GenomeNet

Database: UniProt
Entry: P27909
LinkDB: P27909
Original site: P27909 
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   18-SEP-2019, entry version 147.
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;
DE              EC=2.1.1.57;
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; 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-
RT   Sman, and identification of a type-specific genetic marker for dengue
RT   and tick-borne 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.,
RA   Rey F., Deubel V., Despres P.;
RT   "Genome analysis of dengue type-1 virus isolated between 1990 and 2001
RT   in Brazil reveals a remarkable conservation of the structural proteins
RT   but 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
CC       forms the core of a mature virus particle. During virus entry, may
CC       induce genome penetration in host cytoplasm after hemifusion
CC       induced by surface proteins. Can migrate tot cell nucleus where it
CC       modulates host functions. {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: Peptide pr: Prevents premature fusion activity of
CC       envelope proteins in trans Golgi by binding to envelope protein E
CC       at pH6.0. After virion release in extracellular space gets
CC       dissociated from E 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
CC       avoid catastrophic activation of the viral fusion activity in
CC       acidic GolGi compartment prior to virion release. prM-E cleavage
CC       is 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: Small envelope protein M: May play a role in virus
CC       budding. Exerts cytotoxic effects by activating a mitochondrial
CC       apoptotic pathway through M extodomain. May display a viroporin
CC       activity. {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: Envelope protein E: Binds to host cell surface receptor
CC       and mediates fusion between viral and cellular membranes. Envelope
CC       protein is synthesized in the endoplasmic reticulum in the form of
CC       heterodimer with protein prM. They play a role in virion budding
CC       in the ER, and the newly formed immature particle is covered with
CC       60 spikes composed of heterodimer between precursor prM and
CC       envelope protein E. The virion is transported to the Golgi
CC       apparatus where the low pH causes dissociation of PrM-E
CC       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
CC       polyprotein, is targeted to three destinations: the viral
CC       replication cycle, the plasma membrane and the extracellular
CC       compartment. May play a role in viral genome replication. Assist
CC       membrane bending and envelopment of genomic RNA at the endoplasmic
CC       reticulum. Excreted as a hexameric lipoparticle that plays a role
CC       against host immune responce. {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: Non-structural protein 2A: Component of the viral RNA
CC       replication complex that functions in virion assembly and
CC       antagonizes the host immune response.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: Non-structural protein 2B: Required cofactor for the
CC       serine protease function of NS3 (By similarity). May have
CC       membrane-destabilizing activity and form viroporins (By
CC       similarity). {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
CC       ProRule:PRU00859}.
CC   -!- FUNCTION: Serine protease NS3: Displays three enzymatic
CC       activities: serine protease, NTPase and RNA helicase. NS3 serine
CC       protease, in association with NS2B, performs its autocleavage and
CC       cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM,
CC       NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA
CC       helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.
CC       {ECO:0000255|PROSITE-ProRule:PRU00860}.
CC   -!- FUNCTION: Non-structural protein 4A: Regulates the ATPase activity
CC       of the NS3 helicase activity. NS4A allows NS3 helicase to conserve
CC       energy during unwinding. Plays a role in the inhibition of the
CC       host innate immune response. Interacts with host MAVS and thereby
CC       prevents the interaction between DDX58 and MAVS. In turn, IFN-beta
CC       production is impaired. {ECO:0000250|UniProtKB:P17763,
CC       ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and
CC       is 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,
CC       thereby preventing the establishment of cellular antiviral state
CC       by blocking the IFN-alpha/beta pathway.
CC       {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
CC       cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose
CC       2'-O positions. Besides its role in RNA genome replication, also
CC       prevents the establishment of cellular antiviral state by blocking
CC       the interferon-alpha/beta (IFN-alpha/beta) signaling pathway.
