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Database: UniProt
Entry: Q32ZD7
LinkDB: Q32ZD7
Original site: Q32ZD7 
ID   POLG_ILHV               Reviewed;        3424 AA.
AC   Q32ZD7;
DT   27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   16-OCT-2019, entry version 122.
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;
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 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE     AltName: Full=Non-structural protein 5;
OS   Ilheus virus (ILHV).
OC   Viruses; Riboviria; Flaviviridae; Flavivirus.
OX   NCBI_TaxID=59563;
OH   NCBI_TaxID=37951; Aedes sp..
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=7174; Culex.
OH   NCBI_TaxID=7180; Haemagogus.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=84836; Molothrus bonariensis (Shiny cowbird).
OH   NCBI_TaxID=190765; Ochlerotatus.
OH   NCBI_TaxID=7182; Psorophora.
OH   NCBI_TaxID=53551; Sabethes.
OH   NCBI_TaxID=256689; Sporophila caerulescens (double-collared seedeater).
OH   NCBI_TaxID=704162; Trichoprosopon.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC RNA].
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
RT   insights into components, mechanisms, and unique traits as well as
RT   their evolutionary trends.";
RL   Clin. Microbiol. Rev. 18:608-637(2005).
CC   -!- FUNCTION: Capsid protein C: Plays a role in virus budding by
CC       binding to the cell membrane and gathering the viral RNA into a
CC       nucleocapsid that forms the core of a mature virus particle.
CC       During virus entry, may induce genome penetration into the host
CC       cytoplasm after hemifusion induced by the surface proteins. Can
CC       migrate to the cell nucleus where it modulates host functions.
CC       Overcomes the anti-viral effects of host EXOC1 by sequestering and
CC       degrading the latter through the proteasome degradation pathway.
CC       {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
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 probably to avoid
CC       catastrophic activation of the viral fusion activity in acidic
CC       Golgi compartment prior to virion release. 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: Small envelope protein M: May play a role in virus
CC       budding. Exerts cytotoxic effects by activating a mitochondrial
CC       apoptotic pathway through M ectodomain. 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       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
CC       polyprotein, is targeted to three destinations: the viral
CC       replication cycle, the plasma membrane and the extracellular
CC       compartment. Essential for viral replication. Required for
CC       formation of the replication complex and recruitment of other non-
CC       structural proteins to the ER-derived membrane structures.
CC       Excreted as a hexameric lipoparticle that plays a role against
CC       host immune response. Antagonizing the complement function. Binds
CC       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
CC       antagonizes 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-
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. {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: 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
CC       cellular antiviral state by blocking the IFN-alpha/beta pathway.
CC       Inhibits STAT2 translocation in the nucleus after IFN-alpha
CC       treatment. {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
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:Q9Q6P4}.
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         Evidence={ECO:0000250|UniProtKB:Q9Q6P4};
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. NS1 interacts with NS4B.
CC       Interacts with host complement protein CFH; this interaction leads
CC       to the degradation of C3. Non-structural protein 2A: Interacts
CC       (via N-terminus) with serine protease NS3. Non-structural protein
CC       2B: Forms a heterodimer with serine protease NS3. May form
CC       homooligomers. Serine protease NS3: Forms a heterodimer with NS2B.
CC       Interacts with NS4B. Interacts with unphosphorylated RNA-directed
CC       RNA polymerase NS5; this interaction stimulates RNA-directed RNA
CC       polymerase NS5 guanylyltransferase activity. Non-structural
CC       protein 4B: Interacts with serine protease NS3. RNA-directed RNA
CC       polymerase NS5: Homodimer. Interacts with host STAT2; this
CC       interaction inhibits the phosphorylation of the latter, and, when
CC       all viral proteins are present (polyprotein), targets STAT2 for
CC       degradation. Interacts with serine protease NS3.
