GenomeNet

Database: UniProt
Entry: Q04538
LinkDB: Q04538
Original site: Q04538 
ID   POLG_POWVL              Reviewed;        3415 AA.
AC   Q04538;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   18-SEP-2019, entry version 156.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Peptide 2k;
DE   Contains:
DE     RecName: Full=Capsid protein C;
DE     AltName: Full=Core protein;
DE   Contains:
DE     RecName: Full=Protein prM;
DE   Contains:
DE     RecName: Full=Peptide pr;
DE   Contains:
DE     RecName: Full=Small envelope protein M;
DE     AltName: Full=Matrix protein;
DE   Contains:
DE     RecName: Full=Envelope protein E;
DE   Contains:
DE     RecName: Full=Non-structural protein 1;
DE              Short=NS1;
DE   Contains:
DE     RecName: Full=Non-structural protein 2A;
DE              Short=NS2A;
DE   Contains:
DE     RecName: Full=Serine protease subunit NS2B;
DE     AltName: Full=Flavivirin protease NS2B regulatory subunit;
DE     AltName: Full=Non-structural protein 2B;
DE   Contains:
DE     RecName: Full=Serine protease NS3;
DE              EC=3.4.21.91;
DE              EC=3.6.1.15;
DE              EC=3.6.4.13;
DE     AltName: Full=Flavivirin protease NS3 catalytic subunit;
DE     AltName: Full=Non-structural protein 3;
DE   Contains:
DE     RecName: Full=Non-structural protein 4A;
DE              Short=NS4A;
DE   Contains:
DE     RecName: Full=Non-structural protein 4B;
DE              Short=NS4B;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase NS5;
DE              EC=2.1.1.56 {ECO:0000255|PROSITE-ProRule:PRU00924};
DE              EC=2.1.1.57 {ECO:0000255|PROSITE-ProRule:PRU00924};
DE              EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE     AltName: Full=NS5;
OS   Tick-borne powassan virus (strain LB) (POWV) (Powassan virus).
OC   Viruses; Riboviria; Flaviviridae; Flavivirus.
OX   NCBI_TaxID=39008;
OH   NCBI_TaxID=34620; Dermacentor andersoni (Rocky mountain wood tick).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=35565; Ixodes cookei.
OH   NCBI_TaxID=6945; Ixodes scapularis (Black-legged tick) (Deer tick).
OH   NCBI_TaxID=34614; Ixodes spinipalpis.
OH   NCBI_TaxID=48086; Lepus americanus (Snowshoe hare).
OH   NCBI_TaxID=9995; Marmota monax (Woodchuck).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8097605; DOI=10.1006/viro.1993.1247;
RA   Mandl C.W., Holzmann H., Kunz C., Heinz F.X.;
RT   "Complete genomic sequence of Powassan virus: evaluation of genetic
RT   elements in tick-borne versus mosquito-borne flaviviruses.";
RL   Virology 194:173-184(1993).
CC   -!- FUNCTION: Capsid protein C: Plays a role in virus budding by
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       {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 immune response.
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- FUNCTION: Serine protease subunit NS2B: Required cofactor for the
CC       serine protease function of NS3. May have membrane-destabilizing
CC       activity and form viroporins (By similarity).
CC       {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
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: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. Non-structural protein 4B: Interacts
CC       with serine protease NS3. RNA-directed RNA polymerase NS5:
CC       Homodimer. Interacts with host STAT2; this interaction inhibits
CC       the phosphorylation of the latter, and, when all viral proteins
CC       are present (polyprotein), targets STAT2 for degradation.
CC       Interacts with serine protease NS3. Interacts with host SCRIB;
CC       this interaction targets NS5 to the cell membrane periphery and
CC       nucleus, thereby allowing efficient host nuclear STAT1 inhibition.
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, host perinuclear
CC       region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: Peptide pr: Secreted
CC       {ECO:0000250|UniProtKB:P17763}.
CC   -!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane
CC       {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum
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; L06436; AAA02739.1; -; Genomic_RNA.
