POLG_KOKV
ID POLG_KOKV Reviewed; 3410 AA.
AC Q32ZD5;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Genome polyprotein;
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 {ECO:0000269|PubMed:18004778};
DE EC=3.6.4.13 {ECO:0000269|PubMed:18004778};
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=Peptide 2k;
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:PRU00924};
DE AltName: Full=NS5;
OS Kokobera virus (KOKV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Flavivirus.
OX NCBI_TaxID=44024;
OH NCBI_TaxID=162997; Culex annulirostris (Common banded mosquito).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=644619; Ochlerotatus camptorhynchus.
OH NCBI_TaxID=569589; Ochlerotatus vigilax.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
RC STRAIN=AusMRM 32 {ECO:0000312|EMBL:AAV34157.1};
RX PubMed=16223950; DOI=10.1128/cmr.18.4.608-637.2005;
RA Kuno G., Chang G.J.;
RT "Biological transmission of arboviruses: reexamination of and new insights
RT into components, mechanisms, and unique traits as well as their
RT evolutionary trends.";
RL Clin. Microbiol. Rev. 18:608-637(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1678-2108, FUNCTION (SERINE
RP PROTEASE NS3), BIOPHYSICOCHEMICAL PROPERTIES (SERINE PROTEASE NS3),
RP MUTAGENESIS OF MET-1724, AND CATALYTIC ACTIVITY (SERINE PROTEASE NS3).
RX PubMed=18004778; DOI=10.1002/prot.21812;
RA Speroni S., De Colibus L., Mastrangelo E., Gould E., Coutard B.,
RA Forrester N.L., Blanc S., Canard B., Mattevi A.;
RT "Structure and biochemical analysis of Kokobera virus helicase.";
RL Proteins 70:1120-1123(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. Overcomes the anti-viral effects of host
CC EXOC1 by sequestering and degrading the latter through the proteasome
CC degradation pathway. {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering
CC with host Dicer. {ECO:0000250|UniProtKB:P03314}.
CC -!- FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope
CC proteins in trans-Golgi by binding to envelope protein E at pH6.0.
CC After virion release in extracellular space, gets dissociated from E
CC dimers. {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Protein prM]: Acts as a chaperone for envelope protein E
CC during intracellular virion assembly by masking and inactivating
CC envelope protein E fusion peptide. prM is the only viral peptide
CC matured by host furin in the trans-Golgi network probably to avoid
CC catastrophic activation of the viral fusion activity in acidic Golgi
CC compartment prior to virion release. prM-E cleavage is inefficient, and
CC many virions are only partially matured. These uncleaved prM would play
CC a role in immune evasion. {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Small envelope protein M]: May play a role in virus budding.
CC Exerts cytotoxic effects by activating a mitochondrial apoptotic
CC pathway through M ectodomain. May display a viroporin activity.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and
CC mediates fusion between viral and cellular membranes. Envelope protein
CC is synthesized in the endoplasmic reticulum in the form of heterodimer
CC with protein prM. They play a role in virion budding in the ER, and the
CC newly formed immature particle is covered with 60 spikes composed of
CC heterodimer between precursor prM and envelope protein E. The virion is
CC transported to the Golgi apparatus where the low pH causes dissociation
CC of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is
CC inefficient, and many virions are only partially matured. These
CC uncleaved prM would play a role in immune evasion.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Non-structural protein 1]: Involved in immune evasion,
CC pathogenesis and viral replication. Once cleaved off the polyprotein,
CC is targeted to three destinations: the viral replication cycle, the
CC plasma membrane and the extracellular compartment. Essential for viral
CC replication. Required for formation of the replication complex and
CC recruitment of other non-structural proteins to the ER-derived membrane
CC structures. Excreted as a hexameric lipoparticle that plays a role
CC against host immune response. Antagonizing the complement function.
CC Binds to the host macrophages and dendritic cells. Inhibits signal
CC transduction originating from Toll-like receptor 3 (TLR3).
CC {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- FUNCTION: [Non-structural protein 2A]: Component of the viral RNA
CC replication complex that functions in virion assembly and antagonizes
CC the host alpha/beta interferon antiviral response.
CC {ECO:0000250|UniProtKB:P14335}.
CC -!- FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the
CC serine protease function of NS3. May have membrane-destabilizing
CC activity and form viroporins (By similarity).
CC {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}.