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
CC       region {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
CC       membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
CC       protein {ECO:0000255}. Note=ER membrane retention is mediated by
CC       the 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
CC       membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
CC       protein {ECO:0000255}. Note=ER membrane retention is mediated by
CC       the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted
CC       {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
CC       membrane; Peripheral membrane protein; Lumenal side
CC       {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived
CC       vesicles hosting the replication complex.
CC       {ECO:0000250|UniProtKB:Q9Q6P4}.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic
CC       reticulum membrane {ECO:0000250|UniProtKB:P14335}; Multi-pass
CC       membrane protein {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host
CC       endoplasmic reticulum membrane; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P17763}.
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
CC       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
CC       membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in
CC       RE-associated 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
CC       membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in
CC       RE-derived 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
CC       complex. NS5 protein is mainly localized in the nucleus rather
CC       than in ER vesicles. {ECO:0000250|UniProtKB:P17763}.
CC   -!- DOMAIN: The transmembrane domains of the small envelope protein M
CC       and envelope protein E contain an endoplasmic reticulum retention
CC       signal. {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, whereas
CC       cleavages in the cytoplasmic side are performed by serine protease
CC       NS3. Signal cleavage at the 2K-4B site requires a prior NS3
CC       protease-mediated cleavage at the 4A-2K site.
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.
CC       This cleavage is incomplete as up to 30% of viral particles still
CC       carry 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
CC       is glycosylated and this is required for efficient secretion of
CC       the 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
CC       localization. {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}.
DR   EMBL; AY632539; AAV34155.1; -; Genomic_RNA.
DR   RefSeq; YP_001040006.1; NC_009028.2.
DR   MEROPS; S07.001; -.
DR   GeneID; 5075856; -.
DR   KEGG; vg:5075856; -.
DR   OrthoDB; 136at10239; -.
DR   Proteomes; UP000149844; Genome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   CDD; 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   InterPro; IPR011492; DEAD_Flavivir.
DR   InterPro; IPR000069; Env_glycoprot_M_flavivir.
DR   InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
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; 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   3: Inferred from homology;
KW   Activation of host autophagy by virus; ATP-binding; Capsid protein;
KW   Clathrin-mediated endocytosis of virus by host;
KW   Cleavage on pair of basic residues; 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 cytoplasm; Host endoplasmic reticulum; Host membrane;
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 STAT1 by virus; Inhibition of host STAT2 by virus;
KW   Membrane; Metal-binding; Methyltransferase; mRNA capping;
KW   mRNA processing; Nucleotide-binding; Nucleotidyltransferase;
KW   Phosphoprotein; Protease; RNA-binding; RNA-directed RNA polymerase;
KW   S-adenosyl-L-methionine; Secreted; Serine protease;
KW   Suppressor of RNA silencing; Transcription; Transcription regulation;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Viral attachment to host cell; Viral envelope protein;
KW   Viral immunoevasion; Viral penetration into host cytoplasm;
KW   Viral RNA replication; Virion; Virus endocytosis by host;
KW   Virus entry into host cell; Zinc.
FT   CHAIN         1   3424       Genome polyprotein.
FT                                /FTId=PRO_0000441486.
FT   CHAIN         1    101       Capsid protein C.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441487.
FT   PROPEP      102    118       ER anchor for the capsid protein C,
FT                                removed in mature form by serine protease
FT                                NS3. {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441488.
FT   CHAIN       119    285       Protein prM.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441489.
FT   CHAIN       119    210       Peptide pr.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441490.
FT   CHAIN       211    285       Small envelope protein M.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441491.
FT   CHAIN       286    786       Envelope protein E.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441492.
FT   CHAIN       787   1139       Non-structural protein 1.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441493.
FT   CHAIN      1140   1366       Non-structural protein 2A.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441494.
FT   CHAIN      1367   1497       Serine protease subunit NS2B.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441495.
FT   CHAIN      1498   2115       Serine protease NS3.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441496.
FT   CHAIN      2116   2241       Non-structural protein 4A.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441497.
FT   PEPTIDE    2242   2264       Peptide 2k.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441498.
FT   CHAIN      2265   2519       Non-structural protein 4B.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441499.
