POLG_DEN1B
ID POLG_DEN1B Reviewed; 3392 AA.
AC P27909; P29983; Q8B648;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=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=Non-structural protein 2A-alpha;
DE Short=NS2A-alpha;
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=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;
DE AltName: Full=Non-structural protein 5;
OS Dengue virus type 1 (strain Brazil/97-11/1997) (DENV-1).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Flavivirus.
OX NCBI_TaxID=408685;
OH NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OH NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 232-786.
RC STRAIN=Isolate Caribbean/924-1;
RX PubMed=2738579; DOI=10.1099/0022-1317-70-7-1701;
RA Chu M.C., O'Rourke E.J., Trent D.W.;
RT "Genetic relatedness among structural protein genes of dengue 1 virus
RT strains.";
RL J. Gen. Virol. 70:1701-1712(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 281-778.
RC STRAIN=Isolate Thailand/TH-Sman/1958;
RX PubMed=1339466; DOI=10.1099/0022-1317-73-1-207;
RA Shiu S.Y.W., Jiang W.R., Porterfield J.S., Gould E.A.;
RT "Envelope protein sequences of dengue virus isolates TH-36 and TH-Sman, and
RT identification of a type-specific genetic marker for dengue and tick-borne
RT flaviviruses.";
RL J. Gen. Virol. 73:207-212(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12457974; DOI=10.1016/s0168-1702(02)00180-6;
RA Duarte dos Santos C.N., Rocha C.F.S., Cordeiro M., Fragoso S.P., Rey F.,
RA Deubel V., Despres P.;
RT "Genome analysis of dengue type-1 virus isolated between 1990 and 2001 in
RT Brazil reveals a remarkable conservation of the structural proteins but
RT amino acid differences in the non-structural proteins.";
RL Virus Res. 90:197-205(2002).
CC -!- FUNCTION: [Protein C]: Plays a role in virus budding by binding to
CC membrane and gathering the viral RNA into a nucleocapsid that forms the
CC core of a mature virus particle. During virus entry, may induce genome
CC penetration in host cytoplasm after hemifusion induced by surface
CC proteins. Can migrate tot cell nucleus where it modulates host
CC functions. {ECO:0000250|UniProtKB:P17763}.
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. Presumably to avoid
CC catastrophic activation of the viral fusion activity in acidic GolGi
CC compartment prior to virion release. prM-E cleavage is ineficient, 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 extodomain. 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 ineficient, 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. May play a role in
CC viral genome replication. Assist membrane bending and envelopment of
CC genomic RNA at the endoplasmic reticulum. Excreted as a hexameric
CC lipoparticle that plays a role against host immune response.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Non-structural protein 2A]: Component of the viral RNA
CC replication complex that functions in virion assembly and antagonizes
CC the host immune response. {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the
CC serine protease function of NS3 (By similarity). May have membrane-
CC destabilizing activity and form viroporins (By similarity).
CC {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00859}.
CC -!- FUNCTION: [Serine protease NS3]: Displays three enzymatic activities:
CC serine protease, NTPase and RNA helicase. NS3 serine protease, in
CC association with NS2B, performs its autocleavage and cleaves the
CC polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-
CC NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and
CC unwinds dsRNA in the 3' to 5' direction. {ECO:0000255|PROSITE-
CC ProRule:PRU00860}.
CC -!- FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of
CC the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy
CC during unwinding. Plays a role in the inhibition of the host innate
CC immune response. Interacts with host MAVS and thereby prevents the
CC interaction between DDX58 and MAVS. In turn, IFN-beta production is
CC impaired. Interacts with host AUP1 which mediates induction of
CC lipophagy in host cells and facilitates production of virus progeny
CC particles (By similarity). {ECO:0000250|UniProtKB:P17763,
CC ECO:0000250|UniProtKB:P29991, 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]: Inhibits interferon (IFN)-
CC induced host STAT1 phosphorylation and nuclear translocation, thereby
CC preventing the establishment of cellular antiviral state by blocking
CC the IFN-alpha/beta pathway. {ECO:0000250|UniProtKB:P17763}.
CC -!- FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+)
CC and (-) genome, and performs the capping of genomes in the cytoplasm.
CC NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions.