DR   PIR; A46105; A46105.
DR   RefSeq; NP_620099.1; NC_003687.1.
DR   SMR; Q04538; -.
DR   PRIDE; Q04538; -.
DR   GeneID; 940442; -.
DR   KEGG; vg:940442; -.
DR   Proteomes; UP000006848; Genome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO: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; 1.10.8.970; -; 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; IPR038302; Env_glycoprot_M_sf_flavivir.
DR   InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
DR   InterPro; IPR001122; Flavi_capsidC.
DR   InterPro; IPR027287; Flavi_E_Ig-like.
DR   InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
DR   InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
DR   InterPro; IPR001157; Flavi_NS1.
DR   InterPro; IPR000752; Flavi_NS2A.
DR   InterPro; IPR000487; Flavi_NS2B.
DR   InterPro; IPR000404; Flavi_NS4A.
DR   InterPro; IPR001528; Flavi_NS4B.
DR   InterPro; IPR002535; Flavi_propep.
DR   InterPro; IPR038688; Flavi_propep_sf.
DR   InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR   InterPro; IPR001850; Flavivirus_NS3_S7.
DR   InterPro; IPR014412; Gen_Poly_FLV.
DR   InterPro; IPR011998; Glycoprot_cen/dimer.
DR   InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR   InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR   InterPro; IPR013756; GlyE_cen_dom_subdom2.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR000208; RNA-dir_pol_flavivirus.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR002877; 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; PF00948; Flavi_NS1; 1.
DR   Pfam; PF01005; Flavi_NS2A; 1.
DR   Pfam; PF01350; Flavi_NS4A; 1.
DR   Pfam; PF01349; Flavi_NS4B; 1.
DR   Pfam; PF00972; Flavi_NS5; 1.
DR   Pfam; PF01570; Flavi_propep; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF00949; Peptidase_S7; 1.
DR   PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; 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; Multifunctional enzyme; Nucleotide-binding;
KW   Nucleotidyltransferase; Phosphoprotein; Protease; RNA-binding;
KW   RNA-directed RNA polymerase; S-adenosyl-L-methionine; Secreted;
KW   Serine protease; Suppressor of RNA silencing; Transcription;
KW   Transcription regulation; Transferase; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell;
KW   Viral envelope protein; Viral immunoevasion;
KW   Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW   Virus endocytosis by host; Virus entry into host cell; Zinc.
FT   CHAIN         1   3415       Genome polyprotein.
FT                                /FTId=PRO_0000037724.
FT   CHAIN         1     94       Capsid protein C.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000405239.
FT   PROPEP       95    115       ER anchor for the capsid protein C,
FT                                removed in mature form by serine protease
FT                                NS3. {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000405140.
FT   CHAIN       116    278       Protein prM.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000405141.
FT   CHAIN       116    203       Peptide pr.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000037725.
FT   CHAIN       204    278       Small envelope protein M.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000037726.
FT   CHAIN       279    775       Envelope protein E.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000037727.
FT   CHAIN       776   1128       Non-structural protein 1.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000037728.
FT   CHAIN      1129   1358       Non-structural protein 2A.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT                                /FTId=PRO_0000037729.
FT   CHAIN      1359   1489       Serine protease subunit NS2B.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000037730.
FT   CHAIN      1490   2111       Serine protease NS3.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000037731.
FT   CHAIN      2112   2237       Non-structural protein 4A.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000037732.
FT   PEPTIDE    2238   2260       Peptide 2k.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000405142.
FT   CHAIN      2261   2512       Non-structural protein 4B.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000037733.
FT   CHAIN      2513   3415       RNA-directed RNA polymerase NS5.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000037734.
FT   TOPO_DOM      1     96       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     97    117       Helical. {ECO:0000255}.
FT   TOPO_DOM    118    243       Extracellular. {ECO:0000255}.
FT   TRANSMEM    244    260       Helical. {ECO:0000255}.
