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 27-MAR-2024, entry version 135. DE RecName: Full=Genome polyprotein; DE Contains: DE RecName: Full=Capsid protein C; DE AltName: Full=Core protein; DE Contains: DE RecName: Full=Protein prM; DE Contains: DE RecName: Full=Peptide pr; DE Contains: DE RecName: Full=Small envelope protein M; DE AltName: Full=Matrix protein; DE Contains: DE RecName: Full=Envelope protein E; DE Contains: DE RecName: Full=Non-structural protein 1; DE Short=NS1; DE Contains: DE RecName: Full=Non-structural protein 2A; DE Short=NS2A; DE Contains: DE RecName: Full=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; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes; OC Amarillovirales; Flaviviridae; Orthoflavivirus; Orthoflavivirus flavi. 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., Pest S., RA Parent M., Schmitz H., Warnat M.-A., Niedrig M.; RT "Analysis of two imported cases of yellow fever infection from Ivory Coast RT 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 binding CC to the cell membrane and gathering the viral RNA into a nucleocapsid CC that forms the core of a mature virus particle. During virus entry, may CC induce genome penetration into the host cytoplasm after hemifusion CC induced by the surface proteins. Can migrate to the cell nucleus where CC it modulates host functions. {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 envelope CC proteins in trans-Golgi by binding to envelope protein E at pH6.0. CC After virion release in extracellular space, gets dissociated from E CC 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 Golgi CC compartment prior to virion release. prM-E cleavage is inefficient, and CC many virions are only partially matured. These uncleaved prM would play CC a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. CC -!- FUNCTION: [Small envelope protein M]: May play a role in virus budding. CC Exerts cytotoxic effects by activating a mitochondrial apoptotic CC pathway through M ectodomain. May display a viroporin activity. CC {ECO:0000250|UniProtKB:P17763}. CC -!- FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and CC mediates fusion between viral and cellular membranes. Envelope protein CC is synthesized in the endoplasmic reticulum in the form of heterodimer CC with protein prM. They play a role in virion budding in the ER, and the CC newly formed immature particle is covered with 60 spikes composed of CC heterodimer between precursor prM and envelope protein E. The virion is CC transported to the Golgi apparatus where the low pH causes dissociation CC of PrM-E 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 polyprotein, CC is targeted to three destinations: the viral replication cycle, the CC plasma membrane and the extracellular compartment. Essential for viral CC replication. Required for formation of the replication complex and CC recruitment of other non-structural proteins to the ER-derived membrane CC structures. Excreted as a hexameric lipoparticle that plays a role CC against host immune response. Antagonizing the complement function. CC Binds 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 antagonizes CC the host immune response. {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-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, NS2B- CC NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and CC unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus CC assembly (By similarity). {ECO:0000250|UniProtKB:P03314, CC ECO:0000255|PROSITE-ProRule:PRU00860}. CC -!- FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of CC the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy CC during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. 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|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 cellular CC 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 2'-O CC positions (By similarity). Besides its role in RNA genome replication, CC also prevents the establishment of cellular antiviral state by blocking CC the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I CC induces binding of NS5 to host IFN-activated transcription factor CC STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 CC ligase that interacts with and polyubiquitinates NS5 to promote its CC binding to STAT2 and trigger IFN-I signaling inhibition. CC {ECO:0000250|UniProtKB:P03314}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of CC the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; CC EC=3.4.21.91; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA- CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + CC S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'- CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA- CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, CC ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00924}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'- CC triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S- CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, CC Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; CC EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; CC -!