CC -!- FUNCTION: [Serine protease NS3]: Displays three enzymatic activities:
CC serine protease, NTPase and RNA helicase. NS3 serine protease, in
CC association with NS2B, performs its autocleavage and cleaves the
CC polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-
CC NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and
CC unwinds dsRNA in the 3' to 5' direction (PubMed:18004778).
CC {ECO:0000255|PROSITE-ProRule:PRU00860, ECO:0000269|PubMed:18004778}.
CC -!- FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of
CC the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy
CC during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is
CC required for the interferon antagonism activity of the latter.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-
CC derived membrane vesicles where the viral replication takes place.
CC Inhibits interferon (IFN)-induced host STAT1 phosphorylation and
CC nuclear translocation, thereby preventing the establishment of cellular
CC antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2
CC translocation in the nucleus after IFN-alpha treatment.
CC {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+)
CC and (-) RNA genome, and performs the capping of genomes in the
CC cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O
CC positions. Besides its role in RNA genome replication, also prevents
CC the establishment of cellular antiviral state by blocking the
CC interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host
CC TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-
CC STAT signaling pathway. {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of
CC the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.;
CC EC=3.4.21.91;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000269|PubMed:18004778};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=340 mM for ATPase of serine protease NS3
CC {ECO:0000269|PubMed:18004778};
CC -!- SUBUNIT: [Capsid protein C]: Homodimer (By similarity). Interacts (via
CC N-terminus) with host EXOC1 (via C-terminus); this interaction results
CC in EXOC1 degradation through the proteasome degradation pathway (By
CC similarity). {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Protein prM]: Forms heterodimers with envelope protein E in
CC the endoplasmic reticulum and Golgi. {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Envelope protein E]: Homodimer; in the endoplasmic reticulum
CC and Golgi (By similarity). Interacts with protein prM (By similarity).
CC Interacts with non-structural protein 1 (By similarity).
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Non-structural protein 1]: Homodimer; Homohexamer when
CC secreted (By similarity). Interacts with envelope protein E (By
CC similarity). NS1 interacts with NS4B (By similarity). Interacts with
CC host complement protein CFH; this interaction leads to the degradation
CC of C3 (By similarity). {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- SUBUNIT: [Non-structural protein 2A]: Interacts (via N-terminus) with
CC serine protease NS3. {ECO:0000250|UniProtKB:P03314}.
CC -!- SUBUNIT: [Serine protease subunit NS2B]: Forms a heterodimer with
CC serine protease NS3 (By similarity). May form homooligomers (By
CC similarity). {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Serine protease NS3]: Forms a heterodimer with NS2B (By
CC similarity). Interacts with non-structural protein 2A (via N-terminus)
CC (By similarity). Interacts with NS4B (By similarity). Interacts with
CC unphosphorylated RNA-directed RNA polymerase NS5; this interaction
CC stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity
CC (By similarity). {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Non-structural protein 4B]: Interacts with serine protease
CC NS3 (By similarity). {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [RNA-directed RNA polymerase NS5]: Homodimer (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).
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein C]: Virion
CC {ECO:0000250|UniProtKB:P17763}. Host nucleus
CC {ECO:0000250|UniProtKB:P17763}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region
CC {ECO:0000250|UniProtKB:P06935}.
CC -!- SUBCELLULAR LOCATION: [Peptide pr]: Secreted
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane
CC {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC {ECO:0000255}. Note=ER membrane retention is mediated by the
CC transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
CC -!- SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane
CC {ECO:0000305}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC {ECO:0000255}. Note=ER membrane retention is mediated by the
CC transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted
CC {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane;
CC Peripheral membrane protein; Lumenal side
CC {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles
CC hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic
CC reticulum membrane; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum
CC membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side
CC {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently
CC associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-
CC ProRule:PRU00860}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated
CC vesicles hosting the replication complex.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived
CC vesicles hosting the replication complex.
CC {ECO:0000250|UniProtKB:Q9Q6P4}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host
CC endoplasmic reticulum membrane; Peripheral membrane protein;
CC Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P06935}.
CC Note=Located in RE-associated vesicles hosting the replication complex.
CC NS5 protein is mainly localized in the nucleus rather than in ER
CC vesicles. {ECO:0000250|UniProtKB:P17763}.