CC Besides its role in RNA genome replication, also prevents the
CC establishment of cellular antiviral state by blocking the interferon-
CC alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and
CC STAT2 phosphorylation, thereby preventing activation of JAK-STAT
CC signaling pathway. {ECO:0000250|UniProtKB:P17763}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of
CC the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.;
CC EC=3.4.21.91;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase NS5]:
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: [RNA-directed RNA polymerase NS5]:
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. Interacts (via N-terminus) with
CC host EXOC1 (via C-terminus); this interaction results in EXOC1
CC degradation through the proteasome degradation pathway.
CC {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. Interacts with protein prM. Interacts with non-structural
CC protein 1. {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Non-structural protein 1]: Homodimer; Homohexamer when
CC secreted. Interacts with envelope protein E.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Non-structural protein 2A]: Interacts (via N-terminus) with
CC serine protease NS3. {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. Interacts with host SHFL.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Non-structural protein 4A]: Interacts with host MAVS; this
CC interaction inhibits the synthesis of IFN-beta. Interacts with host
CC SHFL. Interacts with host AUP1; the interaction occurs in the presence
CC of Dengue virus NS4B and induces lipophagy which facilitates production
CC of virus progeny particles (By similarity).
CC {ECO:0000250|UniProtKB:P17763, ECO:0000250|UniProtKB:P29991}.
CC -!- SUBUNIT: [Non-structural protein 4B]: Interacts with serine protease
CC NS3. {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [RNA-directed RNA polymerase NS5]: Homodimer. Interacts with
CC host STAT2; this interaction inhibits the phosphorylation of the
CC latter, and, when all viral proteins are present (polyprotein), targets
CC STAT2 for degradation. Interacts with serine protease NS3.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Protein C]: Virion
CC {ECO:0000250|UniProtKB:P17763}. Host nucleus
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:P17763}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00860};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane
CC {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-ProRule:PRU00860};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted
CC {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane
CC {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00860}; Lumenal side
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 2A-alpha]: Host
CC endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic
CC reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic
CC reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
CC ProRule:PRU00860}.
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 NS3 protease. {ECO:0000255|PROSITE-ProRule:PRU00860}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P17763}. Host mitochondrion
CC {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles
CC hosting the replication complex. Interacts with host MAVS in the
CC mitochondrion-associated endoplasmic reticulum membranes.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic
CC reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host
CC endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860};
CC Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860};
CC Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Host nucleus
CC {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles
CC hosting the replication complex. {ECO:0000250|UniProtKB:P17763}.
CC -!- DOMAIN: Transmembrane domains of the small envelope protein M and
CC envelope protein E contains an endoplasmic reticulum retention signals.
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, wereas cleavages in the cytoplasmic
CC side are performed by the Serine protease NS3. Signal cleavage at the
CC 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K
CC site. {ECO:0000250|UniProtKB:P17763}.
CC -!- PTM: [Non-structural protein 2A-alpha]: A C-terminally truncated form
CC of non-structural protein 2A, results from partial cleavage by NS3.
CC {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: [Non-structural protein 1]: The excreted form is glycosylated and
CC this is required for efficient secretion of the protein from infected
CC 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 -!- PTM: [Envelope protein E]: N-glycosylated.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- PTM: [Non-structural protein 1]: N-glycosylated.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the class I-like SAM-
CC binding methyltransferase superfamily. mRNA cap 0-1 NS5-type
CC methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}.
CC -!- WEB RESOURCE: Name=Virus Pathogen Resource;
CC URL="https://www.viprbrc.org/brc/home.spg?decorator=flavi_dengue";
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DR EMBL; D00504; BAA00396.1; -; Genomic_RNA.
DR EMBL; D10513; BAA01388.1; -; Genomic_RNA.
DR EMBL; AF311956; AAN60368.1; -; Genomic_RNA.
DR PIR; JQ1405; JQ1405.
DR PDB; 3UZQ; X-ray; 1.60 A; B=578-680.
DR PDBsum; 3UZQ; -.
DR SMR; P27909; -.
DR ELM; P27909; -.
DR MEROPS; S07.001; -.
DR PRIDE; P27909; -.
DR ABCD; P27909; 1 sequenced antibody.
DR PRO; PR:P27909; -.
DR Proteomes; UP000007764; 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:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044385; C:integral to membrane of host cell; 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:0005216; F:ion channel activity; IEA:UniProtKB-KW.