FT   CHAIN      2520   3424       RNA-directed RNA polymerase NS5.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000441500.
FT   TOPO_DOM      2    101       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    102    122       Helical. {ECO:0000255}.
FT   TOPO_DOM    123    244       Extracellular. {ECO:0000255}.
FT   TRANSMEM    245    265       Helical. {ECO:0000255}.
FT   TOPO_DOM    266    270       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    271    285       Helical. {ECO:0000305}.
FT   TOPO_DOM    286    738       Extracellular. {ECO:0000255}.
FT   TRANSMEM    739    759       Helical. {ECO:0000255}.
FT   TOPO_DOM    760    765       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    766    786       Helical. {ECO:0000255}.
FT   TOPO_DOM    787   1170       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1171   1191       Helical. {ECO:0000255}.
FT   TOPO_DOM   1192   1213       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1214   1234       Helical. {ECO:0000255}.
FT   TOPO_DOM   1235   1276       Lumenal. {ECO:0000255}.
FT   TRANSMEM   1277   1297       Helical. {ECO:0000255}.
FT   TOPO_DOM   1298   1302       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1303   1323       Helical. {ECO:0000255}.
FT   TOPO_DOM   1324   1333       Lumenal. {ECO:0000255}.
FT   TRANSMEM   1334   1354       Helical. {ECO:0000255}.
FT   TOPO_DOM   1355   1367       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1368   1388       Helical. {ECO:0000255}.
FT   TOPO_DOM   1389   1391       Lumenal. {ECO:0000255}.
FT   TRANSMEM   1392   1412       Helical. {ECO:0000255}.
FT   TOPO_DOM   1413   1469       Cytoplasmic. {ECO:0000255}.
FT   INTRAMEM   1470   1490       Helical. {ECO:0000255}.
FT   TOPO_DOM   1491   2167       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2168   2188       Helical. {ECO:0000255}.
FT   TOPO_DOM   2189   2190       Lumenal. {ECO:0000255}.
FT   INTRAMEM   2191   2211       Helical. {ECO:0000255}.
FT   TOPO_DOM   2212   2213       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2214   2234       Helical. {ECO:0000255}.
FT   TOPO_DOM   2235   2249       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2250   2264       Helical; Note=Signal for NS4B.
FT                                {ECO:0000305}.
FT   TOPO_DOM   2265   2299       Lumenal. {ECO:0000255}.
FT   INTRAMEM   2300   2320       Helical. {ECO:0000255}.
FT   TOPO_DOM   2321   2342       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2343   2363       Helical. {ECO:0000255}.
FT   TOPO_DOM   2364   2371       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2372   2392       Helical. {ECO:0000255}.
FT   TOPO_DOM   2393   2439       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2440   2460       Helical. {ECO:0000255}.
FT   TOPO_DOM   2461   3424       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN     1498   1675       Peptidase S7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   DOMAIN     1678   1834       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1845   2009       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     2520   2784       mRNA cap 0-1 NS5-type MT.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   DOMAIN     3048   3200       RdRp catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00539}.
FT   NP_BIND    1691   1698       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION        2     15       Interaction with host EXOC1.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   REGION       35     70       Hydrophobic; homodimerization of capsid
FT                                protein C.
FT                                {ECO:0000250|UniProtKB:P29990}.
FT   REGION      383    396       Fusion peptide.
FT                                {ECO:0000250|UniProtKB:P14336}.
FT   REGION     1420   1459       Interacts with and activates NS3
FT                                protease. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00859}.
FT   REGION     1682   1685       Important for RNA-binding.
FT                                {ECO:0000250|UniProtKB:P14340}.
FT   REGION     2160   2164       Regulates the ATPase activity of NS3
FT                                helicase. {ECO:0000250|UniProtKB:Q9Q6P4}.
FT   MOTIF      1782   1785       DEAH box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COMPBIAS   2380   2383       Poly-Leu. {ECO:0000255}.
