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 28-FEB-2018, entry version 106. 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; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage; OC Flaviviridae; Flavivirus; Yellow fever virus group. OX NCBI_TaxID=407136; OH NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti). OH NCBI_TaxID=299629; Aedes luteocephalus (Mosquito). OH NCBI_TaxID=7161; Aedes simpsoni. OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=314293; Simiiformes. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate Gambia/2001, and Isolate Ivory Coast/1999; RX PubMed=16036176; DOI=10.1016/j.jcv.2004.12.001; RA Bae H.-G., Drosten C., Emmerich P., Colebunders R., Hantson P., RA Pest S., Parent M., Schmitz H., Warnat M.-A., Niedrig M.; RT "Analysis of two imported cases of yellow fever infection from Ivory RT Coast and The Gambia to Germany and Belgium."; RL J. Clin. Virol. 33:274-280(2005). CC -!- FUNCTION: Capsid protein C: Plays a role in virus budding by CC binding to the cell membrane and gathering the viral RNA into a CC nucleocapsid that forms the core of a mature virus particle. CC During virus entry, may induce genome penetration into the host CC cytoplasm after hemifusion induced by the surface proteins. Can CC migrate to the cell nucleus where it modulates host functions. CC {ECO:0000250|UniProtKB:P17763}. CC -!- FUNCTION: Capsid protein C: Inhibits RNA silencing by interfering CC with host Dicer. {ECO:0000250|UniProtKB:P03314}. CC -!- FUNCTION: Peptide pr: Prevents premature fusion activity of CC envelope proteins in trans-Golgi by binding to envelope protein E CC at pH6.0. After virion release in extracellular space, gets CC dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. CC -!- FUNCTION: Protein prM: Acts as a chaperone for envelope protein E CC during intracellular virion assembly by masking and inactivating CC envelope protein E fusion peptide. prM is the only viral peptide CC matured by host furin in the trans-Golgi network probably to avoid CC catastrophic activation of the viral fusion activity in acidic CC Golgi compartment prior to virion release. prM-E cleavage is CC inefficient, and many virions are only partially matured. These CC uncleaved prM would play a role in immune evasion. CC {ECO:0000250|UniProtKB:P17763}. CC -!- FUNCTION: Small envelope protein M: May play a role in virus CC budding. Exerts cytotoxic effects by activating a mitochondrial CC apoptotic pathway through M ectodomain. May display a viroporin CC activity. {ECO:0000250|UniProtKB:P17763}. CC -!- FUNCTION: Envelope protein E: Binds to host cell surface receptor CC and mediates fusion between viral and cellular membranes. Envelope CC protein is synthesized in the endoplasmic reticulum in the form of CC heterodimer with protein prM. They play a role in virion budding CC in the ER, and the newly formed immature particle is covered with CC 60 spikes composed of heterodimer between precursor prM and CC envelope protein E. The virion is transported to the Golgi CC apparatus where the low pH causes dissociation of PrM-E CC heterodimers and formation of E homodimers. prM-E cleavage is CC inefficient, and many virions are only partially matured. These CC uncleaved prM would play a role in immune evasion. CC {ECO:0000250|UniProtKB:P17763}. CC -!- FUNCTION: Non-structural protein 1: Involved in immune evasion, CC pathogenesis and viral replication. Once cleaved off the CC polyprotein, is targeted to three destinations: the viral CC replication cycle, the plasma membrane and the extracellular CC compartment. Essential for viral replication. Required for CC formation of the replication complex and recruitment of other non- CC structural proteins to the ER-derived membrane structures. CC Excreted as a hexameric lipoparticle that plays a role against CC host immune response. Antagonizing the complement function. Binds CC to the host macrophages and dendritic cells. Inhibits signal CC transduction originating from Toll-like receptor 3 (TLR3). CC {ECO:0000250|UniProtKB:Q9Q6P4}. CC -!