- SUBUNIT: [Capsid protein C]: Homodimer (By similarity). Interacts (via CC N-terminus) with host EXOC1 (via C-terminus); this interaction results CC in EXOC1 degradation through the proteasome degradation pathway (By CC similarity). {ECO:0000250|UniProtKB:P17763}. CC -!- SUBUNIT: [Protein prM]: Forms heterodimers with envelope protein E in CC the endoplasmic reticulum and Golgi. {ECO:0000250|UniProtKB:P17763}. CC -!- SUBUNIT: [Envelope protein E]: Homodimer; in the endoplasmic reticulum CC and Golgi (By similarity). Interacts with protein prM (By similarity). CC Interacts with non-structural protein 1 (By similarity). CC {ECO:0000250|UniProtKB:P17763}. CC -!- SUBUNIT: [Non-structural protein 1]: Homodimer; Homohexamer when CC secreted (By similarity). Interacts with envelope protein E (By CC similarity). {ECO:0000250|UniProtKB:P17763}. CC -!- SUBUNIT: [Non-structural protein 2A]: Interacts (via N-terminus) with CC serine protease NS3. {ECO:0000250|UniProtKB:P03314}. CC -!- SUBUNIT: [Serine protease subunit NS2B]: Forms a heterodimer with CC serine protease NS3 (By similarity). May form homooligomers (By CC similarity). {ECO:0000250|UniProtKB:P17763}. CC -!- SUBUNIT: [Serine protease NS3]: Forms a heterodimer with NS2B (By CC similarity). Interacts with non-structural protein 2A (via N-terminus) CC (By similarity). Interacts with NS4B (By similarity). Interacts with CC unphosphorylated RNA-directed RNA polymerase NS5; this interaction CC stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity CC (By similarity). NS3 interacts with host PDCD6IP; this interaction CC contributes to virion release (By similarity). CC {ECO:0000250|UniProtKB:P17763}. CC -!- SUBUNIT: [Non-structural protein 4B]: Interacts with serine protease CC NS3 (By similarity). {ECO:0000250|UniProtKB:P17763}. CC -!- SUBUNIT: [RNA-directed RNA polymerase NS5]: Homodimer (By similarity). CC Interacts with host STAT2; this interaction prevents the establishment CC of cellular antiviral state (By similarity). Interacts with serine CC protease NS3 (By similarity). Interacts with host TRIM23; this CC interaction leads to NS5 ubiquitination (By similarity). CC {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 region CC {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 membrane CC {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein CC {ECO:0000255}. Note=ER membrane retention is mediated by the CC 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 membrane CC {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein CC {ECO:0000255}. Note=ER membrane retention is mediated by the CC transmembrane domains. {ECO:0000250|UniProtKB:P03314}. CC -!- SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted CC {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; CC Peripheral membrane protein; Lumenal side CC {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles CC hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. CC -!- SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic CC reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane CC protein {ECO:0000250|UniProtKB:P17763}. CC -!- SUBCELLULAR LOCATION: [Serine protease subunit NS2B]: Host endoplasmic CC reticulum membrane; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P17763}. CC -!- SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum CC membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane CC protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side CC {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently CC associated to 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 membrane CC protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated CC 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 membrane CC protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived CC 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 complex. CC NS5 protein is mainly localized in the nucleus rather than in ER CC vesicles. {ECO:0000250|UniProtKB:P17763}. CC -!