CC       Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing
CC       activation of JAK-STAT signaling pathway.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which
CC         each of the Xaa can be either Arg or Lys and Yaa can be either
CC         Ser or Ala.; 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:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
CC         ChEBI:CHEBI:83400; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside
CC         5'-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)-guanosine in mRNA + S-
CC         adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-guanosine in mRNA + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60856, Rhea:RHEA-COMP:15681,
CC         Rhea:RHEA-COMP:15683, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:143971, ChEBI:CHEBI:143975; EC=2.1.1.56;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-adenosine in mRNA + S-
CC         adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-adenosine in mRNA + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60852, Rhea:RHEA-COMP:15680,
CC         Rhea:RHEA-COMP:15682, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:143973, ChEBI:CHEBI:143974; EC=2.1.1.56;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00924};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-guanosine
CC         in mRNA + S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-
CC         triphosphoguanosine)-(2'-O-methyl-guanosine) in mRNA + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:60864, Rhea:RHEA-
CC         COMP:15683, Rhea:RHEA-COMP:15685, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143975,
CC         ChEBI:CHEBI:143977; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00924};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-adenosine
CC         in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-(2'-O-methyl-adenosine) in mRNA + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:60860, Rhea:RHEA-
CC         COMP:15682, Rhea:RHEA-COMP:15684, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143974,
CC         ChEBI:CHEBI:143976; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00924};
CC   -!- SUBUNIT: Capsid protein C: Homodimer. Interacts (via N-terminus)
CC       with host EXOC1 (via C-terminus); this interaction results in
CC       EXOC1 degradation through the proteasome degradation pathway.
CC       Protein prM: Forms heterodimers with envelope protein E in the
CC       endoplasmic reticulum and Golgi. Envelope protein E: Homodimer; in
CC       the endoplasmic reticulum and Golgi. Interacts with protein prM.
CC       Interacts with non-structural protein 1. Non-structural protein 1:
CC       Homodimer; Homohexamer when secreted. Interacts with envelope
CC       protein E. Non-structural protein 2A: Interacts (via N-terminus)
CC       with serine protease NS3. Non-structural protein 2B: Forms a
CC       heterodimer with serine protease NS3. May form homooligomers.
CC       Serine protease NS3: Forms a heterodimer with NS2B. Interacts with
CC       NS4B. Interacts with unphosphorylated RNA-directed RNA polymerase
CC       NS5; this interaction stimulates RNA-directed RNA polymerase NS5
CC       guanylyltransferase activity. Interacts with host SHFL. Non-
CC       structural protein 4A: Interacts with host MAVS; this interaction
CC       inhibits the synthesis of IFN-beta. Interacts with host SHFL. Non-
CC       structural protein 4B: Interacts with serine protease NS3. RNA-
CC       directed RNA polymerase NS5: Homodimer. Interacts with host STAT2;
CC       this interaction inhibits the phosphorylation of the latter, and,
CC       when all viral proteins are present (polyprotein), targets STAT2
CC       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
CC       membrane {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
CC       ProRule:PRU00860}; Multi-pass membrane protein
CC       {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
CC       membrane {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
CC       ProRule:PRU00860}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted
CC       {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
CC       membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral
CC       membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Lumenal
CC       side {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 2A-alpha: Host
CC       endoplasmic reticulum membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic
CC       reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Multi-
CC       pass membrane protein {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host
CC       endoplasmic reticulum membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}; Peripheral membrane protein
CC       {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
CC       ProRule:PRU00860}.
CC   -!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic
CC       reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860};
CC       Peripheral membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}. Note=Remains non-covalently associated to NS3
CC       protease. {ECO:0000255|PROSITE-ProRule:PRU00860}.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass
CC       membrane protein {ECO:0000250|UniProtKB:P17763}. Host
CC       mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-
CC       associated vesicles hosting the replication complex. Interacts
CC       with host MAVS in the mitochondrion-associated endoplasmic
CC       reticulum membranes. {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic
CC       reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Multi-
CC       pass membrane protein {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase NS5: Host
CC       endoplasmic reticulum membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00860}; Peripheral membrane protein
CC       {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side
CC       {ECO:0000255|PROSITE-ProRule:PRU00860}. Host nucleus
CC       {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated
CC       vesicles hosting the replication complex.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- DOMAIN: Transmembrane domains of the small envelope protein M and
CC       envelope protein E contains an endoplasmic reticulum retention
CC       signals. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: Genome polyprotein: Specific enzymatic cleavages in vivo
CC       yield mature proteins. Cleavages in the lumen of endoplasmic
CC       reticulum are performed by host signal peptidase, wereas cleavages
CC       in the cytoplasmic side are performed by the Serine protease NS3.