FT   TOPO_DOM    261    261       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    262    278       Helical. {ECO:0000255}.
FT   TOPO_DOM    279    726       Extracellular. {ECO:0000255}.
FT   TRANSMEM    727    747       Helical. {ECO:0000255}.
FT   TOPO_DOM    748    754       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    755    775       Helical. {ECO:0000255}.
FT   TOPO_DOM    776   1187       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1188   1208       Helical. {ECO:0000250|UniProtKB:P17763,
FT                                ECO:0000255}.
FT   TOPO_DOM   1209   1233       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P17763,
FT                                ECO:0000255}.
FT   TRANSMEM   1234   1253       Helical. {ECO:0000250|UniProtKB:P17763,
FT                                ECO:0000255}.
FT   TOPO_DOM   1254   1254       Lumenal. {ECO:0000250|UniProtKB:P17763,
FT                                ECO:0000255}.
FT   TRANSMEM   1255   1275       Helical. {ECO:0000250|UniProtKB:P17763,
FT                                ECO:0000255}.
FT   TOPO_DOM   1276   1292       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P17763,
FT                                ECO:0000255}.
FT   TRANSMEM   1293   1313       Helical. {ECO:0000250|UniProtKB:P17763,
FT                                ECO:0000255}.
FT   TOPO_DOM   1314   1327       Lumenal. {ECO:0000250|UniProtKB:P17763,
FT                                ECO:0000255}.
FT   TRANSMEM   1328   1348       Helical. {ECO:0000250|UniProtKB:P17763,
FT                                ECO:0000255}.
FT   TOPO_DOM   1349   1359       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P17763,
FT                                ECO:0000255}.
FT   TRANSMEM   1360   1378       Helical. {ECO:0000255}.
FT   TOPO_DOM   1379   1382       Lumenal. {ECO:0000255}.
FT   TRANSMEM   1383   1403       Helical. {ECO:0000255}.
FT   TOPO_DOM   1404   1452       Cytoplasmic. {ECO:0000255}.
FT   INTRAMEM   1453   1473       Helical. {ECO:0000255}.
FT   TOPO_DOM   1474   2163       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2164   2184       Helical. {ECO:0000255}.
FT   TOPO_DOM   2185   2190       Lumenal. {ECO:0000255}.
FT   INTRAMEM   2191   2210       Helical. {ECO:0000255}.
FT   TOPO_DOM   2211   2211       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2212   2232       Helical. {ECO:0000255}.
FT   TOPO_DOM   2233   2243       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2244   2264       Helical; Note=Signal for NS4B.
FT                                {ECO:0000255}.
FT   TOPO_DOM   2265   2300       Lumenal. {ECO:0000255}.
FT   INTRAMEM   2301   2321       Helical. {ECO:0000255}.
FT   TOPO_DOM   2322   2344       Lumenal. {ECO:0000255}.
FT   INTRAMEM   2345   2365       Helical. {ECO:0000255}.
FT   TOPO_DOM   2366   2369       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2370   2390       Helical. {ECO:0000255}.
FT   TOPO_DOM   2391   2433       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2434   2454       Helical. {ECO:0000255}.
FT   TOPO_DOM   2455   2479       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2480   2500       Helical. {ECO:0000255}.
FT   TOPO_DOM   2501   3415       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN     1490   1669       Peptidase S7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   DOMAIN     1675   1832       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1842   2001       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     2513   2777       mRNA cap 0-1 NS5-type MT.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   DOMAIN     3041   3190       RdRp catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00539}.
FT   NP_BIND    1688   1695       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION      376    389       Fusion peptide.
FT                                {ECO:0000250|UniProtKB:P14336}.
FT   REGION     1410   1449       Interacts with and activates NS3
FT                                protease. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00859}.
FT   REGION     2731   2735       Interaction with host SCRIB.
FT                                {ECO:0000250|UniProtKB:Q01299}.
FT   MOTIF      1780   1783       DEAH box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COMPBIAS   1746   1749       Poly-Ser.
