structural protein 2A;
DE              Short=NS2A;
DE   Contains:
DE     RecName: Full=Serine protease subunit NS2B;
DE     AltName: Full=Flavivirin protease NS2B regulatory subunit;
DE     AltName: Full=Non-structural protein 2B;
DE   Contains:
DE     RecName: Full=Serine protease NS3;
DE              EC=3.4.21.91;
DE              EC=3.6.1.15;
DE              EC=3.6.4.13;
DE     AltName: Full=Flavivirin protease NS3 catalytic subunit;
DE     AltName: Full=Non-structural protein 3;
DE   Contains:
DE     RecName: Full=Non-structural protein 4A;
DE              Short=NS4A;
DE   Contains:
DE     RecName: Full=Non-structural protein 4B;
DE              Short=NS4B;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase NS5;
DE              EC=2.1.1.56 {ECO:0000255|PROSITE-ProRule:PRU00924};
DE              EC=2.1.1.57 {ECO:0000255|PROSITE-ProRule:PRU00924};
DE              EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE     AltName: Full=NS5;
OS   Tick-borne powassan virus (strain LB) (POWV) (Powassan virus).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Flavivirus.
OX   NCBI_TaxID=39008;
OH   NCBI_TaxID=34620; Dermacentor andersoni (Rocky mountain wood tick).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=35565; Ixodes cookei.
OH   NCBI_TaxID=6945; Ixodes scapularis (Black-legged tick) (Deer tick).
OH   NCBI_TaxID=34614; Ixodes spinipalpis.
OH   NCBI_TaxID=48086; Lepus americanus (Snowshoe hare).
OH   NCBI_TaxID=9995; Marmota monax (Woodchuck).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8097605; DOI=10.1006/viro.1993.1247;
RA   Mandl C.W., Holzmann H., Kunz C., Heinz F.X.;
RT   "Complete genomic sequence of Powassan virus: evaluation of genetic
RT   elements in tick-borne versus mosquito-borne flaviviruses.";
RL   Virology 194:173-184(1993).
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. 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:P17763}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of
CC         the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.;
CC         EC=3.4.21.91;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC         S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC         COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC         ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00924};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC         in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC         Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC         EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
CC   -!- SUBUNIT: [Capsid protein C]: Homodimer (By similarity). Interacts (via
CC       N-terminus) with host EXOC1 (via C-terminus); this interaction results
CC       in EXOC1 degradation through the proteasome degradation pathway (By
CC       similarity). {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBUNIT: [Protein prM]: Forms heterodimers with envelope protein E in
CC       the endoplasmic reticulum and Golgi. {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBUNIT: [Envelope protein E]: Homodimer; in the endoplasmic reticulum
CC       and Golgi. {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBUNIT: [Non-structural protein 1]: Forms homodimers as well as
CC       homohexamers. NS1 may interact with NS4A.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBUNIT: [Serine protease subunit NS2B]: Forms a heterodimer with
CC       serine protease NS3. May form homooligomers.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBUNIT: [Serine protease NS3]: Forms a heterodimer with NS2B.
CC       Interacts with NS4B. Interacts with unphosphorylated RNA-directed RNA
CC       polymerase NS5; this interaction stimulates RNA-directed RNA polymerase
CC       NS5 guanylyltransferase activity. {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBUNIT: [Non-structural protein 4B]: Interacts with serine protease
CC       NS3. {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBUNIT: [RNA-directed RNA polymerase NS5]: Interacts with host STAT2;
CC       this interaction inhibits the phosphorylation of the latter, and, when
CC       all viral proteins are present (polyprotein), targets STAT2 for
CC       degradation. {ECO:0000250|UniProtKB:Q01299}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein C]: Virion
CC       {ECO:0000250|UniProtKB:P17763}. Host nucleus
CC       {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region
CC       {ECO:0000250|UniProtKB:P17763}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Peptide pr]: Secreted
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane
CC       {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=ER membrane retention is mediated by the
CC       transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
CC   -!- SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane
CC       {ECO:0000305}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=ER membrane retention is mediated by the
CC       transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted
CC       {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane;
CC       Peripheral membrane protein; Lumenal side
CC       {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles
CC       hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic
CC       reticulum membrane; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum
CC       membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane
CC       protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side
CC       {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently
CC       associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated
CC       vesicles hosting the replication complex.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived
CC       vesicles hosting the replication complex.
CC       {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host
CC       endoplasmic reticulum membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}.
CC       Note=Located in RE-associated vesicles hosting the replication complex.
