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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   11-JUN-2014, entry version 85.
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;
DE              EC=3.6.4.13;
DE     AltName: Full=Flavivirin protease NS3 catalytic subunit;
DE     AltName: Full=Non-structural protein 3;
DE   Contains:
DE     RecName: Full=Non-structural protein 4A;
DE              Short=NS4A;
DE   Contains:
DE     RecName: Full=Peptide 2k;
DE   Contains:
DE     RecName: Full=Non-structural protein 4B;
DE              Short=NS4B;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase NS5;
DE              EC=2.1.1.56;
DE              EC=2.1.1.57;
DE              EC=2.7.7.48;
DE     AltName: Full=Non-structural protein 5;
OS   Yellow fever virus (isolate Ivory Coast/1999) (YFV).
OC   Viruses; ssRNA positive-strand viruses, no DNA stage; Flaviviridae;
OC   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 self-assembles to form an icosahedral
CC       capsid about 30 nm in diameter. The capsid encapsulates the
CC       genomic RNA (By similarity).
CC   -!- FUNCTION: prM acts as a chaperone for envelope protein E during
CC       intracellular virion assembly by masking and inactivating envelope
CC       protein E fusion peptide. prM is matured in the last step of
CC       virion assembly, presumably to avoid catastrophic activation of
CC       the viral fusion peptide induced by the acidic pH of the trans-
CC       Golgi network. After cleavage by host furin, the pr peptide is
CC       released in the extracellular medium and small envelope protein M
CC       and envelope protein E homodimers are dissociated (By similarity).
CC   -!- FUNCTION: Envelope protein E binding to host cell surface receptor
CC       is followed by virus internalization through clathrin-mediated
CC       endocytosis. Envelope protein E is subsequently involved in
CC       membrane fusion between virion and host late endosomes.
CC       Synthesized as a homodimer with prM which acts as a chaperone for
CC       envelope protein E. After cleavage of prM, envelope protein E
CC       dissociate from small envelope protein M and homodimerizes (By
CC       similarity).
CC   -!- FUNCTION: Non-structural protein 1 is involved in virus
CC       replication and regulation of the innate immune response (By
CC       similarity).
CC   -!- FUNCTION: Non-structural protein 2A may be involved viral RNA
CC       replication and capsid assembly (Potential).
CC   -!- FUNCTION: Non-structural protein 2B is a required cofactor for the
CC       serine protease function of NS3 (By similarity).
CC   -!- FUNCTION: Serine protease NS3 displays three enzymatic activities:
CC       serine protease, NTPase and RNA helicase. NS3 serine protease, in
CC       association with NS2B, performs its autocleavage and cleaves the
CC       polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B,
CC       NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds
CC       RNA and unwinds dsRNA in the 3' to 5' direction (By similarity).
CC   -!- FUNCTION: Non-structural protein 4A induces host endoplasmic
CC       reticulum membrane rearrangements leading to the formation of
CC       virus-induced membranous vesicles hosting the dsRNA and
CC       polymerase, functioning as a replication complex. NS4A might also
CC       regulate the ATPase activity of the NS3 helicase (By similarity).
CC   -!- FUNCTION: Peptide 2k functions as a signal peptide for NS4B and is
CC       required for the interferon antagonism activity of the latter (By
CC       similarity).
CC   -!- FUNCTION: Non-structural protein 4B inhibits interferon (IFN)-
CC       induced host STAT1 phosphorylation and nuclear translocation,
CC       thereby preventing the establishment of cellular antiviral state
CC       by blocking the IFN-alpha/beta pathway (By similarity).
CC   -!- FUNCTION: RNA-directed RNA polymerase NS5 replicates the viral (+)
CC       and (-) genome, and performs the capping of genomes in the
CC       cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose
CC       2'-O positions. Besides its role in genome replication, also
CC       prevents the establishment of cellular antiviral state by blocking
CC       the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (By
CC       similarity).
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).
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.
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   -!- SUBUNIT: Capsid protein C forms homodimers. prM and envelope
CC       protein E form heterodimers in the endoplasmic reticulum and
CC       Golgi. In immature particles, there are 60 icosaedrally organized
CC       trimeric spikes on the surface. Each spike consists of three
CC       heterodimers of envelope protein M precursor (prM) and envelope
CC       protein E. NS1 forms homodimers as well as homohexamers when
CC       secreted. NS1 may interact with NS4A. NS3 and NS2B form a
CC       heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly
CC       stimulates the latter, acting as a cofactor. In the absence of the
CC       NS2B, NS3 protease is unfolded and inactive. NS3 interacts with
CC       unphosphorylated NS5; this interaction stimulates NS5
CC       guanylyltransferase activity (By similarity).