FT   COMPBIAS   1971   1974       Poly-Asp.
FT   ACT_SITE   1543   1543       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   ACT_SITE   1567   1567       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   ACT_SITE   1627   1627       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   ACT_SITE   2573   2573       For 2'-O-MTase activity.
FT                                {ECO:0000250|UniProtKB:Q6YMS4}.
FT   ACT_SITE   2658   2658       For 2'-O-MTase activity.
FT                                {ECO:0000250|UniProtKB:Q6YMS4}.
FT   ACT_SITE   2695   2695       For 2'-O-MTase activity.
FT                                {ECO:0000250|UniProtKB:Q6YMS4}.
FT   ACT_SITE   2731   2731       For 2'-O-MTase activity.
FT                                {ECO:0000250|UniProtKB:Q6YMS4}.
FT   METAL      2951   2951       Zinc 1. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      2955   2955       Zinc 1; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   METAL      2960   2960       Zinc 1. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      2963   2963       Zinc 1. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      3225   3225       Zinc 2; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   METAL      3241   3241       Zinc 2. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      3360   3360       Zinc 2. {ECO:0000250|UniProtKB:P14335}.
FT   BINDING    2568   2568       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    2599   2599       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2616   2616       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2617   2617       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2643   2643       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2644   2644       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2659   2659       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2733   2733       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE         94     95       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE        114    115       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE        115    116       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE        203    204       Cleavage; by host furin.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE        278    279       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE        775    776       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE       1128   1129       Cleavage; by host.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       1358   1359       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P06935}.
FT   SITE       1489   1490       Cleavage; by autolysis.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE       1950   1950       Involved in NS3 ATPase and RTPase
FT                                activities.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   SITE       1953   1953       Involved in NS3 ATPase and RTPase
FT                                activities.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   SITE       2111   2112       Cleavage; by autolysis.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE       2237   2238       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE       2260   2261       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE       2512   2513       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE       2525   2525       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2528   2528       mRNA cap binding; via carbonyl oxygen.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE       2529   2529       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2531   2531       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       2540   2540       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2573   2573       Essential for 2'-O-methyltransferase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2658   2658       Essential for 2'-O-methyltransferase and
FT                                N-7 methyltransferase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE       2662   2662       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2695   2695       Essential for 2'-O-methyltransferase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2726   2726       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2728   2728       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2731   2731       Essential for 2'-O-methyltransferase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   MOD_RES    2568   2568       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   CARBOHYD    142    142       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    432    432       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000250|UniProtKB:P14336,
FT                                ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    860    860       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    983    983       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    999    999       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   DISULFID    281    308       {ECO:0000250|UniProtKB:P14336}.
FT   DISULFID    338    399       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    338    394       {ECO:0000250|UniProtKB:P14336}.
FT   DISULFID    352    383       {ECO:0000250|UniProtKB:P14336}.
FT   DISULFID    370    399       {ECO:0000250|UniProtKB:P14336}.
FT   DISULFID    370    394       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    464    568       {ECO:0000250|UniProtKB:P14336}.
FT   DISULFID    585    617       {ECO:0000250|UniProtKB:P14336}.
FT   DISULFID    779    790       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    830    920       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    955   1000       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID   1057   1106       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID   1068   1090       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID   1089   1093       {ECO:0000250|UniProtKB:P17763}.