CC       Signal cleavage at the 2K-4B site requires a prior NS3 protease-
CC       mediated cleavage at the 4A-2K site.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: Non-structural protein 2A-alpha: A C-terminally truncated
CC       form of non-structural protein 2A, results from partial cleavage
CC       by NS3. {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.
CC       This cleavage is incomplete as up to 30% of viral particles still
CC       carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: Non-structural protein 1: The excreted form is glycosylated
CC       and this is required for efficient secretion of the protein from
CC       infected cells. {ECO:0000250|UniProtKB:P17763}.
CC   -!- PTM: RNA-directed RNA polymerase NS5: Phosphorylated on serines
CC       residues. This phosphorylation may trigger NS5 nuclear
CC       localization. {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
CC       SAM-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="http://www.viprbrc.org/brc/home.do?decorator=flavi_dengue";
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   PRIDE; P27909; -.
DR   ABCD; P27909; -.
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: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; IEA:UniProtKB-KW.
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:0039545; P:suppression by virus of host MAVS activity; IEA:UniProtKB-KW.
DR   GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039574; P:suppression by virus of host TYK2 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; 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   InterPro; IPR011492; DEAD_Flavivir.
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; rRNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases.
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; 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; Complete proteome; 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;
KW   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;
KW   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; Transcription;
KW   Transcription regulation; Transferase; Transmembrane;
KW   Transmembrane helix; Transport; Viral attachment to host cell;
KW   Viral envelope protein; Viral immunoevasion; Viral ion channel;
KW   Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW   Virus endocytosis by host; Virus entry into host cell.
FT   CHAIN         1   3392       Genome polyprotein.
FT                                /FTId=PRO_0000405203.
FT   CHAIN         1    100       Protein C.
FT                                {ECO:0000250|UniProtKB:P17763}.
FT                                /FTId=PRO_0000264634.
FT   PROPEP      101    114       ER anchor for the protein C, removed in
FT                                mature form by serine protease NS3.
FT                                /FTId=PRO_0000264635.
FT   CHAIN       115    280       Protein prM.
FT                                {ECO:0000250|UniProtKB:P17763}.
FT                                /FTId=PRO_0000264636.
FT   CHAIN       115    205       Peptide pr.
FT                                {ECO:0000250|UniProtKB:P17763}.
FT                                /FTId=PRO_0000264637.
FT   CHAIN       206    280       Small envelope protein M.
FT                                {ECO:0000250|UniProtKB:P17763}.
FT                                /FTId=PRO_0000264638.
FT   CHAIN       281    775       Envelope protein E.
FT                                {ECO:0000250|UniProtKB:P17763}.
FT                                /FTId=PRO_0000264639.
FT   CHAIN       776   1127       Non-structural protein 1.
FT                                {ECO:0000250|UniProtKB:P17763}.
FT                                /FTId=PRO_0000264640.
FT   CHAIN      1128   1345       Non-structural protein 2A.
FT                                {ECO:0000250|UniProtKB:P17763}.
FT                                /FTId=PRO_0000264641.
FT   CHAIN      1128   1315       Non-structural protein 2A-alpha.
FT                                {ECO:0000250|UniProtKB:P17763}.
FT                                /FTId=PRO_0000264642.
FT   CHAIN      1346   1475       Serine protease subunit NS2B.
FT                                {ECO:0000250|UniProtKB:P17763}.
FT                                /FTId=PRO_0000264643.
FT   CHAIN      1476   2094       Serine protease NS3.
FT                                {ECO:0000250|UniProtKB:P17763}.
FT                                /FTId=PRO_0000264644.
FT   CHAIN      2095   2221       Non-structural protein 4A.
FT                                {ECO:0000250|UniProtKB:P17763}.
FT                                /FTId=PRO_0000264645.
FT   PEPTIDE    2222   2244       Peptide 2k.
FT                                /FTId=PRO_0000264646.
FT   CHAIN      2245   2493       Non-structural protein 4B.
FT                                {ECO:0000250|UniProtKB:P17763}.
FT                                /FTId=PRO_0000264647.
