GenomeNet

Database: UniProt
Entry: Q6J3P1
LinkDB: Q6J3P1
Original site: Q6J3P1 
ID   POLG_YEFVC              Reviewed;        3411 AA.
AC   Q6J3P1; Q6PX46;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 102.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Capsid protein C;
DE     AltName: Full=Core protein;
DE   Contains:
DE     RecName: Full=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 {ECO:0000250|UniProtKB:Q9Q6P4};
DE              EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9Q6P4};
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   Yellow fever virus (isolate Ivory Coast/1999) (YFV).
OC   Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
OC   Flaviviridae; Flavivirus; Yellow fever virus group.
OX   NCBI_TaxID=407136;
OH   NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OH   NCBI_TaxID=299629; Aedes luteocephalus (Mosquito).
OH   NCBI_TaxID=7161; Aedes simpsoni.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=314293; Simiiformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Gambia/2001, and Isolate Ivory Coast/1999;
RX   PubMed=16036176; DOI=10.1016/j.jcv.2004.12.001;
RA   Bae H.-G., Drosten C., Emmerich P., Colebunders R., Hantson P.,
RA   Pest S., Parent M., Schmitz H., Warnat M.-A., Niedrig M.;
RT   "Analysis of two imported cases of yellow fever infection from Ivory
RT   Coast and The Gambia to Germany and Belgium.";
RL   J. Clin. Virol. 33:274-280(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       {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 particule 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       Also plays a role in virus assembly (By similarity).
CC       {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE-
CC       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       {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 (By similarity). Besides its role in RNA genome
CC       replication, also prevents the establishment of cellular antiviral
CC       state by blocking the interferon-alpha/beta (IFN-alpha/beta)
CC       signaling pathway. IFN-I induces binding of NS5 to host IFN-
CC       activated transcription factor STAT2, preventing its
CC       transcriptional activity. Host TRIM23 is the E3 ligase that
CC       interacts with and polyubiquitinates NS5 to promote its binding to
CC       STAT2 and trigger IFN-I signaling inhibition.
CC       {ECO:0000250|UniProtKB:P03314}.
CC   -!- CATALYTIC ACTIVITY: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds
CC       in which each of the Xaa can be either Arg or Lys and Yaa can be
CC       either Ser or Ala.
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
CC   -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
CC       adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. {ECO:0000255|PROSITE-
CC       ProRule:PRU00924}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl
CC       5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-
CC       adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-
CC       triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].
CC       {ECO:0000255|PROSITE-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       non-structural protein 2A (via N-terminus). Interacts with NS4B.
CC       Interacts with unphosphorylated RNA-directed RNA polymerase NS5;
CC       this interaction stimulates RNA-directed RNA polymerase NS5
CC       guanylyltransferase activity. NS3 interacts with host PDCD6IP;
CC       this interaction contributes to virion release. Non-structural
CC       protein 4B: Interacts with serine protease NS3. RNA-directed RNA
CC       polymerase NS5: Homodimer. Interacts with host STAT2; this
CC       interaction prevents the establishment of cellular antiviral
CC       state. Interacts with host TRIM23; this interaction leads to NS5
CC       ubiquitination. {ECO:0000250|UniProtKB:P03314}.
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:P17763}; 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:P17763}; 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:P17763}.
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. The nascent capsid protein C contains a C-
CC       terminal hydrophobic domain that act as a signal sequence for
CC       translocation of prM into the lumen of the ER. Mature capsid
CC       protein C is cleaved at a site upstream of this hydrophobic domain
CC       by NS3. prM is cleaved in post-Golgi vesicles by a host furin,
CC       releasing the mature small envelope protein M, and peptide pr.
CC       Non-structural protein 2A-alpha, a C-terminally truncated form of
CC       non-structural protein 2A, results from partial cleavage by NS3.
CC       Specific enzymatic cleavages in vivo yield mature proteins peptide
CC       2K acts as a signal sequence and is removed from the N-terminus of
CC       NS4B by the host signal peptidase in the ER lumen. Signal cleavage
CC       at the 2K-4B site requires a prior NS3 protease-mediated cleavage
CC       at the 4A-2K site. {ECO:0000250|UniProtKB:P03314}.