FT   ACT_SITE   1548   1548       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   ACT_SITE   1572   1572       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   ACT_SITE   1632   1632       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   ACT_SITE   2580   2580       For 2'-O-MTase activity.
FT                                {ECO:0000250|UniProtKB:Q6YMS4}.
FT   ACT_SITE   2665   2665       For 2'-O-MTase activity.
FT                                {ECO:0000250|UniProtKB:Q6YMS4}.
FT   ACT_SITE   2700   2700       For 2'-O-MTase activity.
FT                                {ECO:0000250|UniProtKB:Q6YMS4}.
FT   ACT_SITE   2736   2736       For 2'-O-MTase activity.
FT                                {ECO:0000250|UniProtKB:Q6YMS4}.
FT   METAL      2958   2958       Zinc 1. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      2962   2962       Zinc 1; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   METAL      2967   2967       Zinc 1. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      2970   2970       Zinc 1. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      3235   3235       Zinc 2; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   METAL      3251   3251       Zinc 2. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      3370   3370       Zinc 2. {ECO:0000250|UniProtKB:P14335}.
FT   BINDING    2575   2575       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2605   2605       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2606   2606       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2623   2623       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2624   2624       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2650   2650       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2651   2651       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2666   2666       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2738   2738       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE        100    101       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE        118    119       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE        210    211       Cleavage; by host furin.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE        285    286       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE        786    787       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       1139   1140       Cleavage; by host.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       1366   1367       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       1497   1498       Cleavage; by autolysis.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       1954   1954       Involved in NS3 ATPase and RTPase
FT                                activities.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   SITE       1957   1957       Involved in NS3 ATPase and RTPase
FT                                activities.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   SITE       2115   2116       Cleavage; by autolysis.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       2241   2242       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       2264   2265       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       2519   2520       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       2532   2532       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2535   2535       mRNA cap binding; via carbonyl oxygen.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE       2536   2536       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2538   2538       mRNA cap binding; via carbonyl oxygen.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE       2543   2543       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2547   2547       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2580   2580       Essential for 2'-O-methyltransferase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2665   2665       Essential for 2'-O-methyltransferase and
FT                                N-7 methyltransferase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE       2669   2669       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2700   2700       Essential for 2'-O-methyltransferase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2731   2731       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2733   2733       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2736   2736       Essential for 2'-O-methyltransferase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   MOD_RES    2575   2575       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   CARBOHYD    133    133       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   CARBOHYD    916    916       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000250|UniProtKB:Q9Q6P4}.
FT   CARBOHYD    993    993       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000250|UniProtKB:Q9Q6P4}.
FT   DISULFID    288    315       {ECO:0000250|UniProtKB:P06935}.
FT   DISULFID    345    406       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    345    401       {ECO:0000250|UniProtKB:P06935}.
FT   DISULFID    359    390       {ECO:0000250|UniProtKB:P06935}.
FT   DISULFID    377    406       {ECO:0000250|UniProtKB:P06935}.
FT   DISULFID    377    401       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    475    573       {ECO:0000250|UniProtKB:P06935}.
FT   DISULFID    590    621       {ECO:0000250|UniProtKB:P06935}.
FT   DISULFID    790    801       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    841    929       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    965   1009       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID   1067   1116       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID   1078   1100       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID   1078   1099       {ECO:0000250|UniProtKB:Q9Q6P4}.
FT   DISULFID   1099   1103       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID   1100   1103       {ECO:0000250|UniProtKB:Q9Q6P4}.