CC -!- DOMAIN: The transmembrane domains of the small envelope protein M and
CC envelope protein E contain an endoplasmic reticulum retention signal.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins. Cleavages in the lumen of endoplasmic reticulum are
CC performed by host signal peptidase, whereas cleavages in the
CC cytoplasmic side are performed by serine protease NS3. Signal cleavage
CC at the 2K-4B site requires a prior NS3 protease-mediated cleavage at
CC the 4A-2K site. {ECO:0000250|UniProtKB:P17763}.
CC -!- PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin,
CC releasing the mature small envelope protein M, and peptide pr. This
CC cleavage is incomplete as up to 30% of viral particles still carry
CC uncleaved prM. {ECO:0000250|UniProtKB:P17763}.
CC -!- PTM: [Envelope protein E]: N-glycosylated.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is
CC glycosylated and this is required for efficient secretion of the
CC protein from infected cells. {ECO:0000250|UniProtKB:P17763}.
CC -!- PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines
CC residues. This phosphorylation may trigger NS5 nuclear localization.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the class I-like SAM-
CC binding methyltransferase superfamily. mRNA cap 0-1 NS5-type
CC methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}.
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DR EMBL; AY632541; AAV34157.1; -; Genomic_RNA.
DR RefSeq; YP_001040007.1; NC_009029.2.
DR PDB; 2V6I; X-ray; 2.10 A; A=1678-2108.
DR PDB; 2V6J; X-ray; 2.30 A; A=1678-2108.
DR PDBsum; 2V6I; -.
DR PDBsum; 2V6J; -.
DR SMR; Q32ZD5; -.
DR MEROPS; S07.001; -.
DR GeneID; 5075791; -.
DR KEGG; vg:5075791; -.
DR BRENDA; 3.4.21.91; 10317.
DR EvolutionaryTrace; Q32ZD5; -.
DR Proteomes; UP000124420; 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: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; IDA:UniProtKB.
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: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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR CDD; cd20761; capping_2-OMTase_Flaviviridae; 1.
DR CDD; cd12149; Flavi_E_C; 1.
DR Gene3D; 1.10.10.930; -; 1.
DR Gene3D; 1.10.8.970; -; 1.
DR Gene3D; 1.20.1280.260; -; 1.
DR Gene3D; 2.60.260.50; -; 1.
DR Gene3D; 2.60.40.350; -; 1.
DR Gene3D; 2.60.98.10; -; 1.
DR Gene3D; 3.30.387.10; -; 1.
DR Gene3D; 3.30.67.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011492; DEAD_Flavivir.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000069; Env_glycoprot_M_flavivir.
DR InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
DR InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
DR InterPro; IPR001122; Flavi_capsidC.
DR InterPro; IPR037172; Flavi_capsidC_sf.
DR InterPro; IPR027287; Flavi_E_Ig-like.
DR InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
DR InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
DR InterPro; IPR001157; Flavi_NS1.
DR InterPro; IPR000752; Flavi_NS2A.
DR InterPro; IPR000487; Flavi_NS2B.
DR InterPro; IPR000404; Flavi_NS4A.
DR InterPro; IPR001528; Flavi_NS4B.
DR InterPro; IPR002535; Flavi_propep.
DR InterPro; IPR038688; Flavi_propep_sf.
DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR InterPro; IPR001850; Flavivirus_NS3_S7.
DR InterPro; IPR014412; Gen_Poly_FLV.
DR InterPro; IPR011998; Glycoprot_cen/dimer.
DR InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR InterPro; IPR013756; GlyE_cen_dom_subdom2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR000208; RNA-dir_pol_flavivirus.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01003; Flavi_capsid; 1.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF02832; Flavi_glycop_C; 1.
DR Pfam; PF00869; Flavi_glycoprot; 1.
DR Pfam; PF01004; Flavi_M; 1.
DR Pfam; PF00948; Flavi_NS1; 1.
DR Pfam; PF01005; Flavi_NS2A; 1.
DR Pfam; PF01002; Flavi_NS2B; 1.
DR Pfam; PF01350; Flavi_NS4A; 1.
DR Pfam; PF01349; Flavi_NS4B; 1.
DR Pfam; PF00972; Flavi_NS5; 1.
DR Pfam; PF01570; Flavi_propep; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF00949; Peptidase_S7; 1.
DR PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF101257; SSF101257; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF56983; SSF56983; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR04240; flavi_E_stem; 1.