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: Polyubiquitinated; ubiquitination is probably mediated by
CC       host TRIM23 and is prerequisite for NS5-STAT2 interaction. NS5 is
CC       not ISGylated or sumoylated. {ECO:0000250|UniProtKB:P03314}.
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; AY603338; AAT12476.1; -; Genomic_RNA.
DR   EMBL; AY572535; AAS78199.1; -; Genomic_RNA.
DR   ProteinModelPortal; Q6J3P1; -.
DR   SMR; Q6J3P1; -.
DR   OrthoDB; VOG090001DL; -.
DR   Proteomes; UP000007532; Genome.
DR   Proteomes; UP000141257; 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: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:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
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:InterPro.
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:0070008; F:serine-type exopeptidase 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:0006355; P:regulation of transcription, DNA-templated; 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:0006351; P:transcription, DNA-templated; 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   CDD; cd06174; MFS; 1.
DR   Gene3D; 2.60.40.350; -; 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; 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; 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; IPR000336; Flavivir/Alphavir_Ig-like.
DR   InterPro; IPR001850; Flavivirus_NS3_S7.
DR   InterPro; IPR014412; Gen_Poly_FLV.
DR   InterPro; IPR011998; Glycoprot_cen/dimer.
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; IPR020846; MFS_dom.
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; 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;
KW   GTP-binding; Helicase; Host cytoplasm; Host endoplasmic reticulum;
KW   Host membrane; 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 STAT2 by virus; 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;
KW   Suppressor of RNA silencing; Transcription; Transcription regulation;
KW   Transferase; Transmembrane; Transmembrane helix; Ubl conjugation;
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   3411       Genome polyprotein.
FT                                /FTId=PRO_0000405158.
FT   CHAIN         1    101       Capsid protein C.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000261500.
FT   PROPEP      102    121       ER anchor for the capsid protein C,
FT                                removed in mature form by serine protease
FT                                NS3. {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000261501.
FT   CHAIN       122    285       prM. {ECO:0000250|UniProtKB:P29990}.
FT                                /FTId=PRO_0000261502.
FT   CHAIN       122    210       Peptide pr.
FT                                {ECO:0000250|UniProtKB:P29990}.
FT                                /FTId=PRO_0000261503.
FT   CHAIN       211    285       Small envelope protein M.
FT                                {ECO:0000250|UniProtKB:P29990}.
FT                                /FTId=PRO_0000261504.
FT   CHAIN       286    778       Envelope protein E.
FT                                {ECO:0000250|UniProtKB:P29990}.
FT                                /FTId=PRO_0000261505.
FT   CHAIN       779   1130       Non-structural protein 1.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000261506.
FT   CHAIN      1131   1354       Non-structural protein 2A.
FT                                {ECO:0000250|UniProtKB:P29990}.
FT                                /FTId=PRO_0000261507.
FT   CHAIN      1131   1320       Non-structural protein 2A-alpha.
FT                                {ECO:0000250|UniProtKB:P29990}.
FT                                /FTId=PRO_0000261508.
FT   CHAIN      1355   1484       Serine protease subunit NS2B.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000261509.
FT   CHAIN      1485   2107       Serine protease NS3.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000261510.
FT   CHAIN      2108   2233       Non-structural protein 4A.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000261511.
FT   PEPTIDE    2234   2256       Peptide 2k.
FT                                /FTId=PRO_0000261512.
FT   CHAIN      2257   2506       Non-structural protein 4B.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000261513.
FT   CHAIN      2507   3411       RNA-directed RNA polymerase NS5.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT                                /FTId=PRO_0000261514.
FT   TOPO_DOM      1    104       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    105    125       Helical. {ECO:0000255}.
FT   TOPO_DOM    126    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    730       Extracellular. {ECO:0000255}.
FT   TRANSMEM    731    751       Helical. {ECO:0000255}.
FT   TOPO_DOM    752    757       Extracellular. {ECO:0000255}.
FT   TRANSMEM    758    778       Helical. {ECO:0000255}.
FT   TOPO_DOM    779   1132       Extracellular.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   TRANSMEM   1133   1153       Helical. {ECO:0000250|UniProtKB:P03314}.