FT   CHAIN      2494   3392       RNA-directed RNA polymerase NS5.
FT                                {ECO:0000250|UniProtKB:P17763}.
FT                                /FTId=PRO_0000264648.
FT   TOPO_DOM      1    101       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    102    119       Helical. {ECO:0000255}.
FT   TOPO_DOM    120    242       Extracellular. {ECO:0000255}.
FT   TRANSMEM    243    260       Helical. {ECO:0000255}.
FT   TOPO_DOM    261    261       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    262    280       Helical. {ECO:0000255}.
FT   TOPO_DOM    281    725       Extracellular. {ECO:0000255}.
FT   INTRAMEM    726    746       Helical. {ECO:0000255}.
FT   TOPO_DOM    747    752       Extracellular. {ECO:0000255}.
FT   INTRAMEM    753    775       Helical. {ECO:0000255}.
FT   TOPO_DOM    776   1125       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1126   1146       Helical. {ECO:0000255}.
FT   TOPO_DOM   1147   1157       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1158   1178       Helical. {ECO:0000255}.
FT   TOPO_DOM   1179   1199       Lumenal. {ECO:0000255}.
FT   TRANSMEM   1200   1220       Helical. {ECO:0000255}.
FT   TOPO_DOM   1221   1289       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1290   1310       Helical. {ECO:0000255}.
FT   TOPO_DOM   1311   1315       Lumenal. {ECO:0000255}.
FT   TRANSMEM   1316   1336       Helical. {ECO:0000255}.
FT   TOPO_DOM   1337   1346       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1347   1367       Helical. {ECO:0000255}.
FT   TOPO_DOM   1368   1370       Lumenal. {ECO:0000255}.
FT   TRANSMEM   1371   1391       Helical. {ECO:0000255}.
FT   TOPO_DOM   1392   1447       Cytoplasmic. {ECO:0000255}.
FT   INTRAMEM   1448   1468       Helical. {ECO:0000255}.
FT   TOPO_DOM   1469   2148       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2149   2169       Helical. {ECO:0000255}.
FT   TOPO_DOM   2170   2171       Lumenal. {ECO:0000255}.
FT   INTRAMEM   2172   2192       Helical. {ECO:0000255}.
FT   TOPO_DOM   2193   2193       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2194   2214       Helical. {ECO:0000255}.
FT   TOPO_DOM   2215   2229       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2230   2250       Helical; Note=Signal for NS4B.
FT                                {ECO:0000255}.
FT   TOPO_DOM   2251   2276       Lumenal. {ECO:0000255}.
FT   INTRAMEM   2277   2297       Helical. {ECO:0000255}.
FT   TOPO_DOM   2298   2349       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2350   2370       Helical. {ECO:0000255}.
FT   TOPO_DOM   2371   2415       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2416   2436       Helical. {ECO:0000255}.
FT   TOPO_DOM   2437   2461       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2462   2482       Helical. {ECO:0000255}.
FT   TOPO_DOM   2483   3392       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN     1476   1653       Peptidase S7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   DOMAIN     1656   1812       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1822   1989       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     2495   2756       mRNA cap 0-1 NS5-type MT.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   DOMAIN     3021   3170       RdRp catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00539}.
FT   NP_BIND    1669   1676       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION       33     74       Hydrophobic; homodimerization of capsid
FT                                protein C. {ECO:0000250}.
FT   REGION     1398   1437       Interacts with and activates NS3
FT                                protease. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00859}.
FT   MOTIF      1760   1763       DEAH box.
FT   ACT_SITE   1526   1526       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   ACT_SITE   1550   1550       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   ACT_SITE   1610   1610       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   BINDING    2549   2549       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2579   2579       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2580   2580       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2597   2597       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2598   2598       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2624   2624       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2625   2625       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2640   2640       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2711   2711       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE        100    101       Cleavage; by viral protease NS3.
FT                                {ECO:0000255}.
FT   SITE        114    115       Cleavage; by host signal peptidase.
FT                                {ECO:0000250}.
FT   SITE        205    206       Cleavage; by host furin. {ECO:0000255}.
FT   SITE        280    281       Cleavage; by host signal peptidase.
FT                                {ECO:0000255}.
