ID G3FEY0_9FLAV Unreviewed; 3432 AA. AC G3FEY0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 24-JUL-2024, entry version 89. DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107}; OS Japanese encephalitis virus. OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes; OC Amarillovirales; Flaviviridae; Orthoflavivirus; Orthoflavivirus japonicum. OX NCBI_TaxID=11072 {ECO:0000313|EMBL:AEO86792.1, ECO:0000313|Proteomes:UP000129773}; RN [1] {ECO:0000313|EMBL:AEO86792.1, ECO:0000313|Proteomes:UP000129773} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZMT {ECO:0000313|EMBL:AEO86792.1}; RX PubMed=21697481; DOI=10.1128/JVI.00825-11; RA Pan X.L., Liu H., Wang H.Y., Fu S.H., Liu H.Z., Zhang H.L., Li M.H., RA Gao X.Y., Wang J.L., Sun X.H., Lu X.J., Zhai Y.G., Meng W.S., He Y., RA Wang H.Q., Han N., Wei B., Wu Y.G., Feng Y., Yang D.J., Wang L.H., Tang Q., RA Xia G., Kurane I., Rayner S., Liang G.D.; RT "Emergence of genotype I of Japanese encephalitis virus as the dominant RT genotype in Asia."; RL J. Virol. 85:9847-9853(2011). CC -!- FUNCTION: 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 the only viral peptide matured by host CC furin in the trans-Golgi network probably to avoid catastrophic CC activation of the viral fusion activity in acidic Golgi compartment CC prior to virion release. prM-E cleavage is inefficient, and many CC virions are only partially matured. These uncleaved prM would play a CC role in immune evasion. {ECO:0000256|ARBA:ARBA00035620}. CC -!- FUNCTION: Component of the viral RNA replication complex that functions CC in virion assembly and antagonizes the host alpha/beta interferon CC antiviral response. {ECO:0000256|ARBA:ARBA00035615}. CC -!- FUNCTION: Functions as a signal peptide for NS4B and is required for CC the interferon antagonism activity of the latter. CC {ECO:0000256|ARBA:ARBA00003504}. CC -!- FUNCTION: Inhibits RNA silencing by interfering with host Dicer. CC {ECO:0000256|ARBA:ARBA00035616}. CC -!- FUNCTION: Involved in immune evasion, pathogenesis and viral CC replication. Once cleaved off the polyprotein, is targeted to three CC destinations: the viral replication cycle, the plasma membrane and the CC extracellular compartment. Essential for viral replication. Required CC for formation of the replication complex and recruitment of other non- CC structural proteins to the ER-derived membrane structures. Excreted as CC a hexameric lipoparticle that plays a role against host immune CC response. Antagonizing the complement function. Binds to the host CC macrophages and dendritic cells. Inhibits signal transduction CC originating from Toll-like receptor 3 (TLR3). CC {ECO:0000256|ARBA:ARBA00035605}. CC -!- FUNCTION: May play a role in virus budding. Exerts cytotoxic effects by CC activating a mitochondrial apoptotic pathway through M ectodomain. May CC display a viroporin activity. {ECO:0000256|ARBA:ARBA00035609}. CC -!- FUNCTION: Plays a role in virus budding by binding to the cell membrane CC and gathering the viral RNA into a nucleocapsid that forms the core of CC a mature virus particle. During virus entry, may induce genome CC penetration into the host cytoplasm after hemifusion induced by the CC surface proteins. Can migrate to the cell nucleus where it modulates CC host functions. Overcomes the anti-viral effects of host EXOC1 by CC sequestering and degrading the latter through the proteasome CC degradation pathway. {ECO:0000256|ARBA:ARBA00035602}. 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 Evidence={ECO:0000256|ARBA:ARBA00001556}; 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; Evidence={ECO:0000256|ARBA:ARBA00024468}; 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 Evidence={ECO:0000256|ARBA:ARBA00001491}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- SUBUNIT: Forms heterodimers with envelope protein E in the endoplasmic CC reticulum and Golgi. {ECO:0000256|ARBA:ARBA00035667}. CC -!