FT   TOPO_DOM   1154   1201       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   TRANSMEM   1202   1222       Helical. {ECO:0000250|UniProtKB:P03314}.
FT   TOPO_DOM   1223   1287       Lumenal. {ECO:0000250|UniProtKB:P03314}.
FT   TRANSMEM   1288   1308       Helical. {ECO:0000250|UniProtKB:P03314}.
FT   TOPO_DOM   1309   1355       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   TRANSMEM   1356   1376       Helical. {ECO:0000250|UniProtKB:P03314}.
FT   TOPO_DOM   1377   1378       Lumenal. {ECO:0000250|UniProtKB:P03314}.
FT   TRANSMEM   1379   1399       Helical. {ECO:0000255}.
FT   TOPO_DOM   1400   1456       Cytoplasmic. {ECO:0000255}.
FT   INTRAMEM   1457   1477       Helical. {ECO:0000255}.
FT   TOPO_DOM   1478   2157       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2158   2178       Helical. {ECO:0000255}.
FT   TOPO_DOM   2179   2186       Lumenal. {ECO:0000255}.
FT   INTRAMEM   2187   2207       Helical. {ECO:0000255}.
FT   TOPO_DOM   2208   2209       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2210   2230       Helical. {ECO:0000255}.
FT   TOPO_DOM   2231   2241       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2242   2262       Helical; Note=Signal for NS4B.
FT                                {ECO:0000255}.
FT   TOPO_DOM   2263   2293       Lumenal. {ECO:0000255}.
FT   INTRAMEM   2294   2314       Helical. {ECO:0000255}.
FT   TOPO_DOM   2315   2360       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2361   2380       Helical. {ECO:0000255}.
FT   TOPO_DOM   2381   2421       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2422   2442       Helical. {ECO:0000255}.
FT   TOPO_DOM   2443   2445       Lumenal. {ECO:0000255}.
FT   TRANSMEM   2446   2466       Helical. {ECO:0000255}.
FT   TOPO_DOM   2467   3411       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN     1485   1665       Peptidase S7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   DOMAIN     1669   1825       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1820   1997       Helicase C-terminal.
FT   DOMAIN     2507   2771       mRNA cap 0-1 NS5-type MT.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   DOMAIN     3035   3187       RdRp catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00539}.
FT   NP_BIND    1682   1689       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION      383    396       Fusion peptide.
FT                                {ECO:0000250|UniProtKB:P14336}.
FT   REGION     1407   1446       Interacts with and activates NS3
FT                                protease. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00859}.
FT   REGION     1673   1676       Important for RNA-binding.
FT                                {ECO:0000250|UniProtKB:P14340}.
FT   MOTIF      1773   1776       DEAH box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF      2878   2911       Nuclear localization signal.
FT                                {ECO:0000250}.
FT   COMPBIAS   2656   2660       Poly-Ser.
FT   ACT_SITE   1537   1537       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   ACT_SITE   1561   1561       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   ACT_SITE   1622   1622       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00860}.
FT   ACT_SITE   2567   2567       For 2'-O-MTase activity.
FT                                {ECO:0000250|UniProtKB:Q6YMS4}.
FT   ACT_SITE   2652   2652       For 2'-O-MTase activity.
FT                                {ECO:0000250|UniProtKB:Q6YMS4}.
FT   ACT_SITE   2688   2688       For 2'-O-MTase activity.
FT                                {ECO:0000250|UniProtKB:Q6YMS4}.
FT   ACT_SITE   2724   2724       For 2'-O-MTase activity.
FT                                {ECO:0000250|UniProtKB:Q6YMS4}.
FT   METAL      2945   2945       Zinc 1. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      2949   2949       Zinc 1; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   METAL      2954   2954       Zinc 1. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      2957   2957       Zinc 1. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      3222   3222       Zinc 2; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   METAL      3238   3238       Zinc 2. {ECO:0000250|UniProtKB:P14335}.
FT   METAL      3357   3357       Zinc 2. {ECO:0000250|UniProtKB:P14335}.