- DOMAIN: The transmembrane domains of the small envelope protein M and CC envelope protein E contain an endoplasmic reticulum retention signal. CC {ECO:0000250|UniProtKB:P17763}. CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield CC mature proteins. The nascent capsid protein C contains a C-terminal CC hydrophobic domain that act as a signal sequence for translocation of CC prM into the lumen of the ER. Mature capsid protein C is cleaved at a CC site upstream of this hydrophobic domain by NS3. prM is cleaved in CC post-Golgi vesicles by a host furin, releasing the mature small CC envelope protein M, and peptide pr. Non-structural protein 2A-alpha, a CC C-terminally truncated form of non-structural protein 2A, results from CC partial cleavage by NS3. Specific enzymatic cleavages in vivo yield CC mature proteins peptide 2K acts as a signal sequence and is removed CC from the N-terminus of NS4B by the host signal peptidase in the ER CC lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease- CC mediated cleavage 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. This CC cleavage is incomplete as up to 30% of viral particles still carry CC 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 is CC glycosylated and this is required for efficient secretion of the CC protein from infected cells. {ECO:0000250|UniProtKB:P17763}. CC -!- PTM: Polyubiquitinated; ubiquitination is probably mediated by host CC TRIM23 and is prerequisite for NS5-STAT2 interaction. NS5 is not CC 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 localization. CC {ECO:0000250|UniProtKB:P17763}. CC -!- SIMILARITY: In the N-terminal section; belongs to the class I-like SAM- CC binding methyltransferase superfamily. mRNA cap 0-1 NS5-type CC methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}. 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 BMRB; Q6J3P1; -. DR SMR; Q6J3P1; -. DR MEROPS; S07.001; -. 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:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C: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:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC. DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW. DR GO; GO:0039564; P:disruption by virus of host JAK-STAT cascade via inhibition of STAT2 activity; 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:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR CDD; cd20761; capping_2-OMTase_Flaviviridae; 1. DR CDD; cd17931; DEXHc_viral_Ns3; 1. DR CDD; cd12149; Flavi_E_C; 1. DR CDD; cd17038; Flavi_M; 1. DR CDD; cd23204; Flavivirus_RdRp; 1. DR Gene3D; 1.10.10.930; -; 1. DR Gene3D; 1.10.260.90; -; 1. DR Gene3D; 1.20.1280.260; -; 1. DR Gene3D; 2.40.10.120; -; 2. DR Gene3D; 2.60.40.350; -; 1. DR Gene3D; 1.10.8.970; Flavivirus envelope glycoprotein M-like; 1. DR Gene3D; 2.60.260.50; Flavivirus polyprotein propeptide domain; 1. DR Gene3D; 3.30.70.2840; Flavivirus RNA-directed RNA polymerase, thumb domain; 3. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR Gene3D; 2.60.98.10; Tick-borne Encephalitis virus Glycoprotein, domain 1; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR Gene3D; 3.30.67.10; Viral Envelope Glycoprotein, domain 2; 1. DR Gene3D; 3.30.387.10; Viral Envelope Glycoprotein, domain 3; 1. DR InterPro; IPR043502; DNA/RNA_pol_sf. DR InterPro; IPR000069; Env_glycoprot_M_flavivir. DR InterPro; IPR038302; Env_glycoprot_M_sf_flavivir. DR InterPro; IPR013755; Flav_gly_cen_dom_subdom1. DR InterPro; IPR001122; Flavi_capsidC. DR InterPro; IPR037172; Flavi_capsidC_sf. DR InterPro; IPR011492; Flavi_DEAD. DR InterPro; IPR027287; Flavi_E_Ig-like. DR InterPro; IPR026470; Flavi_E_Stem/Anchor_dom. DR InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf. DR InterPro; IPR011998; Flavi_Glycoprot_E_cen/dimer. DR InterPro; IPR001157; Flavi_NS1. DR InterPro; IPR000752; Flavi_NS2A. DR InterPro; IPR000487; Flavi_NS2B. DR InterPro; IPR001850; Flavi_NS3_S7. DR InterPro; IPR000404; Flavi_NS4A. DR InterPro; IPR001528; Flavi_NS4B. DR InterPro; IPR046811; Flavi_NS5_thumb. DR InterPro; IPR002535; Flavi_propep. DR InterPro; IPR038688; Flavi_propep_sf. DR InterPro; IPR047530; Flavi_RdRp. DR InterPro; IPR000208; Flavi_RdRp_fingers/palm. DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf. DR InterPro; IPR014412; Gen_Poly_FLV. DR InterPro; IPR036253; Glycoprot_cen/dimer_sf. DR InterPro; IPR038055; Glycoprot_E_dimer_dom. DR InterPro; IPR013756; GlyE_cen_dom_subdom2. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR026490; mRNA_cap_0/1_MeTrfase. DR InterPro; IPR049486; NS3-hel_C_flaviviridae. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR NCBIfam; TIGR04240; flavi_E_stem; 1. DR Pfam; PF20907; Flav_NS3-hel_C; 1. DR Pfam; PF01003; Flavi_capsid; 1. DR Pfam; PF07652; Flavi_DEAD; 1. DR Pfam; PF21659; Flavi_E_stem; 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; PF20483; Flavi_NS5_thumb; 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; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR SUPFAM; SSF56983; Viral glycoprotein, central and dimerisation domains; 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; Disulfide bond; KW Fusion of virus membrane with host endosomal membrane; KW Fusion of virus membrane with host membrane; Glycoprotein; GTP-binding; KW Helicase; Host cytoplasm; Host endoplasmic reticulum; Host membrane; KW Host nucleus; Host-virus interaction; Hydrolase; KW Inhibition of host innate immune response by virus; KW Inhibition of host interferon signaling pathway by virus; KW Inhibition of host STAT2 by virus; Interferon antiviral system evasion; KW Membrane; 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; KW Suppressor of RNA silencing; Transcription; Transcription regulation; KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation; KW Viral attachment to host cell; Viral envelope protein; Viral immunoevasion; KW Viral penetration into host cytoplasm; Viral RNA replication; Virion; KW Virus endocytosis by host; Virus entry into host cell; Zinc. FT CHAIN 1..3411 FT /note="Genome polyprotein" FT /id="PRO_0000405158" FT CHAIN 1..101 FT /note="Capsid protein C" FT /evidence="ECO:0000250|UniProtKB:P03314" FT /id="PRO_0000261500" FT PROPEP 102..121 FT /note="ER anchor for the capsid protein C, removed in FT mature form by serine protease NS3" FT /evidence="ECO:0000250|UniProtKB:P03314" FT /id="PRO_0000261501" FT CHAIN 122..285 FT /note="Protein prM" FT /evidence="ECO:0000250|UniProtKB:P29990" FT /id="PRO_0000261502" FT CHAIN 122..210 FT /note="Peptide pr" FT /evidence="ECO:0000250|UniProtKB:P29990" FT /id="PRO_0000261503" FT CHAIN 211..285 FT /note="Small envelope protein M" FT /evidence="ECO:0000250|UniProtKB:P29990" FT /id="PRO_0000261504" FT CHAIN 286..778 FT /note="Envelope protein E" FT /evidence="ECO:0000250|UniProtKB:P29990" FT /id="PRO_0000261505" FT CHAIN 779..1130 FT /note="Non-structural protein 1" FT /evidence="ECO:0000250|UniProtKB:P03314" FT /id="PRO_0000261506" FT CHAIN 1131..1354 FT /note="Non-structural protein 2A" FT /evidence="ECO:0000250|UniProtKB:P29990" FT /id="PRO_0000261507" FT CHAIN 1131..1320 FT /note="Non-structural protein 2A-alpha" FT /evidence="ECO:0000250|UniProtKB:P29990" FT /id="PRO_0000261508" FT CHAIN 1355..1484 FT /note="Serine protease subunit NS2B" FT /evidence="ECO:0000250|UniProtKB:P03314" FT /id="PRO_0000261509" FT CHAIN 1485..2107 FT /note="Serine protease NS3" FT /evidence="ECO:0000250|UniProtKB:P03314" FT /id="PRO_0000261510" FT CHAIN 2108..2233 FT /note="Non-structural protein 4A" FT /evidence="ECO:0000250|UniProtKB:P03314" FT /id="PRO_0000261511" FT PEPTIDE 2234..2256 FT /note="Peptide 2k" FT /id="PRO_0000261512" FT CHAIN 2257..2506 FT /note="Non-structural protein 4B" FT /evidence="ECO:0000250|UniProtKB:P03314" FT /id="PRO_0000261513" FT CHAIN 2507..3411 FT /note="RNA-directed RNA polymerase NS5" FT /evidence="ECO:0000250|UniProtKB:P03314" FT /id="PRO_0000261514" FT TOPO_DOM 1..104 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 105..125 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 126..244 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 245..265 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 266..270 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 271..285 FT /note="Helical" FT /evidence="ECO:0000305" FT TOPO_DOM 286..730 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 731..751 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 752..757 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 758..778 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 779..1132 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P03314" FT TRANSMEM 1133..1153 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P03314" FT TOPO_DOM 1154..1201 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P03314" FT TRANSMEM 1202..1222 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P03314" FT TOPO_DOM 1223..1287 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:P03314" FT TRANSMEM 1288..1308 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P03314" FT TOPO_DOM 1309..1355 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P03314" FT TRANSMEM 1356..1376 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P03314" FT