- FUNCTION: Non-structural protein 2A: Component of the viral RNA CC replication complex that functions in virion assembly and CC antagonizes the host immune response. CC {ECO:0000250|UniProtKB:P17763}. CC -!- FUNCTION: Serine protease subunit NS2B: Required cofactor for the CC serine protease function of NS3. May have membrane-destabilizing CC activity and form viroporins (By similarity). CC {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE- CC ProRule:PRU00859}. CC -!- FUNCTION: Serine protease NS3: Displays three enzymatic CC activities: serine protease, NTPase and RNA helicase. NS3 serine CC protease, in association with NS2B, performs its autocleavage and CC cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, CC NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA CC helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. CC Also plays a role in virus assembly (By similarity). CC {ECO:0000250|UniProtKB:P03314, ECO:0000255|PROSITE- CC ProRule:PRU00860}. CC -!- FUNCTION: Non-structural protein 4A: Regulates the ATPase activity CC of the NS3 helicase activity. NS4A allows NS3 helicase to conserve CC energy during unwinding. {ECO:0000250|UniProtKB:Q9Q6P4}. CC -!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and CC is required for the interferon antagonism activity of the latter. CC {ECO:0000250|UniProtKB:P17763}. CC -!- FUNCTION: Non-structural protein 4B: Induces the formation of ER- CC derived membrane vesicles where the viral replication takes place. CC Inhibits interferon (IFN)-induced host STAT1 phosphorylation and CC nuclear translocation, thereby preventing the establishment of CC cellular antiviral state by blocking the IFN-alpha/beta pathway. CC {ECO:0000250|UniProtKB:Q9Q6P4}. CC -!- FUNCTION: RNA-directed RNA polymerase NS5: Replicates the viral CC (+) and (-) RNA genome, and performs the capping of genomes in the CC cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose CC 2'-O positions (By similarity). Besides its role in RNA genome CC replication, also prevents the establishment of cellular antiviral CC state by blocking the interferon-alpha/beta (IFN-alpha/beta) CC signaling pathway. IFN-I induces binding of NS5 to host IFN- CC activated transcription factor STAT2, preventing its CC transcriptional activity. Host TRIM23 is the E3 ligase that CC interacts with and polyubiquitinates NS5 to promote its binding to CC STAT2 and trigger IFN-I signaling inhibition. CC {ECO:0000250|UniProtKB:P03314}. CC -!- CATALYTIC ACTIVITY: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds CC in which each of the Xaa can be either Arg or Lys and Yaa can be CC either Ser or Ala. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}. CC -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S- CC adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. {ECO:0000255|PROSITE- CC ProRule:PRU00924}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl CC 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S- CC adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'- CC triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA]. CC {ECO:0000255|PROSITE-ProRule:PRU00924}. CC -!- SUBUNIT: Capsid protein C: Homodimer. Interacts (via N-terminus) CC with host EXOC1 (via C-terminus); this interaction results in CC EXOC1 degradation through the proteasome degradation pathway. CC Protein prM: Forms heterodimers with envelope protein E in the CC endoplasmic reticulum and Golgi. Envelope protein E: Homodimer; in CC the endoplasmic reticulum and Golgi. Interacts with protein prM. CC Interacts with non-structural protein 1. Non-structural protein 1: CC Homodimer; Homohexamer when secreted. Interacts with envelope CC protein E. Non-structural protein 2A: Interacts (via N-terminus) CC with serine protease NS3. Non-structural protein 2B: Forms a CC heterodimer with serine protease NS3. May form homooligomers. CC Serine protease NS3: Forms a heterodimer with NS2B. Interacts with CC non-structural protein 2A (via N-terminus). Interacts with NS4B. CC Interacts with unphosphorylated RNA-directed RNA polymerase NS5; CC this interaction stimulates RNA-directed RNA polymerase NS5 CC guanylyltransferase activity. NS3 interacts with host PDCD6IP; CC this interaction contributes to virion release. Non-structural CC protein 4B: Interacts with serine protease NS3. RNA-directed RNA CC polymerase NS5: Homodimer. Interacts with host STAT2; this CC interaction prevents the establishment of cellular antiviral CC state. Interacts with host TRIM23; this interaction leads to NS5 CC ubiquitination. {ECO:0000250|UniProtKB:P03314}. CC -!