DR PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
DR PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; ATP-binding;
KW Capsid protein; Cleavage on pair of basic residues; Coiled coil;
KW Disulfide bond; Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
KW Host cytoplasm; Host endoplasmic reticulum; Host membrane; Host nucleus;
KW Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host STAT1 by virus; Inhibition of host STAT2 by virus;
KW Membrane; Metal-binding; Methyltransferase; mRNA capping; mRNA processing;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
KW RNA-binding; RNA-directed RNA polymerase; S-adenosyl-L-methionine;
KW Secreted; Serine protease; Suppressor of RNA silencing; Transferase;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral immunoevasion; Viral penetration into host cytoplasm;
KW Viral RNA replication; Virion; Virus entry into host cell; Zinc.
FT CHAIN 1..3410
FT /note="Genome polyprotein"
FT /id="PRO_0000441516"
FT CHAIN 1..102
FT /note="Capsid protein C"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441517"
FT PROPEP 103..119
FT /note="ER anchor for the capsid protein C, removed in
FT mature form by serine protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441518"
FT CHAIN 120..286
FT /note="Protein prM"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441519"
FT CHAIN 120..211
FT /note="Peptide pr"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441520"
FT CHAIN 212..286
FT /note="Small envelope protein M"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441521"
FT CHAIN 287..787
FT /note="Envelope protein E"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441522"
FT CHAIN 788..1138
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441523"
FT CHAIN 1139..1362
FT /note="Non-structural protein 2A"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441524"
FT CHAIN 1363..1492
FT /note="Serine protease subunit NS2B"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441525"
FT CHAIN 1493..2108
FT /note="Serine protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441526"
FT CHAIN 2109..2234
FT /note="Non-structural protein 4A"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441527"
FT PEPTIDE 2235..2257
FT /note="Peptide 2k"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441528"
FT CHAIN 2258..2507
FT /note="Non-structural protein 4B"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441529"
FT CHAIN 2508..3410
FT /note="RNA-directed RNA polymerase NS5"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000441530"
FT TOPO_DOM 1..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..245
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..286
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 287..739
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 740..760
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 761..766
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 767..787
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 788..1165
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1166..1186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1187..1214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1215..1235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1236..1242
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1243..1263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1264..1284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1285..1305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1306..1335
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1336..1356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1357..1363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1364..1384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1385..1387
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1388..1408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1409..1464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1465..1485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1486..2158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2159..2179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2180..2185
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 2186..2205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2206
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2207..2227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2228..2242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2243..2257
FT /note="Helical; Note=Signal for NS4B"
FT /evidence="ECO:0000305"
FT TOPO_DOM 2258..2293
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 2294..2314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2315..2336
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2337..2357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2359..2379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2380..2420
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2421..2441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2442..3410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1493..1670
FT /note="Peptidase S7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT DOMAIN 1673..1829
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1839..2006
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2508..2773
FT /note="mRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT DOMAIN 3036..3187
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 2..15
FT /note="Interaction with host EXOC1"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT REGION 38..73
FT /note="Hydrophobic; homodimerization of capsid protein C"
FT /evidence="ECO:0000250|UniProtKB:P29990"
FT REGION 384..397
FT /note="Fusion peptide"
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT REGION 1415..1454
FT /note="Interacts with and activates NS3 protease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00859"
FT REGION 1677..1680
FT /note="Important for RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P14340"
FT REGION 2153..2157
FT /note="Regulates the ATPase activity of NS3 helicase"
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT MOTIF 1777..1780
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 2568
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2653
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2690
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT ACT_SITE 2726
FT /note="For 2'-O-MTase activity"
FT /evidence="ECO:0000250|UniProtKB:Q6YMS4"
FT BINDING 1686..1693
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 2563
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2593
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2594
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2611
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2612
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2638
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2639
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2654
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2728
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2947
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14335"
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 2956
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 3222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT BINDING 3356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 102..103
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 121..122
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 211..212
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 286..287
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 787..788
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1138..1139
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1362..1363
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1492..1493
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 1692
FT /note="Substrate binding"
FT /evidence="ECO:0000269|PubMed:18004778"
FT SITE 1947
FT /note="Involved in NS3 ATPase and RTPase activities"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 1950
FT /note="Involved in NS3 ATPase and RTPase activities"
FT /evidence="ECO:0000250|UniProtKB:P14335"
FT SITE 1950
FT /note="Substrate binding"
FT /evidence="ECO:0000269|PubMed:18004778"
FT SITE 1953
FT /note="Substrate binding"
FT /evidence="ECO:0000269|PubMed:18004778"
FT SITE 2108..2109
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 2234..2235
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 2257..2258
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000255"
FT SITE 2507..2508
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT SITE 2520
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2523
FT /note="mRNA cap binding; via carbonyl oxygen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2524
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2526
FT /note="mRNA cap binding; via carbonyl oxygen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2531
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2535
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2568
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2653
FT /note="Essential for 2'-O-methyltransferase and N-7
FT methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2690
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2721
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2723
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2726
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT MOD_RES 2563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P03314"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 915
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 289..316
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT DISULFID 346..407
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 346..402
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT DISULFID 360..391
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT DISULFID 378..407
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT DISULFID 378..402
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 476..574
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT DISULFID 591..622
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT DISULFID 791..802
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 842..928
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 964..1009
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1066..1115
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1077..1099
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1077..1098
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT DISULFID 1098..1102
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1099..1102
FT /evidence="ECO:0000250|UniProtKB:Q9Q6P4"
FT MUTAGEN 1724
FT /note="M->T: Severe decrease in helicase activity."