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; ISS:UniProtKB.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039574; P:suppression by virus of host JAK-STAT cascade via inhibition of host TYK2 activity; IEA:UniProtKB-KW.
DR GO; GO: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:0039545; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; 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; 2.40.10.10; -; 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; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000208; RNA-dir_pol_flavivirus.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01003; Flavi_capsid; 1.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF02832; Flavi_glycop_C; 1.
DR Pfam; PF00869; Flavi_glycoprot; 1.
DR Pfam; PF01004; Flavi_M; 1.
DR Pfam; PF00948; Flavi_NS1; 1.
DR Pfam; PF01005; Flavi_NS2A; 1.
DR Pfam; PF01002; Flavi_NS2B; 1.
DR Pfam; PF01350; Flavi_NS4A; 1.
DR Pfam; PF01349; Flavi_NS4B; 1.
DR Pfam; PF00972; Flavi_NS5; 1.
DR Pfam; PF01570; Flavi_propep; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF00949; Peptidase_S7; 1.
DR PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF101257; SSF101257; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF56983; SSF56983; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR04240; flavi_E_stem; 1.
DR PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
DR PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; ATP-binding;
KW Capsid protein; Clathrin-mediated endocytosis of virus by host;
KW Cleavage on pair of basic residues; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
KW Host endoplasmic reticulum; Host membrane; Host mitochondrion;
KW Host nucleus; 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 MAVS by virus; Inhibition of host RLR pathway by virus;
KW Inhibition of host STAT2 by virus; Inhibition of host TYK2 by virus;
KW Ion channel; Ion transport; Membrane; Metal-binding; Methyltransferase;
KW mRNA capping; mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Protease; RNA-binding;
KW RNA-directed RNA polymerase; S-adenosyl-L-methionine; Secreted;
KW Serine protease; Transcription; Transcription regulation; Transferase;
KW Transmembrane; Transmembrane helix; Transport;
KW Viral attachment to host cell; Viral envelope protein; Viral immunoevasion;
KW Viral ion channel; Viral penetration into host cytoplasm;
KW Viral RNA replication; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT CHAIN 1..3392
FT /note="Genome polyprotein"
FT /id="PRO_0000405203"
FT CHAIN 1..100
FT /note="Protein C"
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT /id="PRO_0000264634"
FT PROPEP 101..114
FT /note="ER anchor for the protein C, removed in mature form
FT by serine protease NS3"
FT /id="PRO_0000264635"
FT CHAIN 115..280
FT /note="Protein prM"
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT /id="PRO_0000264636"
FT CHAIN 115..205
FT /note="Peptide pr"
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT /id="PRO_0000264637"
FT CHAIN 206..280
FT /note="Small envelope protein M"
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT /id="PRO_0000264638"
FT CHAIN 281..775
FT /note="Envelope protein E"
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT /id="PRO_0000264639"
FT CHAIN 776..1127
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT /id="PRO_0000264640"
FT CHAIN 1128..1345
FT /note="Non-structural protein 2A"
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT /id="PRO_0000264641"
FT CHAIN 1128..1315
FT /note="Non-structural protein 2A-alpha"
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT /id="PRO_0000264642"
FT CHAIN 1346..1475
FT /note="Serine protease subunit NS2B"
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT /id="PRO_0000264643"
FT CHAIN 1476..2094
FT /note="Serine protease NS3"
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT /id="PRO_0000264644"
FT CHAIN 2095..2221
FT /note="Non-structural protein 4A"
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT /id="PRO_0000264645"
FT PEPTIDE 2222..2244
FT /note="Peptide 2k"
FT /id="PRO_0000264646"
FT CHAIN 2245..2493
FT /note="Non-structural protein 4B"