- SUBCELLULAR LOCATION: Capsid protein C: Virion CC {ECO:0000250|UniProtKB:P17763}. Host nucleus CC {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear CC region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm CC {ECO:0000250|UniProtKB:P17763}. CC -!- SUBCELLULAR LOCATION: Peptide pr: Secreted CC {ECO:0000250|UniProtKB:P17763}. CC -!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane CC {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum CC membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane CC protein {ECO:0000255}. Note=ER membrane retention is mediated by CC the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. CC -!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane CC {ECO:0000305}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum CC membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane CC protein {ECO:0000255}. Note=ER membrane retention is mediated by CC the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. CC -!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted CC {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum CC membrane; Peripheral membrane protein; Lumenal side CC {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived CC vesicles hosting the replication complex. CC {ECO:0000250|UniProtKB:Q9Q6P4}. CC -!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic CC reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass CC membrane protein {ECO:0000250|UniProtKB:P17763}. CC -!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host CC endoplasmic reticulum membrane; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P17763}. CC -!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic CC reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; CC Peripheral membrane protein {ECO:0000255|PROSITE- CC ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE- CC ProRule:PRU00860}. Note=Remains non-covalently associated to CC serine protease subunit NS2B. {ECO:0000255|PROSITE- CC ProRule:PRU00860}. CC -!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic CC reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass CC membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in CC RE-associated vesicles hosting the replication complex. CC {ECO:0000250|UniProtKB:P17763}. CC -!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic CC reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass CC membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in CC RE-derived vesicles hosting the replication complex. CC {ECO:0000250|UniProtKB:Q9Q6P4}. CC -!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase NS5: Host CC endoplasmic reticulum membrane; Peripheral membrane protein; CC Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}. CC Note=Located in RE-associated vesicles hosting the replication CC complex. NS5 protein is mainly localized in the nucleus rather CC than in ER vesicles. {ECO:0000250|UniProtKB:P17763}. CC -!- DOMAIN: The transmembrane domains of the small envelope protein M CC and envelope protein E contain an endoplasmic reticulum retention CC signal. {ECO:0000250|UniProtKB:P17763}. CC -!