FT /evidence="ECO:0000269|PubMed:18004778"
FT STRAND 1681..1685
FT /evidence="ECO:0007829|PDB:2V6I"
FT TURN 1692..1695
FT /evidence="ECO:0007829|PDB:2V6I"
FT HELIX 1696..1706
FT /evidence="ECO:0007829|PDB:2V6I"
FT STRAND 1711..1717
FT /evidence="ECO:0007829|PDB:2V6I"
FT HELIX 1718..1727
FT /evidence="ECO:0007829|PDB:2V6I"
FT TURN 1728..1730
FT /evidence="ECO:0007829|PDB:2V6I"
FT STRAND 1733..1735
FT /evidence="ECO:0007829|PDB:2V6I"
FT STRAND 1749..1754
FT /evidence="ECO:0007829|PDB:2V6I"
FT HELIX 1755..1764
FT /evidence="ECO:0007829|PDB:2V6I"
FT STRAND 1772..1778
FT /evidence="ECO:0007829|PDB:2V6I"
FT HELIX 1784..1798
FT /evidence="ECO:0007829|PDB:2V6I"
FT STRAND 1803..1810
FT /evidence="ECO:0007829|PDB:2V6I"
FT STRAND 1826..1829
FT /evidence="ECO:0007829|PDB:2V6I"
FT HELIX 1842..1845
FT /evidence="ECO:0007829|PDB:2V6I"
FT STRAND 1851..1854
FT /evidence="ECO:0007829|PDB:2V6I"
FT HELIX 1858..1870
FT /evidence="ECO:0007829|PDB:2V6I"
FT STRAND 1875..1879
FT /evidence="ECO:0007829|PDB:2V6I"
FT TURN 1880..1882
FT /evidence="ECO:0007829|PDB:2V6I"
FT HELIX 1883..1886
FT /evidence="ECO:0007829|PDB:2V6I"
FT HELIX 1889..1892
FT /evidence="ECO:0007829|PDB:2V6I"
FT STRAND 1896..1900
FT /evidence="ECO:0007829|PDB:2V6I"
FT HELIX 1902..1905
FT /evidence="ECO:0007829|PDB:2V6I"
FT STRAND 1913..1917
FT /evidence="ECO:0007829|PDB:2V6I"
FT STRAND 1920..1927
FT /evidence="ECO:0007829|PDB:2V6I"
FT STRAND 1930..1938
FT /evidence="ECO:0007829|PDB:2V6I"
FT HELIX 1941..1948
FT /evidence="ECO:0007829|PDB:2V6I"
FT STRAND 1961..1964
FT /evidence="ECO:0007829|PDB:2V6I"
FT HELIX 1976..1985
FT /evidence="ECO:0007829|PDB:2V6I"
FT HELIX 2000..2005
FT /evidence="ECO:0007829|PDB:2V6I"
FT TURN 2010..2013
FT /evidence="ECO:0007829|PDB:2V6I"
FT HELIX 2017..2028
FT /evidence="ECO:0007829|PDB:2V6I"
FT HELIX 2034..2042
FT /evidence="ECO:0007829|PDB:2V6I"
FT HELIX 2051..2053
FT /evidence="ECO:0007829|PDB:2V6I"
FT HELIX 2058..2060
FT /evidence="ECO:0007829|PDB:2V6I"
FT STRAND 2070..2072
FT /evidence="ECO:0007829|PDB:2V6I"