FT   BINDING    2519   2519       mRNA cap. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2522   2522       mRNA cap; via carbonyl oxygen.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2523   2523       mRNA cap. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2525   2525       mRNA cap; via carbonyl oxygen.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2534   2534       mRNA cap. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2562   2562       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2592   2592       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2593   2593       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2610   2610       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2611   2611       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2637   2637       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   BINDING    2638   2638       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2656   2656       mRNA cap. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2719   2719       mRNA cap. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2721   2721       mRNA cap. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   BINDING    2726   2726       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE        101    102       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE        121    122       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE        210    211       Cleavage; by host furin.
FT                                {ECO:0000250|UniProtKB:P29990}.
FT   SITE        285    286       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P29990}.
FT   SITE        778    779       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE       1130   1131       Cleavage; by host.
FT                                {ECO:0000250|UniProtKB:P29990}.
FT   SITE       1354   1355       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P29990}.
FT   SITE       1484   1485       Cleavage; by autolysis.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE       1945   1945       Involved in NS3 ATPase and RTPase
FT                                activities.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   SITE       1948   1948       Involved in NS3 ATPase and RTPase
FT                                activities.
FT                                {ECO:0000250|UniProtKB:P14335}.
FT   SITE       2107   2108       Cleavage; by autolysis.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE       2233   2234       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P29990}.
FT   SITE       2256   2257       Cleavage; by host signal peptidase.
FT                                {ECO:0000250|UniProtKB:P29990}.
FT   SITE       2506   2507       Cleavage; by viral protease NS3.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   SITE       2530   2530       mRNA cap binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2567   2567       Essential for 2'-O-methyltransferase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2652   2652       Essential for 2'-O-methyltransferase and
FT                                N-7 methyltransferase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE       2653   2653       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00924}.
FT   SITE       2688   2688       Essential for 2'-O-methyltransferase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   SITE       2724   2724       Essential for 2'-O-methyltransferase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00924}.
FT   MOD_RES    2562   2562       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P03314}.
FT   CARBOHYD    134    134       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    150    150       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    908    908       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    986    986       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   DISULFID    288    315       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    345    406       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    345    401       {ECO:0000250}.
FT   DISULFID    359    390       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    377    406       {ECO:0000250}.
FT   DISULFID    377    401       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    467    568       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    585    615       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    782    793       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    833    921       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID    957   1002       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID   1058   1107       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID   1069   1091       {ECO:0000250|UniProtKB:P17763}.
FT   DISULFID   1090   1094       {ECO:0000250|UniProtKB:P17763}.
FT   VARIANT     107    107       A -> T (in strain: Isolate Gambia 2001).
FT   VARIANT     110    110       F -> L (in strain: Isolate Gambia 2001).
FT   VARIANT     116    116       L -> I (in strain: Isolate Gambia 2001).
FT   VARIANT     148    148       A -> T (in strain: Isolate Gambia 2001).
FT   VARIANT     712    712       L -> F (in strain: Isolate Gambia 2001).
FT   VARIANT     899    899       N -> S (in strain: Isolate Gambia 2001).
FT   VARIANT    1185   1185       T -> I (in strain: Isolate Gambia 2001).
FT   VARIANT    1297   1297       A -> T (in strain: Isolate Gambia 2001).
FT   VARIANT    1433   1433       S -> N (in strain: Isolate Gambia 2001).
FT   VARIANT    2056   2056       D -> E (in strain: Isolate Gambia 2001).
FT   VARIANT    2161   2161       A -> V (in strain: Isolate Gambia 2001).
FT   VARIANT    2373   2373       M -> T (in strain: Isolate Gambia 2001).
FT   VARIANT    2438   2438       A -> S (in strain: Isolate Gambia 2001).
FT   VARIANT    2644   2644       M -> V (in strain: Isolate Gambia 2001).