- SUBUNIT: Homodimer (By similarity). Interacts (via N-terminus) with CC host EXOC1 (via C-terminus); this interaction results in EXOC1 CC degradation through the proteasome degradation pathway. CC {ECO:0000256|ARBA:ARBA00035670}. CC -!- SUBUNIT: Homodimer; Homohexamer when secreted (By similarity). CC Interacts with envelope protein E (By similarity). NS1 interacts with CC NS4B (By similarity). Interacts with host complement protein CFH; this CC interaction leads to the degradation of C3. CC {ECO:0000256|ARBA:ARBA00035664}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Endoplasmic CC reticulum membrane {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane CC protein {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004397}. Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004367}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004367}; Lumenal side CC {ECO:0000256|ARBA:ARBA00004367}. Host cytoplasm, host perinuclear CC region {ECO:0000256|ARBA:ARBA00004407}. Host endoplasmic reticulum CC membrane {ECO:0000256|ARBA:ARBA00004153}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004153}. Host endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004461}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004461}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004461}. Host endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00023443}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00023443}; Lumenal side CC {ECO:0000256|ARBA:ARBA00023443}. Host nucleus CC {ECO:0000256|ARBA:ARBA00004147}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. Membrane CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004287}. Secreted CC {ECO:0000256|ARBA:ARBA00004613}. Virion membrane CC {ECO:0000256|ARBA:ARBA00004385}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004385}. 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; JF706283; AEO86792.1; -; Genomic_RNA. DR Proteomes; UP000129773; Genome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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: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:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro. DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:InterPro. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC. 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:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0046718; P:symbiont entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0052170; P:symbiont-mediated suppression of host innate immune response; IEA:UniProtKB-KW. DR GO; GO:0039563; P:symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW. DR GO; GO:0039564; P:symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity; IEA:UniProtKB-KW. DR GO; GO:0039502; P:symbiont-mediated suppression 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 GO; GO:0019049; P:virus-mediated perturbation of host defense response; 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 CDD; cd18806; SF2_C_viral; 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-like. 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; SSF101257; Flavivirus capsid protein C; 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 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Capsid protein {ECO:0000256|ARBA:ARBA00022561}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR003817-3}; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|ARBA:ARBA00022510}; KW Fusion of virus membrane with host membrane KW {ECO:0000256|ARBA:ARBA00022506}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Helicase {ECO:0000256|ARBA:ARBA00022806}; KW Host endoplasmic reticulum {ECO:0000256|ARBA:ARBA00023184}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870}; KW Host nucleus {ECO:0000256|ARBA:ARBA00022562}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Inhibition of host innate immune response by virus KW {ECO:0000256|ARBA:ARBA00022632}; KW