- PTM: Genome polyprotein: Specific enzymatic cleavages in vivo CC yield mature proteins. The nascent capsid protein C contains a C- CC terminal hydrophobic domain that act as a signal sequence for CC translocation of prM into the lumen of the ER. Mature capsid CC protein C is cleaved at a site upstream of this hydrophobic domain CC by NS3. prM is cleaved in post-Golgi vesicles by a host furin, CC releasing the mature small envelope protein M, and peptide pr. CC Non-structural protein 2A-alpha, a C-terminally truncated form of CC non-structural protein 2A, results from partial cleavage by NS3. CC Specific enzymatic cleavages in vivo yield mature proteins peptide CC 2K acts as a signal sequence and is removed from the N-terminus of CC NS4B by the host signal peptidase in the ER lumen. Signal cleavage CC at the 2K-4B site requires a prior NS3 protease-mediated cleavage CC at the 4A-2K site. {ECO:0000250|UniProtKB:P03314}. CC -!- PTM: Protein prM: Cleaved in post-Golgi vesicles by a host furin, CC releasing the mature small envelope protein M, and peptide pr. CC This cleavage is incomplete as up to 30% of viral particles still CC carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}. CC -!- PTM: Envelope protein E: N-glycosylated. CC {ECO:0000250|UniProtKB:P17763}. CC -!- PTM: Non-structural protein 1: N-glycosylated. The excreted form CC is glycosylated and this is required for efficient secretion of CC the protein from infected cells. {ECO:0000250|UniProtKB:P17763}. CC -!- PTM: Polyubiquitinated; ubiquitination is probably mediated by CC host TRIM23 and is prerequisite for NS5-STAT2 interaction. NS5 is CC not ISGylated or sumoylated. {ECO:0000250|UniProtKB:P03314}. CC -!- PTM: RNA-directed RNA polymerase NS5: Phosphorylated on serines CC residues. This phosphorylation may trigger NS5 nuclear CC localization. {ECO:0000250|UniProtKB:P17763}. CC -!- SIMILARITY: In the N-terminal section; belongs to the class I-like CC SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type CC methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}. 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; -. DR OrthoDB; VOG090001DL; -. DR Proteomes; UP000007532; Genome. DR Proteomes; UP000141257; Genome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro. 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:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro. DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW. DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW. DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW. DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR CDD; cd12149; Flavi_E_C; 1. DR CDD; cd00079; HELICc; 1. DR CDD; cd06174; MFS; 1. DR Gene3D; 2.60.40.350; -; 1. DR Gene3D; 2.60.98.10; -; 3. DR InterPro; IPR011492; DEAD_Flavivir. DR InterPro; IPR000069; Env_glycoprot_M_flavivir. DR InterPro; IPR001122; Flavi_capsidC. DR InterPro; IPR027287; Flavi_E_Ig-like. DR InterPro; IPR026470; Flavi_E_Stem/Anchor_dom. DR InterPro; IPR001157; Flavi_NS1. DR InterPro; IPR000752; Flavi_NS2A. DR InterPro; IPR000487; Flavi_NS2B. DR InterPro; IPR000404; Flavi_NS4A. DR InterPro; IPR001528; Flavi_NS4B. DR InterPro; IPR002535; Flavi_propep. DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf. DR InterPro; IPR001850; Flavivirus_NS3_S7. DR InterPro; IPR014412; Gen_Poly_FLV. DR InterPro; IPR011998; Glycoprot_cen/dimer. DR InterPro; IPR036253; Glycoprot_cen/dimer_sf. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR026490; mRNA_cap_0/1_MeTrfase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR000208; RNA-dir_pol_flavivirus. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01003; Flavi_capsid; 1. DR Pfam; PF07652; Flavi_DEAD; 1. DR Pfam; PF02832; Flavi_glycop_C; 1. DR Pfam; PF00869; Flavi_glycoprot; 1. DR Pfam; PF01004; Flavi_M; 1. DR Pfam; PF00948; Flavi_NS1; 1. DR Pfam; PF01005; Flavi_NS2A; 1. DR Pfam; PF01002; Flavi_NS2B; 1. DR Pfam; PF01350; Flavi_NS4A; 1. DR Pfam; PF01349; Flavi_NS4B; 1. DR Pfam; PF00972; Flavi_NS5; 1. DR Pfam; PF01570; Flavi_propep; 1. DR Pfam; PF01728; FtsJ; 1. DR Pfam; PF00949; Peptidase_S7; 1. DR PIRSF; PIRSF003817; Gen_Poly_FLV; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF50494; SSF50494; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF53335; SSF53335; 1. DR SUPFAM; SSF56983; SSF56983; 1. DR SUPFAM; SSF81296; SSF81296; 1. DR