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT /id="PRO_0000264647"
FT CHAIN 2494..3392
FT /note="RNA-directed RNA polymerase NS5"
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT /id="PRO_0000264648"
FT TOPO_DOM 1..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..725
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 726..746
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 747..752
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 753..775
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 776..1125
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1126..1146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1147..1157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1158..1178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1179..1199
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1200..1220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1221..1289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1290..1310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1311..1315
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1316..1336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1337..1346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1347..1367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1368..1370
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1371..1391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1392..1447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1448..1468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1469..2148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2149..2169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2170..2171
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 2172..2192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2193
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2194..2214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2215..2229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2230..2250
FT /note="Helical; Note=Signal for NS4B"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2251..2276
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 2277..2297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2298..2349
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2350..2370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2371..2415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2416..2436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2437..2461
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2462..2482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2483..3392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1476..1653
FT /note="Peptidase S7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT DOMAIN 1656..1812
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1822..1989
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2495..2756
FT /note="mRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT DOMAIN 3021..3170
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 33..74
FT /note="Hydrophobic; homodimerization of capsid protein C"
FT /evidence="ECO:0000250"
FT REGION 1398..1437
FT /note="Interacts with and activates NS3 protease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00859"
FT MOTIF 1760..1763
FT /note="DEAH box"
FT ACT_SITE 1526
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 1550
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT ACT_SITE 1610
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860"
FT BINDING 1669..1676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 2549
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2579
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2580
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2597
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2598
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2624
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2625
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2640
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT BINDING 2711
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 100..101
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000255"