CC   -!- SUBCELLULAR LOCATION: Capsid protein C: Virion (Potential).
CC   -!- SUBCELLULAR LOCATION: Peptide pr: Secreted (By similarity).
CC   -!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane;
CC       Multi-pass membrane protein (By similarity). Host endoplasmic
CC       reticulum membrane; Multi-pass membrane protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane; Multi-
CC       pass membrane protein (By similarity). Host endoplasmic reticulum
CC       membrane; Multi-pass membrane protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted. Host
CC       endoplasmic reticulum membrane; Peripheral membrane protein;
CC       Lumenal side (By similarity).
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 2A-alpha: Host
CC       endoplasmic reticulum membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic
CC       reticulum membrane; Multi-pass membrane protein (Potential).
CC   -!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host
CC       endoplasmic reticulum membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity).
CC   -!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic
CC       reticulum membrane; Peripheral membrane protein; Cytoplasmic side
CC       (By similarity). Note=Remains non-covalently associated to NS3
CC       protease (By similarity).
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic
CC       reticulum membrane; Multi-pass membrane protein (By similarity).
CC       Note=Located in RE-associated vesicles hosting the replication
CC       complex.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic
CC       reticulum membrane; Multi-pass membrane protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase NS5: Host
CC       endoplasmic reticulum membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Host nucleus (By similarity).
CC       Note=Located in RE-associated vesicles hosting the replication
CC       complex.
CC   -!- DOMAIN: Transmembrane domains of the small envelope protein M and
CC       envelope protein E contains an endoplasmic reticulum retention
CC       signals (By similarity).
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC       The nascent protein C contains a C-terminal hydrophobic domain
CC       that act as a signal sequence for translocation of prM into the
CC       lumen of the ER. Mature protein C is cleaved at a site upstream of
CC       this hydrophobic domain by NS3. prM is cleaved in post-Golgi
CC       vesicles by a host furin, releasing the mature small envelope
CC       protein M, and peptide pr. Non-structural protein 2A-alpha, a C-
CC       terminally truncated form of non-structural protein 2A, results
CC       from partial cleavage by NS3. Specific enzymatic cleavages in vivo
CC       yield mature proteins Peptide 2K acts as a signal sequence and is
CC       removed from the N-terminus of NS4B by the host signal peptidase
CC       in the ER lumen. Signal cleavage at the 2K-4B site requires a
CC       prior NS3 protease-mediated cleavage at the 4A-2K site (By
CC       similarity).
CC   -!- PTM: RNA-directed RNA polymerase NS5 is phosphorylated on serines
CC       residues. This phosphorylation may trigger NS5 nuclear
CC       localization.
CC   -!- PTM: Envelope protein E and non-structural protein 1 are N-
CC       glycosylated (By similarity).
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.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 mRNA cap 0-1 NS5-type MT domain.
CC   -!- SIMILARITY: Contains 1 peptidase S7 domain.
CC   -!- SIMILARITY: Contains 1 RdRp catalytic domain.
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DR   EMBL; AY603338; AAT12476.1; -; Genomic_RNA.
DR   EMBL; AY572535; AAS78199.1; -; Genomic_RNA.
DR   ProteinModelPortal; Q6J3P1; -.
DR   SMR; Q6J3P1; 572-683, 1490-1667, 1671-2107, 2512-2772, 2780-3399.
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:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed 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-mediated 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   Gene3D; 2.60.40.350; -; 1.
DR   Gene3D; 2.60.98.10; -; 2.
DR   Gene3D; 3.30.387.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
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; 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; IPR027287; Flavovir_Ig-like.
DR   InterPro; IPR014412; Gen_Poly_FLV.
DR   InterPro; IPR011998; Glycoprot_cen/dimer.
DR   InterPro; IPR013754; GlyE_dim.
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; 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-like.
DR   InterPro; IPR009003; Trypsin-like_Pept_dom.
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; PF00271; Helicase_C; 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; 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 endoplasmic reticulum; Host membrane; Host nucleus;
KW   Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus; Membrane;
KW   Metal-binding; Methyltransferase; mRNA capping; mRNA processing;
KW   Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW   Phosphoprotein; Protease; RNA-binding; RNA-directed RNA polymerase;
KW   S-adenosyl-L-methionine; Secreted; Serine protease; Transcription;
KW   Transcription regulation; Transferase; Transmembrane;
KW   Transmembrane helix; 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.
FT   CHAIN         1   3411       Genome polyprotein.
FT                                /FTId=PRO_0000405158.
FT   CHAIN         1    101       Capsid protein C (By similarity).
FT                                /FTId=PRO_0000261500.
FT   PROPEP      102    121       ER anchor for the protein C, removed in
FT                                mature form by serine protease NS3.