CC       NS5 protein is mainly localized in the nucleus rather than in ER
CC       vesicles. {ECO:0000250|UniProtKB:P17763}.
CC   -!- DOMAIN: The transmembrane domains of the small envelope protein M and
CC       envelope protein E contain an endoplasmic reticulum retention signal.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield
CC       mature proteins. Cleavages in the lumen of endoplasmic reticulum are
CC       performed by host signal peptidase, whereas cleavages in the
CC       cytoplasmic side are performed by serine protease NS3. Signal cleavage
CC       at the 2K-4B site requires a prior NS3 protease-mediated cleavage at
CC       the 4A-2K site. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin,
CC       releasing the mature small envelope protein M, and peptide pr. This
CC       cleavage is incomplete as up to 30% of viral particles still carry
CC       uncleaved prM. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: [Envelope protein E]: N-glycosylated.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is
CC       glycosylated and this is required for efficient secretion of the
CC       protein from infected cells. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines
CC       residues. This phosphorylation may trigger NS5 nuclear localization.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the class I-like SAM-
CC       binding methyltransferase superfamily. mRNA cap 0-1 NS5-type
CC       methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}.
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DR   EMBL; L06436; AAA02739.1; -; Genomic_RNA.
DR   PIR; A46105; A46105.
DR   RefSeq; NP_620099.1; NC_003687.1.
DR   SMR; Q04538; -.
DR   PRIDE; Q04538; -.
DR   GeneID; 940442; -.
DR   KEGG; vg:940442; -.
DR   Proteomes; UP000006848; Genome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0039563; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039564; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT2 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   CDD; cd20761; capping_2-OMTase_Flaviviridae; 1.
DR   CDD; cd12149; Flavi_E_C; 1.
DR   Gene3D; 1.10.8.970; -; 1.
DR   Gene3D; 1.20.1280.260; -; 1.
DR   Gene3D; 2.60.260.50; -; 1.
DR   Gene3D; 2.60.40.350; -; 1.
DR   Gene3D; 2.60.98.10; -; 1.
DR   Gene3D; 3.30.387.10; -; 1.
DR   Gene3D; 3.30.67.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011492; DEAD_Flavivir.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
DR   InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
DR   InterPro; IPR001122; Flavi_capsidC.
DR   InterPro; IPR027287; Flavi_E_Ig-like.
DR   InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
DR   InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
DR   InterPro; IPR001157; Flavi_NS1.
DR   InterPro; IPR000752; Flavi_NS2A.
DR   InterPro; IPR000487; Flavi_NS2B.
DR   InterPro; IPR000404; Flavi_NS4A.
DR   InterPro; IPR001528; Flavi_NS4B.
DR   InterPro; IPR002535; Flavi_propep.
DR   InterPro; IPR038688; Flavi_propep_sf.
DR   InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR   InterPro; IPR001850; Flavivirus_NS3_S7.
DR   InterPro; IPR014412; Gen_Poly_FLV.
DR   InterPro; IPR011998; Glycoprot_cen/dimer.
DR   InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR   InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR   InterPro; IPR013756; GlyE_cen_dom_subdom2.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR000208; RNA-dir_pol_flavivirus.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01003; Flavi_capsid; 1.
DR   Pfam; PF07652; Flavi_DEAD; 1.
DR   Pfam; PF02832; Flavi_glycop_C; 1.
DR   Pfam; PF00869; Flavi_glycoprot; 1.
DR   Pfam; PF00948; Flavi_NS1; 1.
DR   Pfam; PF01005; Flavi_NS2A; 1.
DR   Pfam; PF01350; Flavi_NS4A; 1.
DR   Pfam; PF01349; Flavi_NS4B; 1.
DR   Pfam; PF00972; Flavi_NS5; 1.
DR   Pfam; PF01570; Flavi_propep; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF00949; Peptidase_S7; 1.
DR   PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   SUPFAM; SSF56983; SSF56983; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   TIGRFAMs; TIGR04240; flavi_E_stem; 1.