Inhibition of host interferon signaling pathway by virus KW {ECO:0000256|ARBA:ARBA00022830}; KW Inhibition of host STAT1 by virus {ECO:0000256|ARBA:ARBA00022961}; KW Inhibition of host STAT2 by virus {ECO:0000256|ARBA:ARBA00022883}; KW Interferon antiviral system evasion {ECO:0000256|ARBA:ARBA00023258}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR003817-4}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603}; KW mRNA capping {ECO:0000256|ARBA:ARBA00023042}; KW mRNA processing {ECO:0000256|ARBA:ARBA00022664}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}; KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804}; KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280}; KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595}; KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}; KW Virion {ECO:0000256|ARBA:ARBA00022844}; KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}; KW Zinc {ECO:0000256|PIRSR:PIRSR003817-4}. FT TRANSMEM 112..130 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 254..273 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 279..298 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 746..767 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 773..794 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1178..1197 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1250..1274 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1280..1304 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1342..1365 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1377..1395 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1477..1497 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2173..2193 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2200..2220 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2226..2244 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2256..2278 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2369..2392 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1374..1504 FT /note="Flavivirus NS2B" FT /evidence="ECO:0000259|PROSITE:PS51527" FT DOMAIN 1505..1682 FT /note="Peptidase S7" FT /evidence="ECO:0000259|PROSITE:PS51528" FT DOMAIN 1685..1841 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 1852..2017 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT DOMAIN 2528..2793 FT /note="MRNA cap 0-1 NS5-type MT" FT /evidence="ECO:0000259|PROSITE:PS51591" FT DOMAIN 3057..3209 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT REGION 1950..1969 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1555 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT ACT_SITE 1579 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT ACT_SITE 1639 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT BINDING 2583 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2613 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2614 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2631 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2632 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2658 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2659 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2747 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2967 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 2971 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 2976 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 2979 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 3244 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 3260 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 3379 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT DISULFID 297..324 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 354..410 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 368..399 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 386..415 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 484..581 