FT STRAND 2078..2080
FT /evidence="ECO:0007829|PDB:2V6I"
FT HELIX 2088..2091
FT /evidence="ECO:0007829|PDB:2V6I"
FT HELIX 2094..2104
FT /evidence="ECO:0007829|PDB:2V6I"
SQ SEQUENCE 3410 AA; 378066 MW; 09A5AAC11C68907C CRC64;
MTKKPGRPGR NRAVNMLKRG ASRALGPMIK LKRMLFGLLD GRGPLRMVLA ILAFFRFTAL
KPTAGLLKRW GMMDKVHALS LLKGFKKDLA SMTDFVHLPK KKSGVSIIGR MLVFSFTAAV
RVTLENGMSL MKIQKADVGK VITIRTDRGE NRCIVQAMDV GEDCEDTMKY LCPAIENPSE
PDDIDCWCDK ADAMVTYGRC SKTRHSRRSR RSTNIAGHAD SRLDSRGSVW MDTKKATSYL
TKAESWALRN PGYALVAAVL GWSLGTSNAQ KVIFTVMILL IAPAYSIRCV GVENRDFIEG
VSGGTWVDVV LEHGGCVTIM APDKPTIDLE LTSTIAKSMA VTRTYCVQAQ VSELSVETRC
PTMGEAHNSK SSDAAYVCKK GFSDRGWGNG CGLFGKGSME TCAKFSCQTK AEGRIIQREN
LEYTIHMNVH ASQETGHFMN DTIASENKHG AKISITATGP SRTADLGDYG MVTLDCEPRA
GLDFDNLYLL TLGRNSWLVN RDWFHDVNLP WIGGAEGHWK NRESLVEFGK THATKREVLA
LGSQEGTLQV ALAGAMIAKF GSNVATINSG HLKCRLKLDK LKIKGTTYHM CKGSFAFTKT
PSDTGHGTVL LELTYSGSDG PCRVPISMSV SLSNIEPVGR MVTVNPIVLS SSPQKTIMIE
VEPPFGDSFI IAGTGEPRAH YHWRKSGSSI GAAFATTIKG ARRLAVIGDD AWDFGSVGGI
LNSVGKALHQ IFGGMFRTLF GGMSWFTQIM IGALCCWLGI NARDRTIAVT FLAVGGVLVF
LATSVNADSG CALDLKRKEF KCGNGIFVFN DAEAWSHSYR YHPSTPKKLA GSIVRAIEEG
QCGVRSVGRL EHEMWRANAR EINAILLENE KNLSVVVLES EYYRKAKNLM PIGDEMPFGW
KSWGKKFFEE PQLQNQTFVV DGRVGKECPE EKRSWNNFRI EDFGFGVFTT SVWMEQRTEY
TEDCDQKVIG AAVKGELAAH SDLGYWIESR SKNGSWELER AYLLESKSCS WPATHTLWNG
GVEESELIIP KSRAGPVSHH NTRKGYHNQI KGPWHLTPLE IRFESCPGTT VVTTEECGNR
GPSLRTTTTS GKVISEWCCR SCTMPPLSFR TADGCWYGME IRPLKEREET MVKSHVSAGR
GDGVDNLSLG LLVLTIALQE VMRKRILGRH ITWMVIAVFM AMILGGLSYR DLGRYLVLVG
AAFAERNSGG DLLHLVLVAT FKVKPMALLG FVLGGRWCRR QSLLLSIGAV LVNFALEFQG
GYFELVDSLA LALLFVKAVV QTDTTSVSLP LLAALAPAGC YTVLGTHRFI MLTLVLVTFL
GCKKTASVKK AGTAAVGVVL GMVGMKTIPM LGMLMVTSRA RRSWPLHEAM AAVGILCALF
GALAETEVDL AGPLAAAGLI VMAYVISGRS NDLSIKKVED VKWSDEAEVT GESVSYHVSL
DVRGDPTLTE DSGPGLEKVL LKVGLMAISG IYPVAIPFAL GAWFFLEKRC KRAGALWDIP
SPREAKPAKV EDGVYRIFSR KLFGESQIGA GVMVKGTFHT MWHVTRGAVL KAGEGLLEPA
WADVRKDLIC YGGNWKLEEH WDGNEEVQLI ALEPGKKVRH IQTKPGIFKT SEGEIGALDL