TIGRFAMs; TIGR04240; flavi_E_stem; 1. DR PROSITE; PS51527; FLAVIVIRUS_NS2B; 1. DR PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. DR PROSITE; PS51591; RNA_CAP01_NS5_MT; 1. PE 3: Inferred from homology; KW Activation of host autophagy by virus; ATP-binding; Capsid protein; KW Clathrin-mediated endocytosis of virus by host; KW Cleavage on pair of basic residues; Complete proteome; Disulfide bond; KW Fusion of virus membrane with host endosomal membrane; KW Fusion of virus membrane with host membrane; Glycoprotein; KW GTP-binding; Helicase; Host cytoplasm; Host endoplasmic reticulum; KW Host membrane; Host nucleus; Host-virus interaction; Hydrolase; KW Inhibition of host innate immune response by virus; KW Inhibition of host interferon signaling pathway by virus; KW Inhibition of host STAT2 by virus; Membrane; Metal-binding; KW Methyltransferase; mRNA capping; mRNA processing; KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase; KW Phosphoprotein; Protease; RNA-binding; RNA-directed RNA polymerase; KW S-adenosyl-L-methionine; Secreted; Serine protease; KW Suppressor of RNA silencing; Transcription; Transcription regulation; KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation; KW Viral attachment to host cell; Viral envelope protein; KW Viral immunoevasion; Viral penetration into host cytoplasm; KW Viral RNA replication; Virion; Virus endocytosis by host; KW Virus entry into host cell; Zinc. FT CHAIN 1 3411 Genome polyprotein. FT /FTId=PRO_0000405158. FT CHAIN 1 101 Capsid protein C. FT {ECO:0000250|UniProtKB:P03314}. FT /FTId=PRO_0000261500. FT PROPEP 102 121 ER anchor for the capsid protein C, FT removed in mature form by serine protease FT NS3. {ECO:0000250|UniProtKB:P03314}. FT /FTId=PRO_0000261501. FT CHAIN 122 285 Protein prM. FT {ECO:0000250|UniProtKB:P29990}. FT /FTId=PRO_0000261502. FT CHAIN 122 210 Peptide pr. FT {ECO:0000250|UniProtKB:P29990}. FT /FTId=PRO_0000261503. FT CHAIN 211 285 Small envelope protein M. FT {ECO:0000250|UniProtKB:P29990}. FT /FTId=PRO_0000261504. FT CHAIN 286 778 Envelope protein E. FT {ECO:0000250|UniProtKB:P29990}. FT /FTId=PRO_0000261505. FT CHAIN 779 1130 Non-structural protein 1. FT {ECO:0000250|UniProtKB:P03314}. FT /FTId=PRO_0000261506. FT CHAIN 1131 1354 Non-structural protein 2A. FT {ECO:0000250|UniProtKB:P29990}. FT /FTId=PRO_0000261507. FT CHAIN 1131 1320 Non-structural protein 2A-alpha. FT {ECO:0000250|UniProtKB:P29990}. FT /FTId=PRO_0000261508. FT CHAIN 1355 1484 Serine protease subunit NS2B. FT {ECO:0000250|UniProtKB:P03314}. FT /FTId=PRO_0000261509. FT CHAIN 1485 2107 Serine protease NS3. FT {ECO:0000250|UniProtKB:P03314}. FT /FTId=PRO_0000261510. FT CHAIN 2108 2233 Non-structural protein 4A. FT {ECO:0000250|UniProtKB:P03314}. FT /FTId=PRO_0000261511. FT PEPTIDE 2234 2256 Peptide 2k. FT /FTId=PRO_0000261512. FT CHAIN 2257 2506 Non-structural protein 4B. FT {ECO:0000250|UniProtKB:P03314}. FT /FTId=PRO_0000261513. FT CHAIN 2507 3411 RNA-directed RNA polymerase NS5. FT {ECO:0000250|UniProtKB:P03314}. FT /FTId=PRO_0000261514. FT TOPO_DOM 1 104 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 105 125 Helical. {ECO:0000255}. FT TOPO_DOM 126 244 Extracellular. {ECO:0000255}. FT TRANSMEM 245 265 Helical. {ECO:0000255}. FT TOPO_DOM 266 270 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 271 285 Helical. {ECO:0000305}. FT TOPO_DOM 286 730 Extracellular. {ECO:0000255}. FT TRANSMEM 731 751 Helical. {ECO:0000255}. FT TOPO_DOM 752 757 Extracellular. {ECO:0000255}. FT TRANSMEM 758 778 Helical. {ECO:0000255}. FT TOPO_DOM 779 1132 Extracellular. FT {ECO:0000250|UniProtKB:P03314}. FT TRANSMEM 1133 1153 Helical. {ECO:0000250|UniProtKB:P03314}. FT TOPO_DOM 1154 1201 Cytoplasmic. FT {ECO:0000250|UniProtKB:P03314}. FT TRANSMEM 1202 1222 Helical. {ECO:0000250|UniProtKB:P03314}. FT TOPO_DOM 1223 1287 Lumenal. {ECO:0000250|UniProtKB:P03314}. FT TRANSMEM 1288 1308 Helical. {ECO:0000250|UniProtKB:P03314}. FT TOPO_DOM 1309 1355 Cytoplasmic. FT {ECO:0000250|UniProtKB:P03314}. FT TRANSMEM 1356 1376 Helical. {ECO:0000250|UniProtKB:P03314}. FT