ID V9IS50_9FLAV Unreviewed; 3390 AA. AC V9IS50; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 27-NOV-2024, entry version 68. DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107}; OS dengue virus type 3. OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes; OC Amarillovirales; Flaviviridae; Orthoflavivirus; Orthoflavivirus denguei; OC Dengue virus. OX NCBI_TaxID=11069 {ECO:0000313|EMBL:AFK83764.1, ECO:0000313|Proteomes:UP000128110}; RN [1] {ECO:0000313|EMBL:AFK83764.1, ECO:0000313|Proteomes:UP000128110} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D3PY/AS10/03 {ECO:0000313|EMBL:AFK83764.1}; RA Alfonso H.L., Amarilla A.A., Goncaves P.F., Barros M.T., Silva E.V.D.A., RA Nunes M., Vasconcelos P.F.C., Vieira D.S., Batista W.C., Bobadilla M.L., RA Vazquez C., Moran M., Figueiredo L.T.M., Aquino V.H.; RT "Molecular characterization of dengue virus type 3 isolated in Brazil and RT Paraguay."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. 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: Regulates the ATPase activity of the NS3 helicase activity. CC NS4A allows NS3 helicase to conserve energy during unwinding. Plays a CC role in the inhibition of the host innate immune response. Interacts CC with host MAVS and thereby prevents the interaction between RIGI and CC MAVS. In turn, IFN-beta production is impaired. Interacts with host CC AUP1 which mediates induction of lipophagy in host cells and CC facilitates production of virus progeny particles. CC {ECO:0000256|ARBA:ARBA00045521}. 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 + phosphate + H(+); 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 + phosphate + H(+); 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. May form CC homooligomers. {ECO:0000256|ARBA:ARBA00046942}. 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. Interacts CC with protein prM. Interacts with non-structural protein 1. CC {ECO:0000256|ARBA:ARBA00047062}. CC -!- SUBUNIT: Interacts (via N-terminus) with serine protease NS3. CC {ECO:0000256|ARBA:ARBA00025871}. CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane CC {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 mitochondrion CC {ECO:0000256|ARBA:ARBA00004181}. Host nucleus CC {ECO:0000256|ARBA:ARBA00004147}. 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; JF808129; AFK83764.1; -; Genomic_RNA. DR Proteomes; UP000128110; 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:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0042025; C:host cell nucleus; 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:0015267; F:channel activity; 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: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:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0039545; P:symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; IEA:UniProtKB-KW. DR GO; GO:0039574; P:symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 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 FunFam; 1.20.1280.260:FF:000001; Envelope glycoprotein; 1. DR FunFam; 2.60.40.350:FF:000001; Envelope glycoprotein; 1. DR FunFam; 1.10.10.930:FF:000001; Genome polyprotein; 1. DR FunFam; 2.60.260.50:FF:000001; Genome polyprotein; 1. DR FunFam; 3.30.70.2840:FF:000001; Genome polyprotein; 1. DR FunFam; 3.30.70.2840:FF:000002; Genome polyprotein; 1. DR FunFam; 3.40.50.150:FF:000105; Genome polyprotein; 1. DR FunFam; 3.40.50.300:FF:000763; Genome polyprotein; 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; 2.40.10.10; Trypsin-like serine proteases; 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; IPR043504; Peptidase_S1_PA_chymotrypsin. 