DR   PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
DR   PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
PE   3: Inferred from homology;
KW   Activation of host autophagy by virus; ATP-binding; Capsid protein;
KW   Clathrin-mediated endocytosis of virus by host;
KW   Cleavage on pair of basic residues; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
KW   Host cytoplasm; Host endoplasmic reticulum; Host membrane; Host nucleus;
KW   Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host 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..3415
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000037724"
FT   CHAIN           1..94
FT                   /note="Capsid protein C"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT                   /id="PRO_0000405239"
FT   PROPEP          95..115
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_0000405140"
FT   CHAIN           116..278
FT                   /note="Protein prM"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000405141"
FT   CHAIN           116..203
FT                   /note="Peptide pr"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000037725"
FT   CHAIN           204..278
FT                   /note="Small envelope protein M"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000037726"
FT   CHAIN           279..775
FT                   /note="Envelope protein E"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000037727"
FT   CHAIN           776..1128
FT                   /note="Non-structural protein 1"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT                   /id="PRO_0000037728"
FT   CHAIN           1129..1358
FT                   /note="Non-structural protein 2A"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT                   /id="PRO_0000037729"
FT   CHAIN           1359..1489
FT                   /note="Serine protease subunit NS2B"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT                   /id="PRO_0000037730"
FT   CHAIN           1490..2111
FT                   /note="Serine protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT                   /id="PRO_0000037731"
FT   CHAIN           2112..2237
FT                   /note="Non-structural protein 4A"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT                   /id="PRO_0000037732"
FT   PEPTIDE         2238..2260
FT                   /note="Peptide 2k"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT                   /id="PRO_0000405142"
FT   CHAIN           2261..2512
FT                   /note="Non-structural protein 4B"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT                   /id="PRO_0000037733"
FT   CHAIN           2513..3415
FT                   /note="RNA-directed RNA polymerase NS5"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT                   /id="PRO_0000037734"
FT   TOPO_DOM        1..96
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        118..243
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        279..726
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        727..747
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        748..754
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        755..775
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        776..1187
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1188..1208
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P17763, ECO:0000255"
FT   TOPO_DOM        1209..1233
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P17763, ECO:0000255"
FT   TRANSMEM        1234..1253
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P17763, ECO:0000255"
FT   TOPO_DOM        1254
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P17763, ECO:0000255"
FT   TRANSMEM        1255..1275
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P17763, ECO:0000255"
FT   TOPO_DOM        1276..1292
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P17763, ECO:0000255"
FT   TRANSMEM        1293..1313
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P17763, ECO:0000255"
FT   TOPO_DOM        1314..1327
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P17763, ECO:0000255"
FT   TRANSMEM        1328..1348
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P17763, ECO:0000255"
FT   TOPO_DOM        1349..1359
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P17763, ECO:0000255"
FT   TRANSMEM        1360..1378
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1379..1382
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1383..1403
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1404..1452
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        1453..1473
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1474..2163
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2164..2184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2185..2190
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        2191..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..2243
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2244..2264
FT                   /note="Helical; Note=Signal for NS4B"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2265..2300