FT                                /FTId=PRO_0000261501.
FT   CHAIN       122    285       prM (By similarity).
FT                                /FTId=PRO_0000261502.
FT   CHAIN       122    210       Peptide pr (By similarity).
FT                                /FTId=PRO_0000261503.
FT   CHAIN       211    285       Small envelope protein M (By similarity).
FT                                /FTId=PRO_0000261504.
FT   CHAIN       286    778       Envelope protein E (By similarity).
FT                                /FTId=PRO_0000261505.
FT   CHAIN       779   1130       Non-structural protein 1 (By similarity).
FT                                /FTId=PRO_0000261506.
FT   CHAIN      1131   1354       Non-structural protein 2A (By
FT                                similarity).
FT                                /FTId=PRO_0000261507.
FT   CHAIN      1131   1320       Non-structural protein 2A-alpha (By
FT                                similarity).
FT                                /FTId=PRO_0000261508.
FT   CHAIN      1355   1484       Serine protease subunit NS2B (By
FT                                similarity).
FT                                /FTId=PRO_0000261509.
FT   CHAIN      1485   2107       Serine protease NS3 (By similarity).
FT                                /FTId=PRO_0000261510.
FT   CHAIN      2108   2233       Non-structural protein 4A (By
FT                                similarity).
FT                                /FTId=PRO_0000261511.
FT   PEPTIDE    2234   2256       Peptide 2k.
FT                                /FTId=PRO_0000261512.
FT   CHAIN      2257   2506       Non-structural protein 4B (By
FT                                similarity).
FT                                /FTId=PRO_0000261513.
FT   CHAIN      2507   3411       RNA-directed RNA polymerase NS5 (By
FT                                similarity).
FT                                /FTId=PRO_0000261514.
FT   TOPO_DOM      1    104       Cytoplasmic (Potential).
FT   TRANSMEM    105    125       Helical; (Potential).
FT   TOPO_DOM    126    244       Extracellular (Potential).
FT   TRANSMEM    245    265       Helical; (Potential).
FT   TOPO_DOM    266    270       Cytoplasmic (Potential).
FT   TRANSMEM    271    285       Helical; (Potential).
FT   TOPO_DOM    286    730       Extracellular (Potential).
FT   INTRAMEM    731    751       Helical; (Potential).
FT   TOPO_DOM    752    757       Extracellular (Potential).
FT   INTRAMEM    758    778       Helical; (Potential).
FT   TOPO_DOM    779   1130       Extracellular (Potential).
FT   TRANSMEM   1131   1151       Helical; (Potential).
FT   TOPO_DOM   1152   1160       Cytoplasmic (Potential).
FT   TRANSMEM   1161   1181       Helical; (Potential).
FT   TOPO_DOM   1182   1201       Lumenal (Potential).
FT   TRANSMEM   1202   1222       Helical; (Potential).
FT   TOPO_DOM   1223   1231       Cytoplasmic (Potential).
FT   TRANSMEM   1232   1252       Helical; (Potential).
FT   TOPO_DOM   1253   1262       Lumenal (Potential).
FT   TRANSMEM   1263   1285       Helical; (Potential).
FT   TOPO_DOM   1286   1355       Cytoplasmic (Potential).
FT   TRANSMEM   1356   1376       Helical; (Potential).
FT   TOPO_DOM   1377   1378       Lumenal (Potential).
FT   TRANSMEM   1379   1399       Helical; (Potential).
FT   TOPO_DOM   1400   1456       Cytoplasmic (Potential).
FT   INTRAMEM   1457   1477       Helical; (Potential).
FT   TOPO_DOM   1478   2157       Cytoplasmic (Potential).
FT   TRANSMEM   2158   2178       Helical; (Potential).
FT   TOPO_DOM   2179   2186       Lumenal (Potential).
FT   INTRAMEM   2187   2207       Helical; (Potential).
FT   TOPO_DOM   2208   2209       Lumenal (Potential).
FT   TRANSMEM   2210   2230       Helical; (Potential).
FT   TOPO_DOM   2231   2241       Cytoplasmic (Potential).
FT   TRANSMEM   2242   2262       Helical; Note=Signal for NS4B;
FT                                (Potential).
FT   TOPO_DOM   2263   2293       Lumenal (Potential).
FT   INTRAMEM   2294   2314       Helical; (Potential).
FT   TOPO_DOM   2315   2338       Lumenal (Potential).
FT   INTRAMEM   2339   2359       Helical; (Potential).
FT   TOPO_DOM   2360   2360       Lumenal (Potential).
FT   TRANSMEM   2361   2380       Helical; (Potential).
FT   TOPO_DOM   2381   2421       Cytoplasmic (Potential).
FT   TRANSMEM   2422   2442       Helical; (Potential).
