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 06-JUL-2016, entry version 94. 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 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 self-assembles to form an icosahedral CC capsid about 30 nm in diameter. The capsid encapsulates the CC genomic RNA. {ECO:0000250}. 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. {ECO:0000250}. 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. CC {ECO:0000250}. CC -!- FUNCTION: Non-structural protein 1 is involved in virus CC replication and regulation of the innate immune response. CC {ECO:0000250}. CC -!- FUNCTION: Non-structural protein 2A may be involved viral RNA CC replication and capsid assembly. {ECO:0000305}. CC -!- FUNCTION: Non-structural protein 2B is a required cofactor for the CC serine protease function of NS3. {ECO:0000255|PROSITE- CC ProRule:PRU00859}. 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 {ECO:0000255|PROSITE-ProRule:PRU00860}. 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. {ECO:0000250}. CC -!- FUNCTION: Peptide 2k functions as a signal peptide for NS4B and is CC required for the interferon antagonism activity of the latter. CC {ECO:0000250}. 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. {ECO:0000250}. 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). {ECO:0000255|PROSITE-ProRule:PRU00539}. 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 -!- 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. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Capsid protein C: Virion {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Peptide pr: Secreted {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host CC endoplasmic reticulum membrane {ECO:0000255|PROSITE- CC ProRule:PRU00860}; Multi-pass membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host CC endoplasmic reticulum membrane {ECO:0000255|PROSITE- CC ProRule:PRU00860}; Multi-pass membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted. Host CC endoplasmic reticulum membrane {ECO:0000255|PROSITE- CC ProRule:PRU00860}; Peripheral membrane protein CC {ECO:0000255|PROSITE-ProRule:PRU00860}; Lumenal side CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Non-structural protein 2A-alpha: Host CC endoplasmic reticulum membrane {ECO:0000255|PROSITE- CC ProRule:PRU00860}; Multi-pass membrane protein {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic CC reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host CC endoplasmic reticulum membrane {ECO:0000255|PROSITE- CC ProRule:PRU00860}; Peripheral membrane protein CC {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side CC {ECO:0000255|PROSITE-ProRule:PRU00860}. CC -!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic CC reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; CC Peripheral membrane protein {ECO:0000255|PROSITE- CC ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE- CC ProRule:PRU00860}. Note=Remains non-covalently associated to NS3 CC protease. {ECO:0000255|PROSITE-ProRule:PRU00860}. CC -!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic CC reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Multi- CC pass membrane protein {ECO:0000250}. Note=Located in RE-associated CC vesicles hosting the replication complex. CC -!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic CC reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase NS5: Host CC endoplasmic reticulum membrane {ECO:0000255|PROSITE- CC ProRule:PRU00860}; Peripheral membrane protein CC {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side CC {ECO:0000255|PROSITE-ProRule:PRU00860}. Host nucleus CC {ECO:0000250}. Note=Located in RE-associated vesicles hosting the CC replication complex. CC -!- DOMAIN: Transmembrane domains of the small envelope protein M and CC envelope protein E contains an endoplasmic reticulum retention CC signals. {ECO:0000250}. 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. CC {ECO:0000250}. 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. {ECO:0000250}. CC -!- SIMILARITY: In the N-terminal section; belongs to the class I-like CC SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type CC methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00541}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 mRNA cap 0-1 NS5-type MT domain. CC {ECO:0000255|PROSITE-ProRule:PRU00924}. CC -!- SIMILARITY: Contains 1 peptidase S7 domain. {ECO:0000255|PROSITE- CC ProRule:PRU00860}. CC -!