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 598..629 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" SQ SEQUENCE 3432 AA; 380151 MW; 6F537678D97E402F CRC64; MTKKPGGPGK NRAINMLKRG LPRVFPLVGV KRVVMSLLDG RGPVRFVLAL ITFFKFTALA PTKTLLGRWK AVEKSVAMKH LTSFKRELGT LIDAVNKRGR KQNKRGGNEG SIMWLASLAV VIACAGAMKL SNFQGKLLMT INNTDIADVI VIPTSKGENR CWVRAIDVGY MCEDTITYEC PKLTMGNDPE DVDCWCDNQE VYVQYGRCTR TRHSKRSRRS VSVQIHGESS LVNKKEAWLD STKATRYLMK TENWIIRNPG YAFLAAVLGW MLGSNNGQRV VFTILLLLVA PAYSFNCLGM GNRDFIEGAS GATWVDLVLE GDSCLTIMAN DKPTLDVRMI NIEASQLAEV RSYCYHASVT DISTVARCPT TGEAHNKKRA DSSYVCKQGF TDRGWGNGCG LFGKGSIDTC AKFSCTSKAI GRTIQPENIK YEVGIFVHGT TTSENHGNYS AQVGASQAAK FTVTPNAPSI TLKLGDYGEV TLDCEPRSGL NTEAFYVMTV GSKSFLVHRE WFHDLALPWT SPSSTAWRNR ELLMEFEEAH ATKQSVVALG SQEGGLHQAL AGAIVVEYSS SVKLTSGHLK CRLKMDKLAL KGTTYGMCTE KFSFAKNPAD TGHGTVVIEL SYSGSDGPCK IPIVSVASLN DMTPVGRLVT VNPFVATSSA NSKVLVEMEP PFGDSYIVVG RGDKQINHHW HKAGSTLGKA FSTTLKGAQR LAALGDTAWD FGSIGGVFNS IGKAVHQVFG GAFRTLFGGM SWITQGLMGA LLLWMGVNAR DRSIALAFLA TGGVLVFLAT NVHADTGCAI DITRKEMRCG SGIFVHNDVE AWVDRYKYLP ETPRSLAKIV HKAHKEGVCG VRSVTRLEHQ MWEAVRDELN VLLKENAVDL SVVVNKPVGR YRSAPKRLSM TQEKFEMGWK AWGKSILFAP ELANSTFVVD GPETKECPDE HRAWNSMQIE DFGFGITSTR VWLKIREEST DECDGAIIGT AVKGHVAVHS DLSYWIESRY NDTWKLERAV FGEVKSCTWP ETHTLWGDGV EESELIIPHT IAGPKSKHNR REGYKTQNQG PWDENGIVLD FDYCPGTKVT ITEDCGKRGP SVRTTTDSGK LITDWCCRSC SLPPLRFRTE NGCWYGMEIR PVRHDETTLV RSQVDAFNGE MVDPFQLGLL VMFLATQEVL RKRWTARLTI PAVLGALLVL MLGGITYTDL ARYVVLVAAA FAEANSGGDV LHLALIAVFK IQPAFLVMNM LSTRWTNQEN VVLVLGAAFF QLASVDLQIG VHGILNAAAI AWMIVRAITF PTTSSVTMPV LALLTPGMRA LYLDTYRIIL LVIGICSLLQ ERKKTMAKKK GAVLLGLALT STGWFSPTTI AAGLMVCNPN KKRGWPATEF LSAVGLMFAI VGGLAELDIE SMSIPFMLAG LMAVSYVVSG KATDMWLERA ADISWEMDAA ITGSSRRLDV KLDDDGDFHL IDDPGVPWKV WVLRMSCIGL AALTPWAIVP AAFGYWLTLK TTKRGGVFWD TPSPKPCSKG DTTTGVYRIM ARGILGTYQA GVGVMYENVF HTLWHTTRGA AIMSGEGKLT PYWGSVKEDR IAYGGPWRFD RKWNGTDDVQ VIVVEPGKAA VNIQTKPGVF RTPFGEVGAV SLDYPRGTSG SPILDSNGDI IGLYGNGVEL GDGSYVSAIV QGDRQEEPVP EAYTPNMLRK RQMTVLDLHP GSGKTRKILP QIIKDAIQQR LRTAVLAPTR VVAAEMAEAL RGLPVRYQTS AVQREHQGNE IVDVMCHATL THRLMSPNRV PNYNLFVMDE AHFTDPASIA ARGYIATKVE LGEAAAIFMT ATPPGTTDPF PDSNAPIHDL QDEIPDRAWS SGYEWITEYA GKTVWFVASV KMGNEIAMCL QRAGKKVIQL NRKSYDTEYP KCKNGDWDFV ITTDISEMGA NFGASRVIDC RKSVKPTILE EGEGRVILGN PSPITSASAA QRRGRVGRNP NQVGDEYHYG GATSEDDSNL AHWTEAKIML DNIHMPNGLV AQLYGPEREK AFTMDGEYRL RGEEKKNFLE LLRTADLPVW LAYKVASNGI QYTDRKWCFD GPRTNAILED NTEVEIVTRM GERKILKPRW LDARVYADHQ ALKWFKDFAA GKRSAVSFIE VLGRMPEHFM GKTREALDTM YLVATAEKGG KAHRMALEEL PDALETITLI VAITVMTGGF FLLMMQRKGI GKMGLGALVL TLATFFLWAA EVPGTKIAGT LLIALLLMVV LIPEPEKQRS QTDNQLAVFL ICVLTVVGVV AANEYGMLEK TKADLKSMFG GKTQASGLTG LPSMALDLRP ATAWALYGGS TVVLTPLLKH LITSEYVTTS LASINSQAGS LFVLPRGVPF TDLDLTVGLV FLGCWGQITL TTFLTAMVLA TLHYGYMLPG WQAEALRAAQ RRTAAGIMKN AVVDGMVATD VPELERTTPL MQKKVGQVLL IGVSVAAFLV NPNVTTVREA GVLVTAATLT LWDNGASAVW NSTTATGLCH VMRGSYLAGG SIAWTLIKNA DKPSLKRGRP GGRTLGEQWK EKLNAMSREE FFKYRREAII EVDRTEARRA RRENNIVGGH PVSRGSAKLR WLVEKGFVSP IGKVIDLGCG RGGWSYYAAT LKKVQEVRGY TKGGAGHEEP MLMQSYGWNL VSLKSGVDVF YKPSEPSDTL FCDIGESSPS PEVEEQRTLR VLEMTSDWLH RGPREFCIKV LCPYMPKVIE KMEVLQRRFG GGLVRLPLSR NSNHEMYWVS GAAGNVVHAV NMTSQVLLGR MDRTVWRGPK YEEDVNLGSG TRAVGKGEVH SNQEKIKKRI QKLKEEFATT WHKDPEHPYR TWTYHGSYEV KATGSASSLV NGVVKLMSKP WDAIANVTTM AMTDTTPFGQ QRVFKEKVDT KAPEPPAGAK EVLNETTNWL WAHLSREKRP RLCTKEEFIK KVNSNAALGA VFAEQNQWST AREAVNDPRF WEMVDEEREN HLRGECHTCI YNMMGKREKK PGEFGKAKGS RAIWFMWLGA RYLEFEALGF LNEDHWLSRE NSGGGVEGSG VQKLGYILRD IAGKQGGKMY ADDTAGWDTR ITRTDLENEA KVLELLDGEH RMLARAIIEL TYRHKVVKVM RPAAEGKTVM DVISREDQRG SGQVVTYALN TFTNIAVQLV RLMEAEGVIG PQHLEQLPRK NKIAVRTWLF ENGEERVTRM AISGDDCVVK PLDDRFATAL HFLNAMSKVR KDIQEWKPSH GWHDWQQVPF CSNHFQEIVM KDGRSIVVPC RGQDELIGRA RISPGAGWNV KDTACLAKAY AQMWLLLYFH RRDLRLMANA ICSAVPVDWV PTGRTSWSIH SKGEWMTTED MLRVWNRVWI EENEWMMDKT PITSWTDVPY VGKREDIWCG SLIGTRSRAT WAENIYAAIN QVRAVIGKEN YVDYMTSLRR YEDVLIQEDR VI //