FT SITE 114..115
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 205..206
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255"
FT SITE 280..281
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000255"
FT SITE 775..776
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000255"
FT SITE 1127..1128
FT /note="Cleavage; by host"
FT /evidence="ECO:0000255"
FT SITE 1345..1346
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000255"
FT SITE 1475..1476
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255"
FT SITE 2094..2095
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255"
FT SITE 2221..2222
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000255"
FT SITE 2244..2245
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000255"
FT SITE 2493..2494
FT /note="Cleavage; by viral protease NS3"
FT /evidence="ECO:0000255"
FT SITE 2507
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2510
FT /note="mRNA cap binding; via carbonyl oxygen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2511
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2513
FT /note="mRNA cap binding; via carbonyl oxygen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2518
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2522
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2554
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2639
FT /note="Essential for 2'-O-methyltransferase and N-7
FT methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2643
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2673
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2704
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2706
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT SITE 2709
FT /note="Essential for 2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 905
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 982
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1190
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2303
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2307
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2459
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 283..310
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 340..401
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 354..385
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 372..396
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 465..565
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 582..613
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 779..790
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 830..918
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 954..998
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1055..1104
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1066..1088
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 1087..1091
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT VARIANT 394
FT /note="L -> I (in strain: Isolate Thailand/TH-Sman/1958)"
FT VARIANT 402
FT /note="V -> A (in strain: Isolate Thailand/TH-Sman/1958)"
FT VARIANT 441
FT /note="I -> T (in strain: Isolate Thailand/TH-Sman/1958)"
FT VARIANT 475..476
FT /note="EM -> RV (in strain: Isolate 924-1)"
FT VARIANT 483
FT /note="E -> K (in strain: Isolate 924-1)"
FT VARIANT 531
FT /note="V -> A (in strain: Isolate 924-1 and Isolate
FT Thailand/TH-Sman/1958)"
FT VARIANT 577
FT /note="T -> M (in strain: Isolate 924-1 and Isolate
FT Thailand/TH-Sman/1958)"
FT VARIANT 619
FT /note="T -> S (in strain: Isolate 924-1)"
FT VARIANT 649
FT /note="T -> E (in strain: Isolate 924-1 and Isolate
FT Thailand/TH-Sman/1958)"
FT VARIANT 677
FT /note="S -> I (in strain: Isolate Thailand/TH-Sman/1958n)"
FT VARIANT 712
FT /note="V -> M (in strain: Isolate Thailand/TH-Sman/1958)"
FT VARIANT 716
FT /note="V -> I (in strain: Isolate 924-1)"
FT VARIANT 719
FT /note="V -> I (in strain: Isolate 924-1)"
FT VARIANT 752
FT /note="S -> N (in strain: Isolate Thailand/TH-Sman/1958)"
FT VARIANT 758
FT /note="T -> M (in strain: Isolate Thailand/TH-Sman/1958)"
FT STRAND 586..590
FT /evidence="ECO:0007829|PDB:3UZQ"
FT STRAND 600..606
FT /evidence="ECO:0007829|PDB:3UZQ"
FT STRAND 612..614