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        2301..2321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2322..2344
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        2345..2365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2366..2369
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2370..2390
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2391..2433
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2434..2454
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2455..2479
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2480..2500
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2501..3415
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..1832
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1842..2001
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          2513..2777
FT                   /note="mRNA cap 0-1 NS5-type MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   DOMAIN          3041..3190
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          376..389
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          2731..2735
FT                   /note="Interaction with host SCRIB"
FT                   /evidence="ECO:0000250|UniProtKB:Q01299"
FT   MOTIF           1780..1783
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        2573
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   ACT_SITE        2658
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   ACT_SITE        2695
FT                   /note="For 2'-O-MTase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT   ACT_SITE        2731
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         2568
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         2599
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         2617
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         2644
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2659
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2733
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   BINDING         2951
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   BINDING         2955
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   BINDING         2960
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   BINDING         2963
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   BINDING         3225
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   BINDING         3241
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   BINDING         3360
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   SITE            94..95
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT   SITE            114..115
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT   SITE            115..116
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT   SITE            203..204
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT   SITE            278..279
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P06935"
FT   SITE            775..776
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            1950
FT                   /note="Involved in NS3 ATPase and RTPase activities"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   SITE            1953
FT                   /note="Involved in NS3 ATPase and RTPase activities"
FT                   /evidence="ECO:0000250|UniProtKB:P14335"
FT   SITE            2111..2112
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT   SITE            2237..2238
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT   SITE            2260..2261
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT   SITE            2512..2513
FT                   /note="Cleavage; by viral protease NS3"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT   SITE            2525
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2528
FT                   /note="mRNA cap binding; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2529
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2531
FT                   /note="mRNA cap binding; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2536
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2540
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2573
FT                   /note="Essential for 2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2658
FT                   /note="Essential for 2'-O-methyltransferase and N-7
FT                   methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2662
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2695
FT                   /note="Essential for 2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2726
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2728
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   SITE            2731
FT                   /note="Essential for 2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT   MOD_RES         2568
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P03314"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        432
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P14336,
