ID A0A1U8ZS77_9FLAV Unreviewed; 3411 AA. AC A0A1U8ZS77; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 08-NOV-2023, entry version 39. DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107}; GN ORFNames=AVI39_00001 {ECO:0000313|EMBL:AMZ00439.1}; OS Yellow fever virus. OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes; OC Amarillovirales; Flaviviridae; Orthoflavivirus; Orthoflavivirus flavi. OX NCBI_TaxID=11089 {ECO:0000313|EMBL:AMZ00439.1}; RN [1] {ECO:0000313|EMBL:AMZ00439.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ogbomosho {ECO:0000313|EMBL:AMZ00439.1}; RG Consortium for Microbial Forensics and Genomics (microFORGE); RA Rossi S.L., Guerbois M., Forrester N.L., Ksiazek T., Lin D., Hari K., RA Weaver S.C.; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. 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: Binds to host cell surface receptor and mediates fusion CC between viral and cellular membranes. Envelope protein is synthesized CC in the endoplasmic reticulum in the form of heterodimer with protein CC prM. They play a role in virion budding in the ER, and the newly formed CC immature particle is covered with 60 spikes composed of heterodimer CC between precursor prM and envelope protein E. The virion is transported CC to the Golgi 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:0000256|ARBA:ARBA00035623}. CC -!- FUNCTION: Component of the viral RNA replication complex that functions CC in virion assembly and antagonizes the host immune response. CC {ECO:0000256|ARBA:ARBA00024317}. 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. {ECO:0000256|ARBA:ARBA00035621}. CC -!- FUNCTION: Prevents premature fusion activity of envelope proteins in CC trans-Golgi by binding to envelope protein E at pH6.0. After virion CC release in extracellular space, gets dissociated from E dimers. CC {ECO:0000256|ARBA:ARBA00035626}. CC -!- FUNCTION: Regulates the ATPase activity of the NS3 helicase activity. CC NS4A allows NS3 helicase to conserve energy during unwinding. CC {ECO:0000256|ARBA:ARBA00035613}. CC -!- FUNCTION: Required cofactor for the serine protease function of NS3. CC May have membrane-destabilizing activity and form viroporins. CC {ECO:0000256|ARBA:ARBA00035601}. 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 -!- SUBUNIT: Forms a heterodimer with serine protease NS3 (By similarity). CC May form homooligomers. {ECO:0000256|ARBA:ARBA00035665}. CC -!- SUBUNIT: Forms heterodimers with envelope protein E in the endoplasmic CC reticulum and Golgi. {ECO:0000256|ARBA:ARBA00035667}. CC -!- SUBUNIT: Homodimer; in the endoplasmic reticulum and Golgi (By CC similarity). Interacts with protein prM (By similarity). Interacts with CC non-structural protein 1. {ECO:0000256|ARBA:ARBA00035666}. CC -!- SUBUNIT: Interacts with serine protease NS3. CC {ECO:0000256|ARBA:ARBA00035663}. 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}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. 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; KU978763; AMZ00439.1; -; Genomic_RNA. 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:0016020; C:membrane; IEA:UniProtKB-SubCell. 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:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro. DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-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: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: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:0046718; P:viral entry into host cell; 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; 1.10.260.90; -; 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; 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; 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; 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; 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 4: Predicted; KW Activation of host autophagy by virus {ECO:0000256|ARBA:ARBA00023050}; 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 GTP-binding {ECO:0000256|ARBA:ARBA00023134}; KW Helicase {ECO:0000256|ARBA:ARBA00022806}; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200}; 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 STAT2 by virus {ECO:0000256|ARBA:ARBA00022883}; 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 Suppressor of RNA silencing {ECO:0000256|ARBA:ARBA00022463}; 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}; Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}; 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|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR003817-4}. FT TRANSMEM 44..62 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 105..125 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 245..264 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 271..287 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 730..751 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 758..778 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1133..1151 