FT /evidence="ECO:0007829|PDB:3UZQ"
FT STRAND 617..621
FT /evidence="ECO:0007829|PDB:3UZQ"
FT STRAND 633..635
FT /evidence="ECO:0007829|PDB:3UZQ"
FT STRAND 637..639
FT /evidence="ECO:0007829|PDB:3UZQ"
FT STRAND 645..649
FT /evidence="ECO:0007829|PDB:3UZQ"
FT STRAND 653..663
FT /evidence="ECO:0007829|PDB:3UZQ"
FT STRAND 666..673
FT /evidence="ECO:0007829|PDB:3UZQ"
SQ SEQUENCE 3392 AA; 378905 MW; BBD894175578E164 CRC64;
MNNQRKKTGR PSFNMLKRAR NRVSTGSQLA KRFSKGLLSG QGPMKLVMAF IAFLRFLAIP
PTAGILARWS SFKKNGAIKV LRGFKKEISS MLNIMNRRKR SVTMLLMLLP TALAFHLTTR
GGEPHMIVSK QERGKSLLFK TSAGVNMCTL IAMDLGELCE DTMTYKCPRI TEAEPDDVDC
WCNATDTWVT YGTCSQTGEH RRDKRSVALA PHVGLGLETR TETWMSSEGA WKQIQKVETW
ALRHPGFTVI ALFLAHAIGT SITQKGIIFI LLMLVTPSMA MRCVGIGNRD FVEGLSGATW
VDVVLEHGSC VTTMAKNKPT LDIELLKTEV TNPAVLRKLC IEAKISNTTT DSRCPTQGEA
TLVEEQDANF VCRRTFVDRG WGNGCGLFGK GSLLTCAKFK CVTKLEGKIV QYENLKYSVI
VTVHTGDQHQ VGNETTEHGT IATITPQAPT SEIQLTDYGA LTLDCSPRTG LDFNEMVLLT
MKEKSWLVHK QWFLDLPLPW TSGASTSQET WNRQDLLVTF KTAHAKKQEV VVLGSQEGAM
HTALTGATEI QTSGTTTIFA GHLKCRLKMD KLTLKGTSYV MCTGSFKLEK EVAETQHGTV
LVQVKYEGTD APCKIPFSTQ DEKGVTQNGR LITANPIVTD KEKPVNIETE PPFGESYIVV
GAGEKALKLS WFKKGSSIGK MFEATARGAR RMAILGDTAW DFGSIGGVFT SVGKLVHQVF
GTAYGVLFSG VSWTMKIGIG ILLTWLGLNS RSTSLSMTCI AVGMVTLYLG VMVQADSGCV
INWKGRELKC GSGIFVTNEV HTWTEQYKFQ ADSPKRLSAA IGRAWEEGVC GIRSATRLEN
IMWKQISNEL NHILLENDIK FTVVVGNANG ILAQGKKMIR PQPMEHKYSW KSWGKAKIIG
ADIQNTTFII DGPDTPECPD EQRAWNIWEV EDYGFGIFTT NIWLKLRDSY TQMCDHRLMS
AAIKDSKAVH ADMGYWIESE KNETWKLARA SFIEVKTCIW PKSHTLWSNG VLESEMIIPK
MYGGPISQHN YRPGYFTQTA GPWHLGKLEL DFDLCEGTTV VVDEHCGSRG PSLRTTTVTG
KIIHEWCCRS CTLPPLRFRG EDGCWYGMEI RPVKEKEENL VRSMVSAGSG EVDSFSLGIL
CVSIMIEEVM RSRWSRKMLM TGTLAVFLLL IMGQLTWNDL IRLCIMVGAN ASDKMGMGTT
YLALMATFKM RPMFAVGLLF RRLTSREVLL LTIGLSLVAS VELPNSLEEL GDGLAMGIMM
LKLLTEFQPH QLWTTLLSLT FIKTTLSLDY AWKTTAMVLS IVSLFPLCLS TTSQKTTWLP
VLLGSFGCKP LTMFLITENE IWGRKSWPLN EGIMAIGIVS ILLSSLLKND VPLAGPLIAG
GMLIACYVIS GSSADLSLEK AAEVSWEEEA EHSGTSHNIL VEVQDDGTMK IKDEERDDTL
TILLKATLLA VSGVYPMSIP ATLFVWYFWQ KKKQRSGVLW DTPSPPEVER AVLDDGIYRI
LQRGLLGRSQ VGVGVFQDGV FHTMWHVTRG AVLMYQGKRL EPSWASVKKD LISYGGGWRF
QGSWNTGEEV QVIAVEPGKN PKNVQTTPGT FKTPEGEVGA IALDFKPGTS GSPIVNREGK
IVGLYGNGVV TTSGTYVSAI AQAKASQEGP LPEIEDEVFK KRNLTIMDLH PGSGKTRRYL
PAIVREAIKR KLRTLILAPT RVVASEMAEA LKGMPIRYQT TAVKSEHTGR EIVDLMCHAT
FTMRLLSPVR VPNYNMIIMD EAHFTDPASI AARGYISTRV GMGEAAAIFM TATPPGSVEA
FPQSNAVIQD EERDIPERSW NSGYDWITDF PGKTVWFVPS IKSGNDIANC LRKNGKRVIQ
LSRKTFDTEY QKTKNNDWDY VVTTDISEMG ANFRADRVID PRRCLKPVIL KDGPERVILA
GPMPVTVASA AQRRGRIGRN QNKEGDQYVY MGQPLNNDED HAHWTEAKML LDNINTPEGI
IPALFEPERE KSAAIDGEYR LRGEARKTFV ELMRRGDLPV WLSYKVASEG FQYSDRRWCF
DGERNNQVLE ENMDVEIWTK EGERKKLRPR WLDARTYSDP LALREFKEFA AGRRSVSGDL
ILEIGKLPQH LTLRAQNALD NLVMLHNSEQ GGKAYRHAME ELPDTIETLM LLALIAVLTG
GVTLFFLSGK GLGKTSIGLL CVTASSALLW MASVEPHWIA ASIILEFFLM VLLIPEPDRQ
RTPQDNQLAY VVIGLLFMIL TVAANEMGLL ETTKKDLGIG HVAAENHQHA TILDVDLHPA
SAWTLYAVAT TVITPMMRHT IENTTANISL TAIANQAAIL MGLDKGWPIS KMDLGVPLLA
LGCYSQVNPL TLTAAVLMLV AHYAIIGPGL QAKATREAQK RTAAGIMKNP TVDGIVAIDL
DPVVYDAKFE KQLGQIMLLI LCTSQILLMR TTWALCESIT LATGPLTTLW EGSPGKFWNT
TIAVSMANIF RGSYLAGAGL AFSLMKSLGG GRRGTGAQGE TLGEKWKRQL NQLSKSEFNT
YKRSGIMEVD RSEAKEGLKR GETTKHAVSR GTAKLRWFVE RNLVKPEGKV IDLGCGRGGW
SYYCAGLKKV TEVKGYTKGG PGHEEPIPMA TYGWNLVKLH SGKDVFFMPP EKCDTLLCDI
GESSPNPTIE EGRTLRVLKM VEPWLRGNQF CIKILNPYMP SVVETLEQMQ RKHGGMLVRN
PLSRNSTHEM YWVSCGTGNI VSAVNMTSRM LLNRFTMAHR KPTYERDVDL GAGTRHVAVE
PEVANLDIIG QRIENIKNEH KSTWHYDEDN PYKTWAYHGS YEVKPSGSAS SMVNGVVRLL
TKPWDVIPMV TQIAMTDTTP FGQQRVFKEK VDTRTPRAKR GTAQIMEVTA KWLWGFLSRN
KKPRICTREE FTRKVRSNAA IGAVFVDENQ WNSAKEAVED ERFWDLVHRE RELHKQGKCA
TCVYNMMGKR EKKLGEFGKA KGSRAIWYMW LGARFLEFEA LGFMNEDHWF SRENSLSGVE
GEGLHKLGYI LRDISKIPGG NMYADDTAGW DTRITEDDLQ NEAKITDIME PEHALLATSI
FKLTYQNKVV RVQRPAKNGT VMDVISRRDQ RGSGQVGTYG LNTFTNMEVQ LIRQMESEGI
FFPSELESPN LAERVLDWLE KHGAERLKRM AISGDDCVVK PIDDRFATAL IALNDMGKVR
KDIPQWEPSK GWNDWQQVPF CSHHFHQLIM KDGREIVVPC RNQDELVGRA RVSQGAGWSL
RETACLGKSY AQMWQLMYFH RRDLRLAANA ICSAVPVDWV PTSRTTWSIH AHHQWMTTED
MLSVWNRVWI EENPWMEDKT HVSSWEEVPY LGKREDQWCG SLIGLTARAT WATNIQVAIN
QVRRLIGNEN YLDYMTSMKR FKNESDPEGA LW