TOPO_DOM 1377..1378 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:P03314" FT TRANSMEM 1379..1399 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1400..1456 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT INTRAMEM 1457..1477 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1478..2157 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 2158..2178 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 2179..2186 FT /note="Lumenal" FT /evidence="ECO:0000255" FT INTRAMEM 2187..2207 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 2208..2209 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 2210..2230 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 2231..2241 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 2242..2262 FT /note="Helical; Note=Signal for NS4B" FT /evidence="ECO:0000255" FT TOPO_DOM 2263..2293 FT /note="Lumenal" FT /evidence="ECO:0000255" FT INTRAMEM 2294..2314 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 2315..2360 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 2361..2380 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 2381..2421 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 2422..2442 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 2443..2445 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 2446..2466 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 2467..3411 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 1485..1665 FT /note="Peptidase S7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860" FT DOMAIN 1669..1825 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 1820..1997 FT /note="Helicase C-terminal" FT DOMAIN 2507..2771 FT /note="mRNA cap 0-1 NS5-type MT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT DOMAIN 3035..3187 FT /note="RdRp catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539" FT REGION 383..396 FT /note="Fusion peptide" FT /evidence="ECO:0000250|UniProtKB:P14336" FT REGION 1407..1446 FT /note="Interacts with and activates NS3 protease" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00859" FT REGION 1673..1676 FT /note="Important for RNA-binding" FT /evidence="ECO:0000250|UniProtKB:P14340" FT REGION 1942..1961 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1773..1776 FT /note="DEAH box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT MOTIF 2878..2911 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250" FT ACT_SITE 1537 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860" FT ACT_SITE 1561 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860" FT ACT_SITE 1622 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00860" FT ACT_SITE 2567 FT /note="For 2'-O-MTase activity" FT /evidence="ECO:0000250|UniProtKB:Q6YMS4" FT ACT_SITE 2652 FT /note="For 2'-O-MTase activity" FT /evidence="ECO:0000250|UniProtKB:Q6YMS4" FT ACT_SITE 2688 FT /note="For 2'-O-MTase activity" FT /evidence="ECO:0000250|UniProtKB:Q6YMS4" FT ACT_SITE 2724 FT /note="For 2'-O-MTase activity" FT /evidence="ECO:0000250|UniProtKB:Q6YMS4" FT BINDING 1682..1689 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT BINDING 2562 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT BINDING 2592 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT BINDING 2593 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT BINDING 2610 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT BINDING 2611 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT BINDING 2637 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT BINDING 2638 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT BINDING 2653 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT BINDING 2726 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT BINDING 2945 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P14335" FT BINDING 2949 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P14335" FT BINDING 2954 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P14335" FT BINDING 2957 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P14335" FT BINDING 3222 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P14335" FT BINDING 3238 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P14335" FT BINDING 3357 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P14335" FT SITE 101..102 FT /note="Cleavage; by viral protease NS3" FT /evidence="ECO:0000250|UniProtKB:P03314" FT SITE 121..122 FT /note="Cleavage; by host signal peptidase" FT /evidence="ECO:0000250|UniProtKB:P03314" FT SITE 210..211 FT /note="Cleavage; by host furin" FT /evidence="ECO:0000250|UniProtKB:P29990" FT SITE 285..286 FT /note="Cleavage; by host signal peptidase" FT /evidence="ECO:0000250|UniProtKB:P29990" FT SITE 778..779 FT /note="Cleavage; by host signal peptidase" FT /evidence="ECO:0000250|UniProtKB:P03314" FT SITE 1130..1131 FT /note="Cleavage; by host" FT /evidence="ECO:0000250|UniProtKB:P29990" FT SITE 1354..1355 FT /note="Cleavage; by viral protease NS3" FT /evidence="ECO:0000250|UniProtKB:P29990" FT SITE 1484..1485 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000250|UniProtKB:P03314" FT SITE 1945 FT /note="Involved in NS3 ATPase and RTPase activities" FT /evidence="ECO:0000250|UniProtKB:P14335" FT SITE 1948 FT /note="Involved in NS3 ATPase and RTPase activities" FT /evidence="ECO:0000250|UniProtKB:P14335" FT SITE 2107..2108 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000250|UniProtKB:P03314" FT SITE 2233..2234 FT /note="Cleavage; by viral protease NS3" FT /evidence="ECO:0000250|UniProtKB:P29990" FT SITE 2256..2257 FT /note="Cleavage; by host signal peptidase" FT /evidence="ECO:0000250|UniProtKB:P29990" FT SITE 2506..2507 FT /note="Cleavage; by viral protease NS3" FT /evidence="ECO:0000250|UniProtKB:P03314" FT SITE 2519 FT /note="mRNA cap binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT SITE 2522 FT /note="mRNA cap binding; via carbonyl oxygen" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT SITE 2523 FT /note="mRNA cap binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT SITE 2525 FT /note="mRNA cap binding; via carbonyl oxygen" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT SITE 2530 FT /note="mRNA cap binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT SITE 2534 FT /note="mRNA cap binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT SITE 2567 FT /note="Essential for 2'-O-methyltransferase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT SITE 2652 FT /note="Essential for 2'-O-methyltransferase and N-7 FT methyltransferase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT SITE 2656 FT /note="mRNA cap binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT SITE 2688 FT /note="Essential for 2'-O-methyltransferase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT SITE 2719 FT /note="mRNA cap binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT SITE 2721 FT /note="mRNA cap binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT SITE 2724 FT /note="Essential for 2'-O-methyltransferase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00924" FT MOD_RES 2562 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P03314" FT CARBOHYD 134 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 150 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 908 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 986 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT DISULFID 288..315 FT /evidence="ECO:0000250|UniProtKB:P17763" FT DISULFID 345..406 FT /evidence="ECO:0000250|UniProtKB:P17763" FT DISULFID 345..401 FT /evidence="ECO:0000250" FT DISULFID 359..390 FT /evidence="ECO:0000250|UniProtKB:P17763" FT DISULFID 377..406 FT /evidence="ECO:0000250" FT DISULFID 377..401 FT /evidence="ECO:0000250|UniProtKB:P17763" FT DISULFID 467..568 FT /evidence="ECO:0000250|UniProtKB:P17763" FT DISULFID 585..615 FT /evidence="ECO:0000250|UniProtKB:P17763" FT DISULFID 782..793 FT /evidence="ECO:0000250|UniProtKB:P17763" FT DISULFID 833..921 FT /evidence="ECO:0000250|UniProtKB:P17763" FT DISULFID 957..1002 FT /evidence="ECO:0000250|UniProtKB:P17763" FT DISULFID 1058..1107 FT /evidence="ECO:0000250|UniProtKB:P17763" FT DISULFID 1069..1091 FT /evidence="ECO:0000250|UniProtKB:P17763" FT DISULFID 1090..1094 FT /evidence="ECO:0000250|UniProtKB:P17763" FT VARIANT 107 FT /note="A -> T (in strain: Isolate Gambia 2001)" FT VARIANT 110 FT /note="F -> L (in strain: Isolate Gambia 2001)" FT VARIANT 116 FT /note="L -> I (in strain: Isolate Gambia 2001)" FT VARIANT 148 FT /note="A -> T (in strain: Isolate Gambia 2001)" FT VARIANT 712 FT /note="L -> F (in strain: Isolate Gambia 2001)" FT VARIANT 899 FT /note="N -> S (in strain: Isolate Gambia 2001)" FT VARIANT 1185 FT /note="T -> I (in strain: Isolate Gambia 2001)" FT VARIANT 1297 FT /note="A -> T (in strain: Isolate Gambia 2001)" FT VARIANT 1433 FT /note="S -> N (in strain: Isolate Gambia 2001)" FT VARIANT 2056 FT /note="D -> E (in strain: Isolate Gambia 2001)" FT VARIANT 2161 FT /note="A -> V (in strain: Isolate Gambia 2001)" FT VARIANT 2373 FT /note="M -> T (in strain: Isolate Gambia 2001)" FT VARIANT 2438 FT /note="A -> S (in strain: Isolate Gambia 2001)" FT VARIANT 2644 FT /note="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 //