TOPO_DOM 1377 1378 Lumenal. {ECO:0000250|UniProtKB:P03314}. FT TRANSMEM 1379 1399 Helical. {ECO:0000255}. FT TOPO_DOM 1400 1456 Cytoplasmic. {ECO:0000255}. FT INTRAMEM 1457 1477 Helical. {ECO:0000255}. FT TOPO_DOM 1478 2157 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 2158 2178 Helical. {ECO:0000255}. FT TOPO_DOM 2179 2186 Lumenal. {ECO:0000255}. FT INTRAMEM 2187 2207 Helical. {ECO:0000255}. FT TOPO_DOM 2208 2209 Lumenal. {ECO:0000255}. FT TRANSMEM 2210 2230 Helical. {ECO:0000255}. FT TOPO_DOM 2231 2241 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 2242 2262 Helical; Note=Signal for NS4B. FT {ECO:0000255}. FT TOPO_DOM 2263 2293 Lumenal. {ECO:0000255}. FT INTRAMEM 2294 2314 Helical. {ECO:0000255}. FT TOPO_DOM 2315 2360 Lumenal. {ECO:0000255}. FT TRANSMEM 2361 2380 Helical. {ECO:0000255}. FT TOPO_DOM 2381 2421 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 2422 2442 Helical. {ECO:0000255}. FT TOPO_DOM 2443 2445 Lumenal. {ECO:0000255}. FT TRANSMEM 2446 2466 Helical. {ECO:0000255}. FT TOPO_DOM 2467 3411 Cytoplasmic. {ECO:0000255}. FT DOMAIN 1485 1665 Peptidase S7. {ECO:0000255|PROSITE- FT ProRule:PRU00860}. FT DOMAIN 1669 1825 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 1820 1997 Helicase C-terminal. FT DOMAIN 2507 2771 mRNA cap 0-1 NS5-type MT. FT {ECO:0000255|PROSITE-ProRule:PRU00924}. FT DOMAIN 3035 3187 RdRp catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU00539}. FT NP_BIND 1682 1689 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT REGION 383 396 Fusion peptide. FT {ECO:0000250|UniProtKB:P14336}. FT REGION 1407 1446 Interacts with and activates NS3 FT protease. {ECO:0000255|PROSITE- FT ProRule:PRU00859}. FT REGION 1673 1676 Important for RNA-binding. FT {ECO:0000250|UniProtKB:P14340}. FT MOTIF 1773 1776 DEAH box. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 2878 2911 Nuclear localization signal. FT {ECO:0000250}. FT COMPBIAS 2656 2660 Poly-Ser. FT ACT_SITE 1537 1537 Charge relay system; for serine protease FT NS3 activity. {ECO:0000255|PROSITE- FT ProRule:PRU00860}. FT ACT_SITE 1561 1561 Charge relay system; for serine protease FT NS3 activity. {ECO:0000255|PROSITE- FT ProRule:PRU00860}. FT ACT_SITE 1622 1622 Charge relay system; for serine protease FT NS3 activity. {ECO:0000255|PROSITE- FT ProRule:PRU00860}. FT ACT_SITE 2567 2567 For 2'-O-MTase activity. FT {ECO:0000250|UniProtKB:Q6YMS4}. FT ACT_SITE 2652 2652 For 2'-O-MTase activity. FT {ECO:0000250|UniProtKB:Q6YMS4}. FT ACT_SITE 2688 2688 For 2'-O-MTase activity. FT {ECO:0000250|UniProtKB:Q6YMS4}. FT ACT_SITE 2724 2724 For 2'-O-MTase activity. FT {ECO:0000250|UniProtKB:Q6YMS4}. FT METAL 2945 2945 Zinc 1. {ECO:0000250|UniProtKB:P14335}. FT METAL 2949 2949 Zinc 1; via tele nitrogen. FT {ECO:0000250|UniProtKB:P14335}. FT METAL 2954 2954 Zinc 1. {ECO:0000250|UniProtKB:P14335}. FT METAL 2957 2957 Zinc 1. {ECO:0000250|UniProtKB:P14335}. FT METAL 3222 3222 Zinc 2; via tele nitrogen. FT {ECO:0000250|UniProtKB:P14335}. FT METAL 3238 3238 Zinc 2. {ECO:0000250|UniProtKB:P14335}. FT METAL 3357 3357 Zinc 2. {ECO:0000250|UniProtKB:P14335}. FT BINDING 2519 2519 mRNA cap. {ECO:0000255|PROSITE- FT ProRule:PRU00924}. FT BINDING 2522 2522 mRNA cap; via carbonyl oxygen. FT {ECO:0000255|PROSITE-ProRule:PRU00924}. FT BINDING 2523 2523 mRNA cap. {ECO:0000255|PROSITE- FT ProRule:PRU00924}. FT BINDING 2525 2525 mRNA cap; via carbonyl oxygen. FT {ECO:0000255|PROSITE-ProRule:PRU00924}. FT BINDING 2534 2534 mRNA cap. {ECO:0000255|PROSITE- FT ProRule:PRU00924}. FT BINDING 2562 2562 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU00924}. FT BINDING 2592 2592 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|PROSITE- FT ProRule:PRU00924}. FT BINDING 2593 2593 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|PROSITE- FT ProRule:PRU00924}. FT BINDING 2610 2610 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU00924}. FT BINDING 2611 2611 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|PROSITE- FT ProRule:PRU00924}. FT BINDING 2637 2637 