FT                   ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        860
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        281..308
FT                   /evidence="ECO:0000250|UniProtKB:P14336"
FT   DISULFID        338..399
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        338..394
FT                   /evidence="ECO:0000250|UniProtKB:P14336"
FT   DISULFID        352..383
FT                   /evidence="ECO:0000250|UniProtKB:P14336"
FT   DISULFID        370..399
FT                   /evidence="ECO:0000250|UniProtKB:P14336"
FT   DISULFID        370..394
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        464..568
FT                   /evidence="ECO:0000250|UniProtKB:P14336"
FT   DISULFID        585..617
FT                   /evidence="ECO:0000250|UniProtKB:P14336"
FT   DISULFID        779..790
FT                   /evidence="ECO:0000250|UniProtKB:P17763"
FT   DISULFID        830..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"
SQ   SEQUENCE   3415 AA;  378570 MW;  E71092FE64049F46 CRC64;
     MMTTSKGKGG GPPRRKLKVT ANKSRPATSP MPKGFVLSRM LGILWHAVTG TARPPVLKMF
     WKTVPLRQAE AVLKKIKRVI GNLMQSLHMR GRRRSGVDWT WIFLTMALMT MAMATTIHRD
     REGYMVMRAS GRDAASQVRV QNGTCVILAT DMGEWCEDSI TYSCVTIDQE EEPVDVDCFC
     RGVDRVKLEY GRCGRQAGSR GKRSVVIPTH AQKDMVGRGH AWLKGDNIRD HVTRVEGWMW
     KNKLLTAAIV ALAWLMVDSW MARVTVILLA LSLGPVYATR CTHLENRDFV TGTQGTTRVS
     LVLELGGCVT ITAEGKPSID VWLEDIFQES PAETREYCLH AKLTNTKVEA RCPTTGPATL
     PEEHQANMVC KRDQSDRGWG NHCGFFGKGS IVACAKFECE EAKKAVGHVY DSTKITYVVK
     VEPHTGDYLA ANETNSNRKS AQFTVASEKV ILRLGDYGDV SLTCKVASGI DVAQTVVMSL
     DSSKDHLPSA WQVHRDWFED LALPWKHKDN QDWNSVEKLV EFGPPHAVKM DVFNLGDQTA
     VLLKSLAGVP LASVEGQKYH LKSGHVTCDV GLEKLKLKGT TYSMCDKAKF KWKRVPVDSG
     HDTVVMEVSY TGSDKPCRIP VRAVAHGVPA VNVAMLITPN PTIETNGGGF IEMQLPPGDN
     IIYVGDLSQQ WFQKGSTIGR MFEKTRRGLE RLSVVGEHAW DFGSVGGVLS SVGKAIHTVL
     GGAFNTLFGG VGFIPKMLLG VALVWLGLNA RNPTMSMTFL AVGALTLMMT MGVGADYGCA
     IDPERMEIRC GEGLVVWKEV SEWYDGYAYH PESPDTLAQA LREAFERGVC GVVPQNRLEM
     AMWRSTAPEL NLVLSEGEAN LTIVVDKTDP ADYRGGTPMV LKKTGKESKV SWKSWGKSIL
     WSVPDSPRRM MMGVDGVGEC PLYRRATGVF TVAEFGVGLR TKVFLDLRGE ASKECDTGVM
     GAAVKNGKAI HTDQSMWMSS FRNDTGTYIH ELILTDLRNC TWPASHTIDN DGVLDSHLFL
     PVTLAGPRSK YNRIPGYSEQ VRGPWDQTPL RVVRDHCPGT SVRIDSHCDK RGASVRSTTE
     SGKIIPEWCC RACELPPVTF RSGTDCWYAM EIRPVHSQGG LVRSMVVADN GALLSEGGVP
     GLVAVFVLME FLLRRRPGSV TSILWGGILM LGLLVTGLVR VEEIVRYVIA VGVTFHLELG
     PETMVLVMLQ AVFNMRTCYL MGFLVKRVIT TREVVTVYFL LLVLEMGIPE MNFGHLWEWA
     DALAMGLLII KASAMEDRRG LGFLLAGLMT QRHLVAVHHG LMVFLTVALA VVGRNIYNGQ
     KERKGLCFTV PLASLLGGSG SGLRMLALWE CLGGRGRRSL SEPLTVVGVM LAMASGLLRH
     SSQEALLALS AGSFLILMLI LGTRRLQLTA EWAGVVEWNP ELVNEGGEVS LKVRQDAMGN
     LHLTEVEREE RRLALWLVFG LLASAYHWSG ILVTMGAWTV YELFSSTRRT DLVFSGQLPD
     QGEKRSFDIK EGVYRIYAPG LFWGYRQIGV GYGTKGVLHT MWHVTRGAAL SVEGATSGPY
     WADVREDVVC YGGAWGLDKK WGGEVVQVHA FPPDSGHKIH QCQPGKLNLE GGRVLGAIPI
     DLPRGTSGSP IINAQGDVLG LYGNGLKSND VYISSIAQGN VEKSRPEMPL AVQGGKWTSK
     GSITVLDMHP GSGKTHRVLP ELIRECIDKR LRTVVLAPTR VVLKEMERAL QGKRVKFHSA
     AVDNASSSSG AIVDVMCHAT YVNRRLLPQG RQNWEVAIMD EAHWTDPHSI AARGHLYSLA
     KENRCALVLM TATPPGKSEA FPESKGAIVS EEKPIPEGEW RDGFDWITEF EGRTAWFVPS
     IAKGGAIART LRQKGKSVIC LNSKTFDKDY GRVHEEKPDF VVTTDISEMG ANLDVNRVID
     GRTNIKPEEI DGKVELIGTR RVTTASAAQR RGRVGRHEGR TDLYVYSGQC DDDDSSLVQW
     KEAQILLDNI TTVRGPVATF YGPEQGKMLE VAGHFRLTEE KRKHFRHLLT NCDFTPWLAW
     HVAANTACVT DRKWTWEGPD ENAIDGPGGE LVTFRSPNGA ERKLKPIWKD SRMFREGRDV
     ADFIQYASGR RSAVDILTGL GGVPDLLRLR CTAAWDVVYT LLNETPGSRA MKMAERDAPE
     AMLTLLEVAV LGIATLGVVW CFIVRTSVSR MVLGTLVLAV ALILLWLGGM DYGTMAGVAL
     IFYLLLTVLQ PEPGKQRSGE DNRLAFLLIG LGSVVGLVAA NELGYLEQTK TDISGLFRRE
     DQGGMVWDAW TNIDIQPARS WGTYVLIVSL FTPYMLHQLQ TKIQRLVNSS VAAGTQAMRD
     LGGGTPFFGV AGHVVALGVT SLVGATPTSL ALGVALAALH LAVVTSGLEA ELTQRAHRAF
     FSAMVKNPMV DGEIINPIPD GDPKPALYER KMSLFLAIGL CIAAVALNRT AAAMTEAGAV
     AVAALGQLLR PEEESWWTMP MACGMAGLVR GSLWGLLPVL HRIWLRTQGA RRGGAEGSTL
     GDIWKQRLNS CTKEEFFAYR RTGVMETNRD QARELLRRGE TNMGLAVSRG CAKLAWLEER
     GYATLKGEVV DLGCGRGGWS YYAASRPSVM AVRAYTIGGK GHEAPRLVTS LGWNLIKFRS
     GMDVFSMATT RADTILCDIG ESSPDPEKEG ARSRRVILLM EQWKARNPDA AAVFKVLAPY
     RPEVLEALHR FQLQWGGGLV RVPFSRNSTH EMYYSTAVTG NLVNSVNVLS RKLLARFGET
     RGPIQVPEID LGTGTRCVTL AEDKVKPRDV AERIGALREQ YSESWHEDKE HPYRTWQYWG
     SYRTPATGSA ASLINGVVKL LSWPWNARED VTRMAMTDTT AFGQQRVFKE KVDTKAQEPQ
     PGTRVIMRAV SDWLLEHLSR RAKVRMCTKD EFIAKVRSNA ALGAWSDEQN KWSSAKEAVE
     DPEFWKLVDE ERSRHLKGQC RHCVYNMMGK REKKLGEFGV AKGSRAIWYM WLGSRFLEFE
     VLGFLNEEHW ASREVSGAGV EGTSLNYLGW LLRELGMKDG GKLYADDTAG WDTRITNADL
     EDEEQILRYM EGEHHVLAKT ILEKAYHAKV VKVARPSPQG GCVMDVITRR DQRGSGQVVT
     YALNTITNMK VQLIRMMEGE GVIGPADSQD PRLKRVETWL KEHGVERLGR MLVSGDDCVV
     KPIDDRFGKA LYFLNDMAKV RKDVGEWEPS MGFTEWEEVP FCSHHFHELV MKDGRSLIVP
     CRDQDELVGR ARVSPGCGWS VRETACLSKA YGQMWLLNYF HRRDLRTLGF AICSAVPVSW
     VPMGRTTWSI HASGEWMTTE DMLRIWNKVW ILDNPHMEDK QTVDEWRDIP YLPKTQDLVC
     SSLVGRKERA EWAKNIWGSV EKVRKLIGPE DYRDYLSSMD RHDLHWELKL ESSII
 
 
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