SQ   SEQUENCE   3411 AA;  378956 MW;  C121A19ABEA92218 CRC64;
     MSGRKAQGKT LGVNMVRRGV RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF FLFNILTGKK
     ITAHLKRLWK MLDPRQGLAV LRKVKRVVAS LMRGLSSRKR RSHDALAVQF LILGMLLMAG
     GVTLVRKNRW LLLNVTSEDL GKTFSVGAGN CTTNILEAKY WCPDSMEYNC PNLSPREEPD
     DIDCWCYGVE NVRVAYGKCD SAGRSRRSRR AIDLPTHENH GLKTRQEKWM TGRMGERQLQ
     KIERWLVRNP FFAVTALTIA YLVGSNMTQR VVIALLVLAV GPAYSAHCIG ITDRDFIEGV
     HGGTWVSATL EQDKCVTVMA PDKPSLDISL ETVAIDGPAE ARKVCYNAVL THVKINDKCP
     STGEAHLAEE NEGDNACKRT YSDRGWGNGC GLFGKGSIVA CAKFTCAKSM SLFEVDQTKI
     QYVIRAQLHV GAKQENWNTD IKTLKFDALS GSQEAEFTGY GKATLECQVQ TAVDFGNSYI
     AEMEKESWIV DRQWAQDLTL PWQSGSGGVW REMHHLVEFE PPHAATIRVL ALGNQEGSLK
     TALTGAMRVT KDTNDNNLYK LHGGHVSCRV KLSALTLKGT SYKMCTDKMS FVKNPTDTGH
     GTVVMQVKVP KGAPCKIPVI VADDLTAAIN KGILVTVNPI ASTNDDEVLI EVNPPFGDSY
     IIVGTGDSRL TYQWHKEGSS IGKLFTQTMK GAERLAVMGD AAWDFSSAGG FLTSVGKGIH
     TVFGSAFQGL FGGLSWITKV IMGAVLIWVG INTRNMTMSM SMILVGVIMM FLSLGVGADQ
     GCAINFGKRE LKCGDGIFIF RDSDDWLNKY SYYPEDPVKL ASIVKASFEE GKCGLNSVDS
     LEHEMWRSRA DEINAILEEN EVDISVVVQD PKNVYQRGTH PFSRIRDGLQ YGWKTWGKNL
     VFSPGRKNGS FIIDGKSRKE CPFSNRVWNS FQIEEFGTGV FTTRVYMDAV FEYTIDCDGS
     ILGAAVNGKK SAHGSPTFWM GSHEVNGTWM IHTLEALDYK ECEWPLTHTI GTSVEESEMF
     MPRSIGGPVS SHNHIPGYKV QTNGPWMQVP LEVRREACPG TSVIIDGNCD GRGKSTRSTT
     DSGKIIPEWC CRSCTMPPVS FHGSDGCWYP MEIRPRKTHE SHLVRSWVTA GEIHAVPFGL
     VSMMIAMEVV LRKRQGPKQM LVGGVVLLGA MLVGQVTLLD LLKLTVAVGL HFHEMNNGGD
     AMYMALIAAF SIRPGLLIGF GLRTLWSPRE RLVLTLGAAM VEIALGGMMG GLWKYLNAVS
     LCILTINAVA SRKASNTILP LMALLTPVTM AEVRLAAMLF CTVVIIGVLH QNSKDTSMQK
     TIPLVALTLT SYLGLTQPFL GLCAFLATRL FGRRSIPVNE ALAAAGLVGV LAGLAFQEME
     NFLGPIAVGG ILMMLVSVAG RVDGLELRKL GEVSWEEEAE ISGSSARYDV ALSEQGEFKL
     LSEEKVPWDQ VVMTSLALVG AAIHPFALLL VLAGWLFHVK GARRSGDVLW DIPTPKIIEE
     CEHLEDGIYG IFQSTFLGAS QRGVGVAQGG VFHTMWHVTR GAFLVRNGKK LIPSWASVKE
     DLVAYGGSWK LEGRWDGEEE VQLIAAVPGK NVVNVQTKPS LFKVRNGGEI GAVALDYPSG
     TSGSPIVNRN GEVIGLYGNG ILVGDNSFVS AISQTEVKEE GKEELQEIPT MLKKGMTTIL