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 Acetylation {ECO:0000256|ARBA:ARBA00022990}; 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 Clathrin-mediated endocytosis of virus by host KW {ECO:0000256|ARBA:ARBA00022570}; KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685}; 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 mitochondrion {ECO:0000256|ARBA:ARBA00023147}; 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 MAVS by virus {ECO:0000256|ARBA:ARBA00022986}; KW Inhibition of host RLR pathway by virus {ECO:0000256|ARBA:ARBA00022482}; KW Inhibition of host STAT2 by virus {ECO:0000256|ARBA:ARBA00022883}; KW Inhibition of host TYK2 by virus {ECO:0000256|ARBA:ARBA00022923}; KW Interferon antiviral system evasion {ECO:0000256|ARBA:ARBA00023258}; KW Ion channel {ECO:0000256|ARBA:ARBA00023303}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065}; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; 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 Transcription {ECO:0000256|ARBA:ARBA00023163}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}; 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}; Transport {ECO:0000256|ARBA:ARBA00022448}; KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804}; KW Viral envelope protein {ECO:0000256|ARBA:ARBA00022879}; KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280}; KW Viral ion channel {ECO:0000256|ARBA:ARBA00023039}; 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 endocytosis by host {ECO:0000256|ARBA:ARBA00022890}; KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}; KW Zinc {ECO:0000256|PIRSR:PIRSR003817-4}. FT TRANSMEM 46..69 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 722..746 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 752..771 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1157..1175 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1195..1218 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2147..2166 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2173..2190 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2196..2213 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2225..2242 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1344..1473 FT /note="Flavivirus NS2B" FT /evidence="ECO:0000259|PROSITE:PS51527" FT DOMAIN 1474..1651 FT /note="Peptidase S7" FT /evidence="ECO:0000259|PROSITE:PS51528" FT DOMAIN 1654..1810 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 1820..1986 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT DOMAIN 2492..2753 FT /note="MRNA cap 0-1 NS5-type MT" FT /evidence="ECO:0000259|PROSITE:PS51591" FT DOMAIN 3017..3167 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT ACT_SITE 1524 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT ACT_SITE 1548 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT ACT_SITE 1608 FT /note="Charge relay system; for serine protease NS3 FT activity" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1" FT BINDING 2546 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2576 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2577 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2594 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2595 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2621 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2622 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2708 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2" FT BINDING 2927 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 2931 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 2936 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 2939 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 3202 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 3218 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT BINDING 3337 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4" FT DISULFID 283..310 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 340..396 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 354..385 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 372..401 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 463..563 