SQ   SEQUENCE   3424 AA;  379057 MW;  314D2282C5FF6CBA CRC64;
     MSKKPGKSAA KRTVNMLKRL ASVSPSRGRR TIRRMLDVRG APRLILALMA FFRFAAIKPT
     LGLKKRWRSV NKTVAVKHLT NFKKELTTML DSVNKRKEKK KSFSTALLWI TMITAVAGLK
     ISSHRDRPLL MVNKTDVSDA IPVPSVKGTN MCTIRALDVG YTCAYDTTYE CPHLEVTMDP
     EDIDCWCTLE SVYVNYGLCK QNHHVRRGRR AINIPHHGES HLENRATPWM DTTKTTKYLT
     KVENWVIRNP GYALVALATA WMLGSNTPQR VVFMIMMMLI APAYSLNCLG ISNRDFVEGL
     SGGTWVDIVL EGGSCVTVMA KDKPTLDIKL IRMEAKDLAT VRSYCYQATV TDSSTEARCP
     TMGEAHNSKS LDASYVCKSS YVDRGWGNGC GLFGKGSIQT CVKFSCPGKA TGKSIQRENL
     NYDVAVYVHG PISAAAHGNY TAQLTGKYAA KFSITPSAPT YTANLGEYGE ATMECEPRAA
     LDIDNYYVMS LNNKHWLVNR DWFHDLDLPW TGPATESWKN RESLIEFEEP HATRQTVVAL
     GNQEGALHTA LAGAIPVEVS STTLTLNSGH LKCRLKLDKL KIKGTTYAMC KGTFAFAQTP
     VDTGHGTIVA ELTYTGTDGP CKIPISMTAD LRDMTPIGRL VTVNPIIPSS AKSQKILVEL
     EPPFGSSFIL VGQENNQIKY QWHKTGSTIG NALKTTWKGA QRFAVLGDTA WDFGSVGGIF
     NSIGKTIHGV FGTAFRSLFG GMSWVTQALM GALLLWLGIS ARERTVSLIM LSVGGILLFL
     AVNVHADTGC AIDMARRELK CGSGIFIHND VETWRNNYKY HPLTPRGFAK VIQMSKDKGV
     CGIRSVGRLE HEMWEAIAPE LNAIFEDNGV DLSVVVKGQT GIYKRAPKRL TETKDEMSFG
     WKNWGKSFIF STETANSTFI VDGPESKECP TSDRAWNSLE LEDFGFGIIS TKIFLKVNEQ
     RGNSCDSAVI GTAVKGNEAV HSDLGFWIQS TKNESWQLER AVLGEVKSCT WPESHTLWGD
     GVEESDLIIP ITLAGPKSHH NMRPGYKTQT KGPWHEETPL VIEFAECPGT TVTQEESCGG
     RGPSIRTTTA SGRTIRNWCC KNCTLPPLRF MAGENCWYGV EVRPKRENEE TLIKSKVSAG
     NGQTIEPFQL GILMAFVFTQ EVLRRRWTAN LALPTSALLM ACFIFGGFTY LDLFRYFILV
     GAAFAEANSG GDVVHLAMIA AFNIQPVALV TTFFRKNWTN RENMILIIAA ACTQMACMEL
     KIELFHVMNS LSLAWMILKA LTTGTTSTLA MPFLAALSPP MNWLGLDVVR CLLIMAGVAA
     LISERRESLA KKKGALLISA ALALTGAFSP LVLQGALMFT QSLGKRGWPA SEVLTAVGMT
     FALAGSVARL DGGTMAIPLA TMAILAVAYV LSGKSTDMWL ERCADISWIN EAEITGTSPR
     LDVELDSNGD FKMINDPGVP MWMWTCRMGL MAMAAYNPVL IPVSMAGYWM TVKIHKRGGV
     MWDVPAPKQF GKTELKPGVY RVMTMGILGR YQSGVGVMWD GVFHTMWHVT QGAALRNGEG
     RLNPTWGSVR DDLISYGGKW KLSATWNGSE EVQMIAVEPG KAAKNYQTKP GVFKTPAGEI
     GAITLDFPKG TSGSPIINKA GEITGLYGNG IVLERGAYVS AITQGERQEE ETPEAFTPDM
     LKKRRLTILD LHPGAGKTRR VIPQIVRECV KARLRTVILV PTRVVAAEMA EALRGLPIRY