FT   TOPO_DOM   2443   2445       Lumenal (Potential).
FT   TRANSMEM   2446   2466       Helical; (Potential).
FT   TOPO_DOM   2467   3411       Cytoplasmic (Potential).
FT   DOMAIN     1485   1665       Peptidase S7.
FT   DOMAIN     1669   1825       Helicase ATP-binding.
FT   DOMAIN     1820   1997       Helicase C-terminal.
FT   DOMAIN     2507   2771       mRNA cap 0-1 NS5-type MT.
FT   DOMAIN     3035   3187       RdRp catalytic.
FT   NP_BIND    1682   1689       ATP (Potential).
FT   REGION       30     74       Hydrophobic; homodimerization of capsid
FT                                protein C (By similarity).
FT   REGION      383    396       Involved in fusion (By similarity).
FT   REGION     1407   1446       Interacts with and activates NS3 protease
FT                                (By similarity).
FT   MOTIF      1773   1776       DEAH box.
FT   MOTIF      2878   2911       Nuclear localization signal (By
FT                                similarity).
FT   COMPBIAS   2656   2660       Poly-Ser.
FT   ACT_SITE   1537   1537       Charge relay system; for serine protease
FT                                NS3 activity (By similarity).
FT   ACT_SITE   1561   1561       Charge relay system; for serine protease
FT                                NS3 activity (By similarity).
FT   ACT_SITE   1622   1622       Charge relay system; for serine protease
FT                                NS3 activity (By similarity).
FT   BINDING    2519   2519       mRNA cap (By similarity).
FT   BINDING    2522   2522       mRNA cap; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING    2523   2523       mRNA cap (By similarity).
FT   BINDING    2525   2525       mRNA cap; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING    2534   2534       mRNA cap (By similarity).
FT   BINDING    2562   2562       S-adenosyl-L-methionine (By similarity).
FT   BINDING    2592   2592       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING    2593   2593       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING    2610   2610       S-adenosyl-L-methionine (By similarity).
FT   BINDING    2611   2611       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING    2637   2637       S-adenosyl-L-methionine (By similarity).
FT   BINDING    2638   2638       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING    2656   2656       mRNA cap (By similarity).
FT   BINDING    2719   2719       mRNA cap (By similarity).
FT   BINDING    2721   2721       mRNA cap (By similarity).
FT   BINDING    2726   2726       S-adenosyl-L-methionine (By similarity).
FT   SITE        101    102       Cleavage; by viral protease NS3
FT                                (Potential).
FT   SITE        121    122       Cleavage; by host signal peptidase (By
FT                                similarity).
FT   SITE        210    211       Cleavage; by host furin (Potential).
FT   SITE        285    286       Cleavage; by host signal peptidase
FT                                (Potential).
FT   SITE        778    779       Cleavage; by host signal peptidase
FT                                (Potential).
FT   SITE       1130   1131       Cleavage; by host (Potential).
FT   SITE       1354   1355       Cleavage; by viral protease NS3
FT                                (Potential).
FT   SITE       1484   1485       Cleavage; by autolysis (Potential).
FT   SITE       2107   2108       Cleavage; by autolysis (Potential).
FT   SITE       2233   2234       Cleavage; by viral protease NS3
FT                                (Potential).
FT   SITE       2256   2257       Cleavage; by host signal peptidase
FT                                (Potential).
FT   SITE       2506   2507       Cleavage; by viral protease NS3
FT                                (Potential).
FT   SITE       2530   2530       mRNA cap binding (By similarity).
FT   SITE       2567   2567       Essential for 2'-O-methyltransferase
FT                                activity (By similarity).
FT   SITE       2652   2652       Essential for 2'-O-methyltransferase and
FT                                N-7 methyltransferase activity (By
FT                                similarity).
FT   SITE       2653   2653       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   SITE       2688   2688       Essential for 2'-O-methyltransferase
FT                                activity (By similarity).
FT   SITE       2724   2724       Essential for 2'-O-methyltransferase
FT                                activity (By similarity).
FT   CARBOHYD    134    134       N-linked (GlcNAc...); by host
FT                                (Potential).
FT   CARBOHYD    150    150       N-linked (GlcNAc...); by host
FT                                (Potential).
FT   CARBOHYD    908    908       N-linked (GlcNAc...); by host
FT                                (Potential).
FT   CARBOHYD    986    986       N-linked (GlcNAc...); by host
FT                                (Potential).
FT   DISULFID    288    315       By similarity.
FT   DISULFID    345    401       By similarity.
FT   DISULFID    359    390       By similarity.
FT   DISULFID    377    406       By similarity.
FT   DISULFID    467    568       By similarity.
FT   DISULFID    585    615       By similarity.
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
//
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