- SIMILARITY: Contains 1 RdRp catalytic domain. CC {ECO:0000255|PROSITE-ProRule:PRU00539}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY603338; AAT12476.1; -; Genomic_RNA. DR EMBL; AY572535; AAS78199.1; -; Genomic_RNA. DR ProteinModelPortal; Q6J3P1; -. DR SMR; Q6J3P1; 572-683, 1504-1653, 1671-2107, 2512-2772, 2780-3399. DR Proteomes; UP000007532; 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: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; 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; 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. {ECO:0000250}. 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. {ECO:0000250}. FT /FTId=PRO_0000261502. FT CHAIN 122 210 Peptide pr. {ECO:0000250}. FT /FTId=PRO_0000261503. FT CHAIN 211 285 Small envelope protein M. {ECO:0000250}. FT /FTId=PRO_0000261504. FT CHAIN 286 778 Envelope protein E. {ECO:0000250}. FT /FTId=PRO_0000261505. FT CHAIN 779 1130 Non-structural protein 1. {ECO:0000250}. FT /FTId=PRO_0000261506. FT CHAIN 1131 1354 Non-structural protein 2A. {ECO:0000250}. FT /FTId=PRO_0000261507. FT CHAIN 1131 1320 Non-structural protein 2A-alpha. FT {ECO:0000250}. FT /FTId=PRO_0000261508. FT CHAIN 1355 1484 Serine protease subunit NS2B. FT {ECO:0000250}. FT /FTId=PRO_0000261509. FT CHAIN 1485 2107 Serine protease NS3. {ECO:0000250}. FT /FTId=PRO_0000261510. FT CHAIN 2108 2233 Non-structural protein 4A. {ECO:0000250}. FT /FTId=PRO_0000261511. FT PEPTIDE 2234 2256 Peptide 2k. FT /FTId=PRO_0000261512. FT CHAIN 2257 2506 Non-structural protein 4B. {ECO:0000250}. FT /FTId=PRO_0000261513. FT CHAIN 2507 3411 RNA-directed RNA polymerase NS5. FT {ECO:0000250}. 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:0000255}. FT TOPO_DOM 286 730 Extracellular. {ECO:0000255}. FT INTRAMEM 731 751 Helical. {ECO:0000255}. FT TOPO_DOM 752 757 Extracellular. {ECO:0000255}. FT INTRAMEM 758 778 Helical. {ECO:0000255}. FT TOPO_DOM 779 1130 Extracellular. {ECO:0000255}. FT TRANSMEM 1131 1151 Helical. {ECO:0000255}. FT TOPO_DOM 1152 1160 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 1161 1181 Helical. {ECO:0000255}. FT TOPO_DOM 1182 1201 Lumenal. {ECO:0000255}. FT TRANSMEM 1202 1222 Helical. {ECO:0000255}. FT TOPO_DOM 1223 1231 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 1232 1252 Helical. {ECO:0000255}. FT TOPO_DOM 1253 1262 Lumenal. {ECO:0000255}. FT TRANSMEM 1263 1285 Helical. {ECO:0000255}. FT TOPO_DOM 1286 1355 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 1356 1376 Helical. {ECO:0000255}. FT TOPO_DOM 1377 1378 Lumenal. {ECO:0000255}. 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 2338 Lumenal. {ECO:0000255}. FT INTRAMEM 2339 2359 Helical. {ECO:0000255}. FT TOPO_DOM 2360 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 30 74 Hydrophobic; homodimerization of capsid FT protein C. {ECO:0000250}. FT REGION 383 396 Involved in fusion. {ECO:0000250}. FT REGION 1407 1446 Interacts with and activates NS3 FT protease. {ECO:0000255|PROSITE- FT ProRule:PRU00859}. FT MOTIF 1773 1776 DEAH box. 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 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:0000255}. FT SITE 121 122 Cleavage; by host signal peptidase. FT {ECO:0000250}. FT SITE 210 211 Cleavage; by host furin. {ECO:0000255}. FT SITE 285 286 Cleavage; by host signal peptidase. FT {ECO:0000255}. FT SITE 778 779 Cleavage; by host signal peptidase. FT {ECO:0000255}. FT SITE 1130 1131 Cleavage; by host. {ECO:0000255}. FT SITE 1354 1355 Cleavage; by viral protease NS3. FT {ECO:0000255}. FT SITE 1484 1485 Cleavage; by autolysis. {ECO:0000255}. FT SITE 2107 2108 Cleavage; by autolysis. {ECO:0000255}. FT SITE 2233 2234 Cleavage; by viral protease NS3. FT {ECO:0000255}. FT SITE 2256 2257 Cleavage; by host signal peptidase. FT {ECO:0000255}. FT SITE 2506 2507 Cleavage; by viral protease NS3. FT {ECO:0000255}. 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 CARBOHYD 134 134 N-linked (GlcNAc...); by host. FT {ECO:0000255}. FT CARBOHYD 150 150 N-linked (GlcNAc...); by host. FT {ECO:0000255}. FT CARBOHYD 908 908 N-linked (GlcNAc...); by host. FT {ECO:0000255}. FT CARBOHYD 986 986 N-linked (GlcNAc...); by host. FT {ECO:0000255}. FT DISULFID 288 315 {ECO:0000250}. FT DISULFID 345 401 {ECO:0000250}. FT DISULFID 359 390 {ECO:0000250}. FT DISULFID 377 406 {ECO:0000250}. FT DISULFID 467 568 {ECO:0000250}. FT DISULFID 585 615 {ECO:0000250}. 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 //