     QTSAVKAEHS GNEIVDAMRH ATLTQRLLTP AKVPNYNVFV MDEAHFTDPA SIAARGYIST
     KVELGEAAAI FMTATPPGTT DPFPDSNAPI IDQEAEIPDR AWNSGFEWIT EYTGKTVWFV
     PSVRMGNEIA MCLTKAGKKV IQLNRKSYDS EYQKCKGNDW DFVITTDISE MGANFGAHRV
     IDSRKCVKPV ILDGDDRVLM NGPAPITPAS AAQRRGRIGR DPTQSGDEYF YGGPTTTDDT
     GHAHWIEAKI LLDNIQLQNG LVAQLYGPER DKVFTTDGEY RLRSEQKKNF VEFLRTGDLP
     VWLSYKVAEA GYAYTDRRWC FDGPANNTIL EVRGDPEVWT RQGEKRILRP RWSDARVYCD
     NQALRSFKEF AAGKRSAGSV MEVMGRMPDY FWTKTLNAAD NLYVLATANK GGRAHQAALE
     ELPDTVETIL LMTMMCVASL GMFTLMVHRR GLGKTGLGTL VLATVTVLLW ISDVPAPKIA
     GVLLIAFLLM IVLIPEPEKQ RSQTDNHLAI FLVCVLLLIG AVSANEMGWL ETTKKDIGKL
     FRSSGDTQEQ STWQSWAPEV RAATAWAGYA GLTVFLTPLF RHLITTQYVS FSLTAITAQA
     SALFGLSAGY PFVGIDLAVG FLLLGCYGQY NLPTAVATGL LLLAHYGYMI PGWQAEAMRA
     AQKRTAAGVM KNAVVDGIVA TDIPEVDTAT PITEKKLGQI LLILLCGASL LVKFDTMVLV
     EAGVLTTSAM ATLIEGNANT VWNSTVAVGV CHLMRGAWLA GPSIGWTIVR NLENPKLKRG
     GGSAPTLGEI WKAQLNQLTR EEFMAYRRDG ILEVDRTQAR RARQSGITTG GHPVSRGTAK
     LRWMVERGFV RPIGKVVDLG CGRGGWSYYC ATLRHVQEVR GYTKGGPGHE EPVMMQSYGW
     NIVTMKSGVD VFYKPTESCD TLLCDIGESS SSVGVEEART LRVLDMVEPW LRAANSFCIK
     VLCPYTPKVI ERLERLQRAY GGGLVRVPLS RNSTHEMYWV SGASSNIINA VTVTSQILVQ
     RMNKGCRHGP RYEEDVCLGS GTRAVATQAS PSDHTKIKHR LERLRKEFSA TWHIDLEHPY
     RTWHYHGSYE VQPTGSANSM VNGVVRLLSK PWDAITSVVT MAMTDTTPFG QQRVFKEKVD
     TRAPDPAVGV AQALDITTGW LWTFLARSKK PRMCTREEFI AKVNSNAALG AVFDEQNQWS
     TAREAVEDPA FWNLVDEERK AHLAGRCETC IYNMMGKREK KLGEFGKAKG SRAIWYMWLG
     ARFLEFEALG FLNEDHWMSR ENSLGGVEGQ GLQKLGYILR DISHLEGGNM FADDTAGWDT
     RITRADLENE AKVMNMMDGE HKQLAKAIIE LTYRHKVVKV MRPARGGKTV MDIISREDQR
     GSGQVVTYAL NTFTNLAAQL VRCMEGEELL TESDVHGLSP KKKQAVRNWL IQNGRERLSR
     MAVSGDDCVV KPIDDRFASA LHFLNGMAKI RKDTQEWKPS VGWSNWQEVP FGSHHFNELL
     MKDGRTIVVP CRSQDELVGR ARVSPGSGWS LRETACLSKA YAQMWLLMYF HRRDLRLMAN
     AICSAVPVDW VPTGRTTWSI HGKGEWMTTE DMLQVWNRVW IEDNEHMEDK TPITSWTDIP
     YIGKREDQWC GSLIGTRQRA TWAENIYTPI MQIRNLIGDE KYVDCMVSQH RFETPSPVLF
     TGAI
//
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