     DFHPGAGKTR RFLPQILAEC ARRRLRTLVL APTRVVLSEM KEAFHGLDVK FHTQAFSAHG
     SGREVIDAMC HATLTYRMLE PTRIVNWEVI IMDEAHFLDP ASIAARGWAA HRARANESAT
     ILMTATPPGT SDEFPHSNGE IEDVQTDIPS EPWNTGHDWI LADKRPTAWF LPSIRAANVM
     AASLRKAGKS VVVLNRKTFE REYPTIKQKK PDFILATDIA EMGANLCVER VLDCRTAFKP
     VLVDEGRKVA IKGPLRISAS SAAQRRGRIG RNPNRDGDSY YYSEPTSEDN AHHVCWLEAS
     MLLDNMEVRG GMVAPLYGVE GTKTPVSPGE MRLRDDQRKV FRELVRNCDQ PVWLSWQVAK
     AGLKTNDRKW CFEGPDEHEI LNDSGETVKC RAPGGAKKPL RPRWCDERVS SDQSALADFI
     KFAEGRRGAA EVLVVLSELP DFLAKKGGEA MDTISVFLHS EEGSRAYRNA LSMMPEAMTI
     AMLFILAGLL TSGMVIFFMS PKGISRMSMA MGTMAGCGYL MFLGGVKPTH ISYIMLIFFV
     LMVVVIPEPG QQRSIQDNQV AYLIIGILTL VSVVAANELG MLEKTKEDLF GKKDLIPSSA
     SPWSWPDLDL KPGAAWTVYV GIVTMLSPML HHWIKVEYGN LSLSGIAQSA SVLSFMDKGI
     PFMKMNISVI ILLVSGWNSI TVMPLLCGIG CAMLHWSLIL PGIKAQQSKL AQRRVFHGVA
     KNPVVDGNPT VDIEEAPEMP ALYEKKLALY LLLALSLASV AMCRTPFSLA EGIVLASAAL
     GPLIEGNTSL LWNGPMAVSM TGVMRGNYYA FVGVMYNLWK MKTGRRGRAN GKTLGEVWKR
     ELNLLDKQQF ELYKRTDIVE VDRDTARRHL AEGKVDTGVA VSRGTAKLRW FHERGYVKLE
     GRVTDLGCGR GGWCYYAAAQ KEVSGVKGFT LGRDGHEKPM NVQSLGWNII TFKDKTDIHR
     LEPMKCDTLL CDIGESSSSS VTEGERTMRV LDTVEKWLAC GVDNFCVKVL APYMPDVLEK
     LELLQRRFGG TVIRNPLSRN STHEMYYVSG ARSNVTFTVN QTSRLLMRRM RRPTGKVTLE
     ADVILPIGTR SVETDKGPLD REAIEERVER IKSEYMTTWF YDNDNPYRTW HYCGSYVTKT
     SGSAASMVNG VIKILTYPWD RIEEVTRMAM TDTTPFGQQR VFKEKVDTRA KDPPAGTRKI
     MKVVNRWLFR HLAREKNPRL CTKEEFIAKV RSHAAIGAYL EEQEQWKTAN EAVQDPKFWE
     LVDEERKLHQ QGRCRTCVYN MMGKREKKLS EFGKAKGSRA IWYMWLGARY LEFEALGFLN
     EDHWASRENS GGGVEGIGLQ YLGYVIRDLA AMDGGGFYAD DTAGWDTRIT EADLDDEQEI
     LNYMSPHHKK LAQAVMEMTY KNKVVKVLRP APGGKAYMDV ISRRDQRGSG QVVTYALNTI
     TNLKVQLIRM AEAEMVIHHQ HVQDCDESAL ARLEAWLTEH GCDRLKRMAV SGDDCVVRPI
     DDRFGLALSH LNAMSKVRKD ISEWQPSKGW NDWENVPFCS HHFHELHLKD GRRIVVPCRE
     QDELIGRGRV SPGNGWMIKE TACLSKAYAN MWSLMYFHKR DMRLLSLAVS SAVPTSWVPQ
     GRTTWSIHGK GEWMTTEDML GVWNRVWITN NPHMQDKTVV KEWRDVPYLT KRQDKLCGSL
     IGMTNRATWA SHIHLVIHRI RTLIGQEKYT DYLTVMDRYS VDADLQPGEL I
//
DBGET integrated database retrieval system