DCMAGTSGSP IVNKNGEVVG LYGNGVLIKG DRYVSAISQK ENVGQEDGAE IEDNWFRKRE
LTVLDLHPGA GKTRRVLPQL VREAVKKRLR TVILAPTRVV ASEMYEALRG EPIRYMTPAV
QSERTGNEIV DFMCHSTFTM KLFQGVRVPN YNLYIMDEAH FLDPASVAAR GYIETRVSMG
DAGAIFMTAT PPGTTEAFPP SNSPIIDEET RIPDKAWNSG YEWIIEFDGR TVWFVHSIKQ
GAEIGTCLQK AGKKVLYLNR KTFESEYPKC KSEKWDFVIT TDISEMGANF KADRVIDPRK
TIKPILLDGR VSMQGPIAIT PASAAQRRGR IGRNPEKLGD IYAYSGNVSS DNEGHVSWTE
ARMLLDNVHV QGGVVAQLYT PEREKTEAYE GEFKLKTNQR KVFSELIRTG DLPVWLAFQV
ASANVEYHDR KWCFDGPNEH LLLENNQEIE VWTRQGQRRV LKPRWLDGRI TSDHLNLKSF
KEFASGKRSA LSILDLIAVL PSHLNLRLQE ALDTAAILSR SEPGSRSYKA ALENSPEMIE
TFLLCALVCL MTIGLVVVLV RGKGPGKLAF GMVSIGVMTW LLWSAGVDPG KIAAAVILVF
LLLVVLIPEP EKQRSVQDNQ LAMLMLLIAT ILGGVAANEM GWLEKTKADL SWVVRGRSST
TTPVVELDMK PATAWTLYAL ATTLLTPLFQ HLIVTKYANI SLMAIASQAG TLFSMDSGIP
FSSIELSVPL LALGCWTQIT PCSLILACVL LSTHYAILLP GMQAQAARDA QRRTAAGIMK
NAVVDGIVAT DIPPLDGAGP LTEKKLGQLL LFAAAVTGVV ITRSPRSWSE LGVLGSAVGS
TLIEGSAGKF WNATTVTAMC NLFRGSYLAG VPLTYTIIRN SNPSNKRGGG IGETLGEKWK
ARLNQMNTLE FHRYRRSHIM EVDREPARAA LKSGDFTRGA AVSRGSAKLR WMHERGYIRL
HDKVVDLGCG RGGWCYYSAT VKEVKEVKGY TKGGRGHEEP VLTQSYGWNI VQMKSGVDVF
YKEAEPCDVV LCDIGECSSS PAVEADRSTK VLELAERWLE RNDGADFCIK VLCPYMPEVV
EKLSKLQLRY GGCLVRNPLS RNSTHEMYWV SGYKGNLIGV INSTSALLLR RMEIKFAEPR
YEEDVNLSCG TRAVSIAPPK FDYKKIGQRV ERLKAEHMST WHYDCEHPYR TWAYHGSYVV
KPSGSASSQV NGVVKLLSKP WDVSSEVTGM SMTDTTPFGQ QRVFKEKVDT KAPEPPAGAE
MASVIVSEWL WKRLNREKKP RLCTKEEFVR KVRGNAALGP VFEEENQWKD AAEAVQDPGF
WNLVDMERKN HLEGKCETCV YNMMGKREKK RGEFGKAKGS RAIWYMWLGA RFLEFEALGF
LNEDHWMSRG NSGGGVEGLG IQKLGYVMRE IGEKGGILYA DDTAGWDTRI TECDLRNEAH
IMEYMENEHR KLARAIFELT YKHKVVKVMR PGKGVPLMDI ISREDQRGSG QVVTYALNTF
TNLVVQLIRM AEAECVLTPE DLHEMSQSAK LRLLKWLKEE GWERLTRMAV SGDDCVVAAP
DARFGAALTF LNAMSKIRKD IKEWTPSKGW KNWEEVPFCS HHFHRLQMKD GRELVVPCRS
QDELIGRARV TQGPGDLMSS ACLAKAYAQM WQLLYFHRRD LRLMGNAICS AVPVDWVPTG
RTTWSIHGKG EWMTSENMLE VWNRVWIEEN EHMEDKTPVR EWTDIPYLGK REDPWCGSYI
GYRPRSTWAE NIKVPVNVIR VKIGGNKYQD YLGTQKRYES EKRVEFRGVL