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" FT DISULFID 580..611 FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3" SQ SEQUENCE 3390 AA; 377814 MW; 594D3241159AD3DB CRC64; MNNQRKKTGK PSINMLKRVR NRVSTGSQLA KRFSKGLLNG QGPMKLVMAF IAFLRFLAIP PTAGVLARWG TFKKSGAIKV LKGFKKEISN MLSIINKRKK TSLCLMMILP AALAFHLTSR DGEPRMIVGK NERGKSLLFK TASGINMCTL IAMDLGEMCD DTVTYKCPHI TEVEPEDIDC WCNLTSTWVT YGTCNQAGEH RRDKRSVALA PHVGMGLDTR TQTWMSAEGA WRQVEKVETW ALRHPGFTIL ALFLAHYIGT SLTQKVVIFI LLMLVTPSMT MRCVGVGNRD FVEGLSGATW VDVVLEHGGC VTTMAKNKPT LDIELQKTEA TQLATLRKLC IEGKITNITT DSRCPTQGEA VLPEEQDQNY VCKHTYVDRG WGNGCGLFGK GSLVTCAKFQ CLEPIEGKVV QYENLKYTVI ITVHTGDQHQ VGNETQGVTA EITPQASTTE AILPEYGTLG LECSPRTGLD FNEMILLTMK NKAWMVHRQW FFDLPLPWTS GATTETPTWN RKELLVTFKN AHAKKQEVVV LGSQEGAMHT ALTGATEIQN SGGTSIFAGH LKCRLKMDKL ELKGMSYAMC TNTFVLKKEV SETQHGTILI KVEYKGEDAP CKIPFSTEDG QGKAHNGRLI TANPVVTKKE EPVNIEAEPP FGESNIVIGI GDNALKINWY KKGSSIGKMF EATARGARRM AILGDTAWDF GSVGGVLNSL GKMVHQIFGS AYTALFSGVS WVMKIGIGVL LTWIGLNSKN TSMSFSCIAI GIITLYLGAV VQADMGCVIN WKGKELKCGS GIFVTNEVHT WTEQYKFQAD SPKRLATAIA GAWENGVCGI RSTTRMENLL WKQIANELNY ILWENNIKLT VVVGDITGVL EQGKRTLTPQ PMELKYSWKT WGKAKIVTAE TQNSSFIIDG PNTPECPSAS RAWNVWEVED YGFGVFTTNI WLKLREVYTQ LCDHRLMSAA VKDERAVHAD MGYWIESQKN GSWKLEKASL IEVKTCTWPK SHTLWSNGVL ESDMIIPKSL AGPISQHNHR PGYHTQTAGP WHLGKLELDF NYCEGTTVVI TENCGTRGPS LRTTTVSGKL IHEWCCRSCT LPPLRYMGED GCWYGMEIRP ISEKEENMVK SLVSAGSGKV DNCTMGVLCL AILFEDVMRG KFGKKHMIAG VFFTFVLLLS GQITWRDMAH TLIMIGSNAS DRMGMGVTYL ALIATFKIQP FLALGFFLRK LTSRENLLLG VGLAMATTLQ LPEDIEQMAN GIALGLMALK LITQFETYQL WTALISLTCS NTMFTLTVAW RTATLILAGV SLLPVCQSSS MRKTDWLPMA VAAMGVPPLP LFIFSLKDTL KRRSWPLNEG VMAVGLVSIL ASSLLRNDVP MAGPLVAGGL LIACYVITGT SADLTVEKAA DITWEEEAEQ TGVSHNLMTT VDDDGTMRIK DDETENILTV LLKTALTIVS GVFPYSIPAT LLVWHTWQKQ TQRSGVLWDV PSPPETQKAE QEEGVYRIKQ QGIFGKTQVG VGVQKEGVFH TMWHVTRGAV LTYNGKRLEP NWASVKKDLI SYGGGWRLSA QWQKGEEVQV IAVEPGKNPK NFQTMPGTFQ TTTGEIGAIA LDFKPGTSGS PIINREGKVV GLYGNGVVTK NGGYVSGIAQ TNAEPDGPTP ELEEEMFKKR NLTIMDLHPG SGKTRKYLPA IVREAIKRRL RTLILAPTRV VAAEMEEALK GLPIRYQTTA TKSEHTGREI VDLMCHATFT MRLLSPVRVP TYNLIIMDEA HFTDPASIAA RGYISTRVGM GEAAAIFMTA TPPGTADAFP QSNAPIQDEE RDIPERSWNS GNEWITDFAG KTVWFVPSIK AGNDIANCLR KNGKKVIQLS RKTFDTEYQK TKLNDWDFVV TTDISEMGAN FKADRVIDPR RCLKPVILTD GPERVILAGP MPVTAASAAQ RRGRVGRNPQ KENDQYIFTG QPLNNDEDHA HWTEAKMLLD NINTPEGIIP ALFEPEREKS AAIDGEYRLK GESRKTFVEL MRRGDLPVWL AHKVASEGIK YTDRKWCFDG QRNNQILEEN MDVEIWTKEG EKKKLRPRWL DARTYSDPLA LKEFKDFAAG RKSIALDLVT EIGRVPSHLA HRTRNALDNL VMLHTSEHGG RAYRHAVEEL PETMETLLLL GLMILLTGGA MLFLISGKGI GKTSIGLICV IASSGMLWMA EIPLQWIASA IVLEFFMMVL LIPEPEKQRT PQDNQLAYVV IGILTLAAII AANEMGLLET TKRDLGMSKE PGVVSPTSYL DVDLHPASAW TLYAVATTVI TPMLRHTIEN STANVSLAAI ANQAVVLMGL DKGWPISKMD LGVPLLALGC YSQVNPLTLT AAVLLLITHY AIIGPGLQAK ATREAQKRTA AGIMKNPTVD GIMTIDLDPV IYDSKFEKQL GQVMLLVLCA VQLLLMRTSW ALCEALTLAT GPITTLWEGS PGKFWNTTIA VSMANIFRGS YLAGAGLAFS IMKSVGTGKR GTGSQGETLG EKWKKKLNQL SRKEFDLYKK SGITEVDRTE AKEGLKRGEI THHAVSRGSA KLQWFVERNM VIPEGRVIDL GCGRGGWSYY CAGLKKVTEV RGYTKGGPGH EEPVPMSTYG WNIVKLMSGK DVFYLPPEKC DTLLCDIGES SPSPTVEESR TIRVLKMVEP WLKNNQFCIK VLNPYMPTVI EHLERLQRKH GGMLVRNPLS RNSTHEMYWI SNGTGNIVAS VNMVSRLLLN RFTMTHRRPT IEKDVDLGAG TRHVNAEPET PNMDVIGERI KRTKEEHNST WHYDDENPYK TWAYHGSYEV KATGSASSMI NGVVKLLTKP WDVVPMVTQM AMTDTTPFGQ QRVFKEKVDT RTPRSMPGTR RVMGITAEWL WRTLGRNKKP RLCTREEFTK KVRTNAAMGA VFTEENQWDS AKAAVEDEDF WKLVDREREL HKLGKCGSCV YNMMGKREKK LGEFGKAKGS RAIWYMWLGA RYLEFEALGF LNEDHWFSRE NSYSGVEGEG LHKLGYILRD ISKIPGGAMY ADDTAGWDTR ITEDDLHNEE KITQQMDPEH RQLANAIFKL TYQNKVVKVQ RPTPTGTVMD IISRKDQRGS GQVGTYGLNT FTNMEAQLIR QMEGEGVLSK ADLENPHLPE KKITQWLETK GVERLKRMAI SGDDCVVKPI DDRFANALLA LNDMGKVRKD IPQWQPSKGW HDWQQVPFCS HHFHELIMKD GRKLVVPCRP QDELIGRARI SQGAGWSLRE TACLGKAYAQ MWSLMYFHRR DLRLASNAIC SAVPVHWVPT SRTTWSIHAH HQWMTTEDML TVWNRVWIED NPWMEDKTPV TTWENVPYLG KREDQWCGSL IGLTSRATWA QNIPTAIQQV RSLIGNEEFL DYMPSMKRFR KEEESEGAIW //