SQ   SEQUENCE   3415 AA;  378570 MW;  E71092FE64049F46 CRC64;
     MMTTSKGKGG GPPRRKLKVT ANKSRPATSP MPKGFVLSRM LGILWHAVTG TARPPVLKMF
     WKTVPLRQAE AVLKKIKRVI GNLMQSLHMR GRRRSGVDWT WIFLTMALMT MAMATTIHRD
     REGYMVMRAS GRDAASQVRV QNGTCVILAT DMGEWCEDSI TYSCVTIDQE EEPVDVDCFC
     RGVDRVKLEY GRCGRQAGSR GKRSVVIPTH AQKDMVGRGH AWLKGDNIRD HVTRVEGWMW
     KNKLLTAAIV ALAWLMVDSW MARVTVILLA LSLGPVYATR CTHLENRDFV TGTQGTTRVS
     LVLELGGCVT ITAEGKPSID VWLEDIFQES PAETREYCLH AKLTNTKVEA RCPTTGPATL
     PEEHQANMVC KRDQSDRGWG NHCGFFGKGS IVACAKFECE EAKKAVGHVY DSTKITYVVK
     VEPHTGDYLA ANETNSNRKS AQFTVASEKV ILRLGDYGDV SLTCKVASGI DVAQTVVMSL
     DSSKDHLPSA WQVHRDWFED LALPWKHKDN QDWNSVEKLV EFGPPHAVKM DVFNLGDQTA
     VLLKSLAGVP LASVEGQKYH LKSGHVTCDV GLEKLKLKGT TYSMCDKAKF KWKRVPVDSG
     HDTVVMEVSY TGSDKPCRIP VRAVAHGVPA VNVAMLITPN PTIETNGGGF IEMQLPPGDN
     IIYVGDLSQQ WFQKGSTIGR MFEKTRRGLE RLSVVGEHAW DFGSVGGVLS SVGKAIHTVL
     GGAFNTLFGG VGFIPKMLLG VALVWLGLNA RNPTMSMTFL AVGALTLMMT MGVGADYGCA
     IDPERMEIRC GEGLVVWKEV SEWYDGYAYH PESPDTLAQA LREAFERGVC GVVPQNRLEM
     AMWRSTAPEL NLVLSEGEAN LTIVVDKTDP ADYRGGTPMV LKKTGKESKV SWKSWGKSIL
     WSVPDSPRRM MMGVDGVGEC PLYRRATGVF TVAEFGVGLR TKVFLDLRGE ASKECDTGVM
     GAAVKNGKAI HTDQSMWMSS FRNDTGTYIH ELILTDLRNC TWPASHTIDN DGVLDSHLFL
     PVTLAGPRSK YNRIPGYSEQ VRGPWDQTPL RVVRDHCPGT SVRIDSHCDK RGASVRSTTE
     SGKIIPEWCC RACELPPVTF RSGTDCWYAM EIRPVHSQGG LVRSMVVADN GALLSEGGVP
     GLVAVFVLME FLLRRRPGSV TSILWGGILM LGLLVTGLVR VEEIVRYVIA VGVTFHLELG
     PETMVLVMLQ AVFNMRTCYL MGFLVKRVIT TREVVTVYFL LLVLEMGIPE MNFGHLWEWA
     DALAMGLLII KASAMEDRRG LGFLLAGLMT QRHLVAVHHG LMVFLTVALA VVGRNIYNGQ
     KERKGLCFTV PLASLLGGSG SGLRMLALWE CLGGRGRRSL SEPLTVVGVM LAMASGLLRH
     SSQEALLALS AGSFLILMLI LGTRRLQLTA EWAGVVEWNP ELVNEGGEVS LKVRQDAMGN
     LHLTEVEREE RRLALWLVFG LLASAYHWSG ILVTMGAWTV YELFSSTRRT DLVFSGQLPD
     QGEKRSFDIK EGVYRIYAPG LFWGYRQIGV GYGTKGVLHT MWHVTRGAAL SVEGATSGPY
     WADVREDVVC YGGAWGLDKK WGGEVVQVHA FPPDSGHKIH QCQPGKLNLE GGRVLGAIPI
     DLPRGTSGSP IINAQGDVLG LYGNGLKSND VYISSIAQGN VEKSRPEMPL AVQGGKWTSK