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1160..1181 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1201..1220 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1232..1249 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1293..1310 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1322..1346 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1358..1376 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1382..1400 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1451..1477 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2157..2180 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2187..2204 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2210..2227 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2239..2256 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2293..2314 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1355..1484 FT /note="Flavivirus NS2B" FT /evidence="ECO:0000259|PROSITE:PS51527" FT DOMAIN 1485..1665 FT /note="Peptidase S7" FT /evidence="ECO:0000259|PROSITE:PS51528" FT DOMAIN 1669..1825 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 1820..1997 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT DOMAIN 2507..2771 FT /note="MRNA cap 0-1 NS5-type MT" FT /evidence="ECO:0000259|PROSITE:PS51591" FT DOMAIN 3035..3187 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT REGION 1942..1961 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1537 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT ACT_SITE 1561 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT ACT_SITE 1622 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT BINDING 2945 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 2949 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 2954 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 2957 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 3222 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 3238 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 3357 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT DISULFID 288..315 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 345..401 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 359..390 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 377..406 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 467..568 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 585..615 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" SQ SEQUENCE 3411 AA; 379326 MW; BE7F4059402A7DA3 CRC64; MSGRKAQGKT LGVNMVRRGV RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF FLFNILTGKK ITAHLKRLWK MLDPRQGLAV LRKVKRVVAG LMRGLSSRKR RSHDVLTVQF LILGMLLMAG GVTLVRKNRW LLLNVTSEDL GKTFSVGTGN CTTNILEAKY WCPDSMEYNC PNLSPREEPD DIDCWCYGVE NVRVAYGKCD SAGRSRRSRR AIDLPTHENH GLKTRQEKWM TGRMGERQLQ KIERWLVRNP FFAVTALAIA 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 TALTGATRVT KDTNDNNLYK LHGGHVSCRV KLSALTLKGT SYKMCTDKMS FVKNPTDTGH GTVVMQVKVP KGAPCKIPVI VADDLTAAIN KGILVTVNPI ASTNDDEVLI EVNPPFGDSY IIVGTGDSRL TYQWHKEGSS IGKLFTQTMK GAERLAVMGD AAWDFSSAGG FFTSIGKGIH 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 IHTLETLDYK ECEWPLTHTI GTSVEESDMF MPRSIGGPVS SHNHIPGYKV QTNGPWMQVP LEVKREACPG TSVIIDGNCD GRGKSTRSTT DSGKIIPEWC CRSCTMPPVS FHGNDGCWYP MEIRPRKTHE SHLVRSWVTA GEIHAVPFGL VSMMIAMEVV LRKRQGPKQM LVGGMVLLGA MLVGQVTLLD LLKLTMAVGL HFHEMNNGGD AMYMALIAAF SIRPGLLIGF GLRTLWSPRE RLVLTLGAAM VEIALGGMMG GLWKYLNAVS LCILTINAVA SRRASNIILP LMALLTPVTM AEVRLATMLF CTVVIIGVLH QNSKDTSMQK TIPLVALTLT SYLGLTQPFL GLCAFLATRI FGRRSIPVNE ALAAAGLVGV LAGLAFQEME NFLGPIAVGG ILMMLVSVAG RVDGLELKKL GEVSWEEEAE ISGSSARYDV TLSEQGEFKL 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 KEYPTIKQKK PDFILATDIA EMGANLCVER VLDCRTAFKP VLVDEGRKVA IKGPLRISAS SAAQRRGRIG RNPNRDGDSY YYSEPTSEDN AHHVCWLEAS MLLDNMEVRG GMVAPLYGIE GTKTPVSPGE MRLRDDQRRV FRELVRNCDL PVWLSWQVAK AGLKTNDRKW CFEGPEEHEI LNDSGETVKC RAPGGAKRPL RPRWCDERVS SDQSALADFI KFAEGRRGAA EVLVVLSELP DFLAKKGGEA MDTISVFLHS EEGSRAYRNA LSMMPEAMTI VMLFILAGLL TSGMVIFFMS PKGISRMSMA MGTMAGCGYL MFLGGVKPTH ISYIMLIFFV LMVVVIPEPG QQRSIQDNQV AYLIIGILTL VSVVAANELG MLERTKEDLF GKKNLISSSA SPWSWPDLDL KPGAAWTVYV GIVTMLSPML HHWIKVEYGN LSLSGIAQSA SVLSFMDKGI PFMKMNISVI ILLVSGWNSI TVMPLLCGIG CAMLHWTLIL PGIKAQQSKL AQRRVFHGVA KNPVVDGNPT VDIEEAPEMP ALYEKKLALY LLLALSLASV AMCRTPFSLA EGIVLVSAAL GPLIEGNTSL LWNGPMAVSM TGVMRGNYYA FVGVMYNLWK MKTGRRGSAN GKTLGEVWKR ELNLLDKQQF ELYKRTDIVE VDRDTARRHL AEGKVDTGVA VSRGTAKLRW FHERGYVKLE GRVTDLGCGR GGWCYYAAAQ KEVSGVKGFT LGREGHEKPM NVQSLGWNII TFKDKTDIHR LEPVKCDTLL CDIGESSSSS VTEGERTMRV LDTVERWLAC GVDNFCVKVL APYMPDVLEK LELLQRRFGG TVIRNPLSRN STHEMYYVSG ARSNVTFTVN QTSRLLMRRM RRPTGKVTLE ADVILPIGTR SVETDKGPLN 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 AEAEMVIHHH HVQDCDDSTL ARLEAWLIEH GCDRLNRMAV SGDDCVVRPI DDRFGMALSH LNAMSKVRKD ISEWQPSKGW NDWENVPFCS HHFHELQLKD GRRIVVPCRE QDELIGRGRV SPGNGWMIKE TACLSKAYAN MWSLMYFHKR DMRLLSLAVS SAVPTSWVPQ GRTTWSIHGK GEWMTTEDML EVWNRVWITN NPHMQDKTVV KEWRDVPYLT KRQDKLCGSL IGMTNRATWA SHIHLVIHRI RTLIGQEKYT DYLTVMDRYS VDADLQPGEL I //