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU00924}. FT BINDING 2638 2638 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|PROSITE- FT ProRule:PRU00924}. FT BINDING 2656 2656 mRNA cap. {ECO:0000255|PROSITE- FT ProRule:PRU00924}. FT BINDING 2719 2719 mRNA cap. {ECO:0000255|PROSITE- FT ProRule:PRU00924}. FT BINDING 2721 2721 mRNA cap. {ECO:0000255|PROSITE- FT ProRule:PRU00924}. FT BINDING 2726 2726 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU00924}. FT SITE 101 102 Cleavage; by viral protease NS3. FT {ECO:0000250|UniProtKB:P03314}. FT SITE 121 122 Cleavage; by host signal peptidase. FT {ECO:0000250|UniProtKB:P03314}. FT SITE 210 211 Cleavage; by host furin. FT {ECO:0000250|UniProtKB:P29990}. FT SITE 285 286 Cleavage; by host signal peptidase. FT {ECO:0000250|UniProtKB:P29990}. FT SITE 778 779 Cleavage; by host signal peptidase. FT {ECO:0000250|UniProtKB:P03314}. FT SITE 1130 1131 Cleavage; by host. FT {ECO:0000250|UniProtKB:P29990}. FT SITE 1354 1355 Cleavage; by viral protease NS3. FT {ECO:0000250|UniProtKB:P29990}. FT SITE 1484 1485 Cleavage; by autolysis. FT {ECO:0000250|UniProtKB:P03314}. FT SITE 1945 1945 Involved in NS3 ATPase and RTPase FT activities. FT {ECO:0000250|UniProtKB:P14335}. FT SITE 1948 1948 Involved in NS3 ATPase and RTPase FT activities. FT {ECO:0000250|UniProtKB:P14335}. FT SITE 2107 2108 Cleavage; by autolysis. FT {ECO:0000250|UniProtKB:P03314}. FT SITE 2233 2234 Cleavage; by viral protease NS3. FT {ECO:0000250|UniProtKB:P29990}. FT SITE 2256 2257 Cleavage; by host signal peptidase. FT {ECO:0000250|UniProtKB:P29990}. FT SITE 2506 2507 Cleavage; by viral protease NS3. FT {ECO:0000250|UniProtKB:P03314}. FT SITE 2530 2530 mRNA cap binding. {ECO:0000255|PROSITE- FT ProRule:PRU00924}. FT SITE 2567 2567 Essential for 2'-O-methyltransferase FT activity. {ECO:0000255|PROSITE- FT ProRule:PRU00924}. FT SITE 2652 2652 Essential for 2'-O-methyltransferase and FT N-7 methyltransferase activity. FT {ECO:0000255|PROSITE-ProRule:PRU00924}. FT SITE 2653 2653 S-adenosyl-L-methionine binding. FT {ECO:0000255|PROSITE-ProRule:PRU00924}. FT SITE 2688 2688 Essential for 2'-O-methyltransferase FT activity. {ECO:0000255|PROSITE- FT ProRule:PRU00924}. FT SITE 2724 2724 Essential for 2'-O-methyltransferase FT activity. {ECO:0000255|PROSITE- FT ProRule:PRU00924}. FT MOD_RES 2562 2562 Phosphoserine. FT {ECO:0000250|UniProtKB:P03314}. FT CARBOHYD 134 134 N-linked (GlcNAc...) asparagine; by host. FT {ECO:0000255}. FT CARBOHYD 150 150 N-linked (GlcNAc...) asparagine; by host. FT {ECO:0000255}. FT CARBOHYD 908 908 N-linked (GlcNAc...) asparagine; by host. FT {ECO:0000255}. FT CARBOHYD 986 986 N-linked (GlcNAc...) asparagine; by host. FT {ECO:0000255}. FT DISULFID 288 315 {ECO:0000250|UniProtKB:P17763}. FT DISULFID 345 406 {ECO:0000250|UniProtKB:P17763}. FT DISULFID 345 401 {ECO:0000250}. FT DISULFID 359 390 {ECO:0000250|UniProtKB:P17763}. FT DISULFID 377 406 {ECO:0000250}. FT DISULFID 377 401 {ECO:0000250|UniProtKB:P17763}. FT DISULFID 467 568 {ECO:0000250|UniProtKB:P17763}. FT DISULFID 585 615 {ECO:0000250|UniProtKB:P17763}. FT DISULFID 782 793 {ECO:0000250|UniProtKB:P17763}. FT DISULFID 833 921 {ECO:0000250|UniProtKB:P17763}. FT DISULFID 957 1002 {ECO:0000250|UniProtKB:P17763}. FT DISULFID 1058 1107 {ECO:0000250|UniProtKB:P17763}. FT DISULFID 1069 1091 {ECO:0000250|UniProtKB:P17763}. FT DISULFID 1090 1094 {ECO:0000250|UniProtKB:P17763}. FT VARIANT 107 107 A -> T (in strain: Isolate Gambia 2001). FT VARIANT 110 110 F -> L (in strain: Isolate Gambia 2001). FT VARIANT 116 116 L -> I (in strain: Isolate Gambia 2001). FT VARIANT 148 148 A -> T (in strain: Isolate Gambia 2001). FT VARIANT 712 712 L -> F (in strain: Isolate Gambia 2001). FT VARIANT 899 899 N -> S (in strain: Isolate Gambia 2001). FT VARIANT 1185 1185 T -> I (in strain: Isolate Gambia 2001). FT VARIANT 1297 1297 A -> T (in strain: Isolate Gambia 2001). FT VARIANT 1433 1433 S -> N (in strain: Isolate Gambia 2001). FT VARIANT 2056 2056 D -> E (in strain: Isolate Gambia 2001). FT VARIANT 2161 2161 A -> V (in strain: Isolate Gambia 2001). FT VARIANT 2373 2373 M -> T (in strain: Isolate Gambia 2001). FT VARIANT 2438 2438 A -> S (in strain: Isolate Gambia 2001). FT VARIANT 2644 2644 M -> V (in strain: Isolate Gambia 2001). SQ SEQUENCE 3411 AA; 378956 MW; C121A19ABEA92218 CRC64; MSGRKAQGKT LGVNMVRRGV RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF FLFNILTGKK ITAHLKRLWK MLDPRQGLAV LRKVKRVVAS LMRGLSSRKR RSHDALAVQF LILGMLLMAG GVTLVRKNRW LLLNVTSEDL GKTFSVGAGN CTTNILEAKY WCPDSMEYNC PNLSPREEPD DIDCWCYGVE NVRVAYGKCD SAGRSRRSRR AIDLPTHENH GLKTRQEKWM TGRMGERQLQ KIERWLVRNP FFAVTALTIA YLVGSNMTQR VVIALLVLAV GPAYSAHCIG ITDRDFIEGV HGGTWVSATL EQDKCVTVMA PDKPSLDISL ETVAIDGPAE ARKVCYNAVL THVKINDKCP STGEAHLAEE NEGDNACKRT YSDRGWGNGC GLFGKGSIVA CAKFTCAKSM SLFEVDQTKI QYVIRAQLHV GAKQENWNTD IKTLKFDALS GSQEAEFTGY GKATLECQVQ TAVDFGNSYI AEMEKESWIV DRQWAQDLTL PWQSGSGGVW REMHHLVEFE PPHAATIRVL ALGNQEGSLK TALTGAMRVT KDTNDNNLYK LHGGHVSCRV KLSALTLKGT SYKMCTDKMS FVKNPTDTGH GTVVMQVKVP KGAPCKIPVI VADDLTAAIN KGILVTVNPI ASTNDDEVLI EVNPPFGDSY IIVGTGDSRL TYQWHKEGSS IGKLFTQTMK GAERLAVMGD AAWDFSSAGG FLTSVGKGIH TVFGSAFQGL FGGLSWITKV IMGAVLIWVG INTRNMTMSM SMILVGVIMM FLSLGVGADQ GCAINFGKRE LKCGDGIFIF RDSDDWLNKY SYYPEDPVKL ASIVKASFEE GKCGLNSVDS LEHEMWRSRA DEINAILEEN EVDISVVVQD PKNVYQRGTH PFSRIRDGLQ YGWKTWGKNL VFSPGRKNGS FIIDGKSRKE CPFSNRVWNS FQIEEFGTGV FTTRVYMDAV FEYTIDCDGS ILGAAVNGKK SAHGSPTFWM GSHEVNGTWM IHTLEALDYK ECEWPLTHTI GTSVEESEMF MPRSIGGPVS SHNHIPGYKV QTNGPWMQVP LEVRREACPG TSVIIDGNCD GRGKSTRSTT DSGKIIPEWC CRSCTMPPVS FHGSDGCWYP MEIRPRKTHE SHLVRSWVTA GEIHAVPFGL VSMMIAMEVV LRKRQGPKQM LVGGVVLLGA MLVGQVTLLD LLKLTVAVGL HFHEMNNGGD AMYMALIAAF SIRPGLLIGF GLRTLWSPRE RLVLTLGAAM VEIALGGMMG GLWKYLNAVS LCILTINAVA SRKASNTILP LMALLTPVTM AEVRLAAMLF CTVVIIGVLH QNSKDTSMQK TIPLVALTLT SYLGLTQPFL GLCAFLATRL FGRRSIPVNE ALAAAGLVGV LAGLAFQEME NFLGPIAVGG ILMMLVSVAG RVDGLELRKL GEVSWEEEAE ISGSSARYDV ALSEQGEFKL LSEEKVPWDQ VVMTSLALVG AAIHPFALLL VLAGWLFHVK GARRSGDVLW DIPTPKIIEE CEHLEDGIYG IFQSTFLGAS QRGVGVAQGG VFHTMWHVTR GAFLVRNGKK LIPSWASVKE DLVAYGGSWK LEGRWDGEEE VQLIAAVPGK NVVNVQTKPS LFKVRNGGEI GAVALDYPSG TSGSPIVNRN GEVIGLYGNG ILVGDNSFVS AISQTEVKEE GKEELQEIPT MLKKGMTTIL DFHPGAGKTR RFLPQILAEC ARRRLRTLVL APTRVVLSEM KEAFHGLDVK FHTQAFSAHG SGREVIDAMC HATLTYRMLE PTRIVNWEVI IMDEAHFLDP ASIAARGWAA HRARANESAT ILMTATPPGT SDEFPHSNGE IEDVQTDIPS EPWNTGHDWI LADKRPTAWF LPSIRAANVM AASLRKAGKS VVVLNRKTFE REYPTIKQKK PDFILATDIA EMGANLCVER VLDCRTAFKP VLVDEGRKVA IKGPLRISAS SAAQRRGRIG RNPNRDGDSY YYSEPTSEDN AHHVCWLEAS MLLDNMEVRG GMVAPLYGVE GTKTPVSPGE MRLRDDQRKV FRELVRNCDQ PVWLSWQVAK AGLKTNDRKW CFEGPDEHEI LNDSGETVKC RAPGGAKKPL RPRWCDERVS SDQSALADFI KFAEGRRGAA EVLVVLSELP DFLAKKGGEA MDTISVFLHS EEGSRAYRNA LSMMPEAMTI AMLFILAGLL TSGMVIFFMS PKGISRMSMA MGTMAGCGYL MFLGGVKPTH ISYIMLIFFV LMVVVIPEPG QQRSIQDNQV AYLIIGILTL VSVVAANELG MLEKTKEDLF GKKDLIPSSA SPWSWPDLDL KPGAAWTVYV GIVTMLSPML HHWIKVEYGN LSLSGIAQSA SVLSFMDKGI PFMKMNISVI ILLVSGWNSI TVMPLLCGIG CAMLHWSLIL PGIKAQQSKL AQRRVFHGVA KNPVVDGNPT VDIEEAPEMP ALYEKKLALY LLLALSLASV AMCRTPFSLA EGIVLASAAL GPLIEGNTSL LWNGPMAVSM TGVMRGNYYA FVGVMYNLWK MKTGRRGRAN GKTLGEVWKR ELNLLDKQQF ELYKRTDIVE VDRDTARRHL AEGKVDTGVA VSRGTAKLRW FHERGYVKLE GRVTDLGCGR GGWCYYAAAQ KEVSGVKGFT LGRDGHEKPM NVQSLGWNII TFKDKTDIHR LEPMKCDTLL CDIGESSSSS VTEGERTMRV LDTVEKWLAC GVDNFCVKVL APYMPDVLEK LELLQRRFGG TVIRNPLSRN STHEMYYVSG ARSNVTFTVN QTSRLLMRRM RRPTGKVTLE ADVILPIGTR SVETDKGPLD REAIEERVER IKSEYMTTWF YDNDNPYRTW HYCGSYVTKT SGSAASMVNG VIKILTYPWD RIEEVTRMAM TDTTPFGQQR VFKEKVDTRA KDPPAGTRKI MKVVNRWLFR HLAREKNPRL CTKEEFIAKV RSHAAIGAYL EEQEQWKTAN EAVQDPKFWE LVDEERKLHQ QGRCRTCVYN MMGKREKKLS EFGKAKGSRA IWYMWLGARY LEFEALGFLN EDHWASRENS GGGVEGIGLQ YLGYVIRDLA AMDGGGFYAD DTAGWDTRIT EADLDDEQEI LNYMSPHHKK LAQAVMEMTY KNKVVKVLRP APGGKAYMDV ISRRDQRGSG QVVTYALNTI TNLKVQLIRM AEAEMVIHHQ HVQDCDESAL ARLEAWLTEH GCDRLKRMAV SGDDCVVRPI DDRFGLALSH LNAMSKVRKD ISEWQPSKGW NDWENVPFCS HHFHELHLKD GRRIVVPCRE QDELIGRGRV SPGNGWMIKE TACLSKAYAN MWSLMYFHKR DMRLLSLAVS SAVPTSWVPQ GRTTWSIHGK GEWMTTEDML GVWNRVWITN NPHMQDKTVV KEWRDVPYLT KRQDKLCGSL IGMTNRATWA SHIHLVIHRI RTLIGQEKYT DYLTVMDRYS VDADLQPGEL I //