FT   SITE        775    776       Cleavage; by host signal peptidase.
FT                                {ECO:0000255}.
FT   SITE       1127   1128       Cleavage; by host. {ECO:0000255}.
FT   SITE       1345   1346       Cleavage; by viral protease NS3.
FT                                {ECO:0000255}.
FT   SITE       1475   1476       Cleavage; by autolysis. {ECO:0000255}.
FT   SITE       2094   2095       Cleavage; by autolysis. {ECO:0000255}.
FT   SITE       2221   2222       Cleavage; by viral protease NS3.
FT                                {ECO:0000255}.
FT   SITE       2244   2245       Cleavage; by host signal peptidase.
FT                                {ECO:0000255}.
FT   SITE       2493   2494       Cleavage; by viral protease NS3.
FT                                {ECO:0000255}.
FT   SITE       2507   2507       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2510   2510       mRNA cap binding; via carbonyl oxygen.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE       2511   2511       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2513   2513       mRNA cap binding; via carbonyl oxygen.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE       2518   2518       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2522   2522       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2554   2554       Essential for 2'-O-methyltransferase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2639   2639       Essential for 2'-O-methyltransferase and
FT                                N-7 methyltransferase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE       2643   2643       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2673   2673       Essential for 2'-O-methyltransferase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2704   2704       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2706   2706       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2709   2709       Essential for 2'-O-methyltransferase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   CARBOHYD    183    183       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    347    347       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    433    433       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    905    905       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    982    982       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   1190   1190       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   2303   2303       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   2307   2307       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   2459   2459       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   DISULFID    283    310       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    340    401       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    354    385       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    372    396       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    465    565       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    582    613       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    779    790       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    830    918       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    954    998       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID   1055   1104       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID   1066   1088       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID   1087   1091       {ECO:0000250|UniProtKB:P17763}.
FT   VARIANT     394    394       L -> I (in strain: Isolate Thailand/TH-
FT                                Sman/1958).
FT   VARIANT     402    402       V -> A (in strain: Isolate Thailand/TH-
FT                                Sman/1958).
FT   VARIANT     441    441       I -> T (in strain: Isolate Thailand/TH-
FT                                Sman/1958).
FT   VARIANT     475    476       EM -> RV (in strain: Isolate 924-1).
FT   VARIANT     483    483       E -> K (in strain: Isolate 924-1).
FT   VARIANT     531    531       V -> A (in strain: Isolate 924-1 and
FT                                Isolate Thailand/TH-Sman/1958).
FT   VARIANT     577    577       T -> M (in strain: Isolate 924-1 and
FT                                Isolate Thailand/TH-Sman/1958).
FT   VARIANT     619    619       T -> S (in strain: Isolate 924-1).
FT   VARIANT     649    649       T -> E (in strain: Isolate 924-1 and
FT                                Isolate Thailand/TH-Sman/1958).
FT   VARIANT     677    677       S -> I (in strain: Isolate Thailand/TH-
FT                                Sman/1958n).
FT   VARIANT     712    712       V -> M (in strain: Isolate Thailand/TH-
FT                                Sman/1958).
FT   VARIANT     716    716       V -> I (in strain: Isolate 924-1).
FT   VARIANT     719    719       V -> I (in strain: Isolate 924-1).
FT   VARIANT     752    752       S -> N (in strain: Isolate Thailand/TH-
FT                                Sman/1958).
FT   VARIANT     758    758       T -> M (in strain: Isolate Thailand/TH-
FT                                Sman/1958).
FT   STRAND      586    590       {ECO:0000244|PDB:3UZQ}.
FT   STRAND      600    606       {ECO:0000244|PDB:3UZQ}.
FT   STRAND      612    614       {ECO:0000244|PDB:3UZQ}.
FT   STRAND      617    621       {ECO:0000244|PDB:3UZQ}.
FT   STRAND      633    635       {ECO:0000244|PDB:3UZQ}.
FT   STRAND      637    639       {ECO:0000244|PDB:3UZQ}.
FT   STRAND      645    649       {ECO:0000244|PDB:3UZQ}.
FT   STRAND      653    663       {ECO:0000244|PDB:3UZQ}.
FT   STRAND      666    673       {ECO:0000244|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
//
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