     GSITVLDMHP GSGKTHRVLP ELIRECIDKR LRTVVLAPTR VVLKEMERAL QGKRVKFHSA
     AVDNASSSSG AIVDVMCHAT YVNRRLLPQG RQNWEVAIMD EAHWTDPHSI AARGHLYSLA
     KENRCALVLM TATPPGKSEA FPESKGAIVS EEKPIPEGEW RDGFDWITEF EGRTAWFVPS
     IAKGGAIART LRQKGKSVIC LNSKTFDKDY GRVHEEKPDF VVTTDISEMG ANLDVNRVID
     GRTNIKPEEI DGKVELIGTR RVTTASAAQR RGRVGRHEGR TDLYVYSGQC DDDDSSLVQW
     KEAQILLDNI TTVRGPVATF YGPEQGKMLE VAGHFRLTEE KRKHFRHLLT NCDFTPWLAW
     HVAANTACVT DRKWTWEGPD ENAIDGPGGE LVTFRSPNGA ERKLKPIWKD SRMFREGRDV
     ADFIQYASGR RSAVDILTGL GGVPDLLRLR CTAAWDVVYT LLNETPGSRA MKMAERDAPE
     AMLTLLEVAV LGIATLGVVW CFIVRTSVSR MVLGTLVLAV ALILLWLGGM DYGTMAGVAL
     IFYLLLTVLQ PEPGKQRSGE DNRLAFLLIG LGSVVGLVAA NELGYLEQTK TDISGLFRRE
     DQGGMVWDAW TNIDIQPARS WGTYVLIVSL FTPYMLHQLQ TKIQRLVNSS VAAGTQAMRD
     LGGGTPFFGV AGHVVALGVT SLVGATPTSL ALGVALAALH LAVVTSGLEA ELTQRAHRAF
     FSAMVKNPMV DGEIINPIPD GDPKPALYER KMSLFLAIGL CIAAVALNRT AAAMTEAGAV
     AVAALGQLLR PEEESWWTMP MACGMAGLVR GSLWGLLPVL HRIWLRTQGA RRGGAEGSTL
     GDIWKQRLNS CTKEEFFAYR RTGVMETNRD QARELLRRGE TNMGLAVSRG CAKLAWLEER
     GYATLKGEVV DLGCGRGGWS YYAASRPSVM AVRAYTIGGK GHEAPRLVTS LGWNLIKFRS
     GMDVFSMATT RADTILCDIG ESSPDPEKEG ARSRRVILLM EQWKARNPDA AAVFKVLAPY
     RPEVLEALHR FQLQWGGGLV RVPFSRNSTH EMYYSTAVTG NLVNSVNVLS RKLLARFGET
     RGPIQVPEID LGTGTRCVTL AEDKVKPRDV AERIGALREQ YSESWHEDKE HPYRTWQYWG
     SYRTPATGSA ASLINGVVKL LSWPWNARED VTRMAMTDTT AFGQQRVFKE KVDTKAQEPQ
     PGTRVIMRAV SDWLLEHLSR RAKVRMCTKD EFIAKVRSNA ALGAWSDEQN KWSSAKEAVE
     DPEFWKLVDE ERSRHLKGQC RHCVYNMMGK REKKLGEFGV AKGSRAIWYM WLGSRFLEFE
     VLGFLNEEHW ASREVSGAGV EGTSLNYLGW LLRELGMKDG GKLYADDTAG WDTRITNADL
     EDEEQILRYM EGEHHVLAKT ILEKAYHAKV VKVARPSPQG GCVMDVITRR DQRGSGQVVT
     YALNTITNMK VQLIRMMEGE GVIGPADSQD PRLKRVETWL KEHGVERLGR MLVSGDDCVV
     KPIDDRFGKA LYFLNDMAKV RKDVGEWEPS MGFTEWEEVP FCSHHFHELV MKDGRSLIVP
     CRDQDELVGR ARVSPGCGWS VRETACLSKA YGQMWLLNYF HRRDLRTLGF AICSAVPVSW
     VPMGRTTWSI HASGEWMTTE DMLRIWNKVW ILDNPHMEDK QTVDEWRDIP YLPKTQDLVC
     SSLVGRKERA EWAKNIWGSV EKVRKLIGPE DYRDYLSSMD RHDLHWELKL ESSII
//
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