ID W8NKY8_9FLAV Unreviewed; 3390 AA.
AC W8NKY8;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
GN Name=POLY {ECO:0000313|EMBL:QDG00748.1};
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:AHL17466.1, ECO:0000313|Proteomes:UP000142644};
RN [1] {ECO:0000313|EMBL:AHL17466.1, ECO:0000313|Proteomes:UP000142644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13GDZDVS30C {ECO:0000313|EMBL:AHL17466.1};
RA Shi W., Wu Y., Xie Y.;
RT "Molecular epidemiology of Dengue virus 3 epidemic in Zhongshan City in
RT 2013.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QDG00748.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=D13054 {ECO:0000313|EMBL:QDG00748.1};
RA Wu D., Zhang X., Zhang H., Tan Q., Liang M., Sun L., Liu D., Sun B.;
RL Submitted (JUN-2019) 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 -!- 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: Interacts (via N-terminus) with serine protease NS3.
CC {ECO:0000256|ARBA:ARBA00025871}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC {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 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}. 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}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}. 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}.
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DR EMBL; KF954947; AHL17466.1; -; Genomic_RNA.
DR EMBL; MN018386; QDG00748.1; -; Genomic_RNA.
DR Proteomes; UP000142644; 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:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005216; F:monoatomic ion channel activity; 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:0039574; P:disruption by virus of host JAK-STAT cascade via inhibition of host TYK2 activity; IEA:UniProtKB-KW.
DR GO; GO:0039564; P:disruption by virus of host JAK-STAT cascade via inhibition of STAT2 activity; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; 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:0039545; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; 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:0039707; P:virus-mediated pore formation in host cell membrane; 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; 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.
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 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:ARBA00022883};
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 247..272
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 1316..1334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1437..1464
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; 378062 MW; C365BE64A7BB139B 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 VGNETQGITA 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 SPKRLATAIV GAWENGVCGI RSTTRMENLL
WKQIANELNY ILWENNIKLT VVVGDTIGVL EQGKRTLTPQ PMELKYSWKT WGKAKIVTAE
TQNSSFIIDG PNTPECPSAS RAWNVWEVED YGFGVFTTNI WLKLREVYTQ MCDHRLMSAA
VKDERAVHAD MGYWIESQKN GSWKLEKASL IEVKTCTWPK SHTLWSNGVL ESDMIIPKSL
AGPISQHNYR PGYHTQTAGP WHLGKLELDF NYCEGTTVVI TENCGTRGPS LRTTTVSGKL
IHEWCCRSCT LPPLRYMGED GCWYGMEIRP ISEKEENMVK SLVSAGSGKV DNFTMGVLCL
AILFEEVMRG KFGKKHMIAG VFFTFVLLLS GQITWRDMAH TLIMIGSNAS DRMGMGVTYL
ALIATFKIQP FLALGFFLRK LTSRENLLLG VGLAMATTLQ LPEDIEQMAN GIALGLMALK
LITQFETYQL WTALISLTCS NTIFTLTVAW RTATLILAGV SLLPVCQSSS MRKTDWLPMT
VAAMGVPPLP LFIFSLKDTL KRRSWPLNEG VMAVGLVSML ASSLLRNDVP MAGPLVAGGL
LIACYVITGT SADLTVEKAA DVTWEEEAEQ TGVSHNLMIT VDDDGTMRIK DDETENILTV
LLKTALLIVS GIFPYSIPAT LLVWHTWQKQ TQRSGVLWDV PSPPETQKAE LEEGVYRIKQ
QGILGKTQVG VGVQKDGVFH TMWHVTRGAV LTHNGKRLEP NWASVKKDLI SYGGGWRLSA
QWQKGEEVQV IAVEPGKNPK NFQTMPGTFQ TTTGEIGAIA LDFKPGTSGS PIINREGKVV
GLYGNGVVTK NGGYVSGIAQ TNAEPDGPTP ELEEEMFKKR NLTIMDLHPG SGKTRKYLPA
IVREAIKRRL RTLILAPTRV VAAEMEEALK GLPIRYQTTA TKSEHTGREI VDLMCHATFT
MRLLSPVRVP NYNLIIMDEA 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 IGILTMAAII AANEMGLLET TKRDLGMSKE PGVVSPTSYL DVDLHPASAW
TLYAVATTVI TPMLRHTIEN STANVSLAAI ANQAVVLMGL DKGWPISKMD LGVPLLALGC
YSQVNPLTLT AAVLLLVTHY AIIGPGLQAK ATREAQKRTA AGIMKNPTVD GIITIDLDPV
IYDSKFEKQL GQVMLLVLCA VQLLLMRTSW ALCEALTLAT GPITTLWEGS PGKFWNTTIA
VSMANIFRGS YLAGAGLAFS IMKSVGTGKR GTGSQGETLG EKWKKKLNQL SRKEFDLYKK
SGITEVDRTE AKEGLKRGET THHAVSRGSA KLQWFVERNM VIPEGRVIDL GCGRGGWSYY
CAGLKKVTEV RGYTKGGPGH EEPVPMSTYG WNIVKLMSGK DVFYLPPEKC DTLLCDIGES
SPSPTVEESR TIRVLKMVEP WLKNNQFCIK VLNPYMPAVI EHLERLQRKH GGMLVRNPLS
RNSTHEMYWI SNGTGNIVSS VNMVSRLLLN RFTMTHRRPT IEKDVDLGAG TRHVNAEPET
PNMDVIGERI KRIKEEHNST WHYDDENPYK TWAYHGSYEV KATGSASSMI NGVVKLLTKP
WDVVPMVTQM AMTDTTPFGQ QRVFKEKVDT RTPRPMPGTR KVMEITAEWL WRTLGRNKRP
RLCTREEFTK KVRTNAAMGA VFTEENQWDS AKAAVEDEEF WKLVDREREL HKLGKCGSCV
YNMMGKREKK LGEFGKAKGS RAIWYMWLGA RYLEFEALGF LNEDHWFSRE NSYSGVEGEG
LHKLGYILRD ISKIPGGAMY ADDTAGWDTR ITEDDLHNEE KITQRMDPEH RLLANAIFKL
TYQNKVVKVQ RPTPTGTVMD IISRKDQRGS GQVGTYGLNT FTNMEAQLVR QMEGEGVLSK
TDLENPHLPE KKITQWLETK GVERLKRMAI SGDDCVVKPI DDRFANALLA LNDMGKVRKD
IPQWQPSKGW HDWQQVPFCS HHFHELIMKD GRKLVVPCRP QDELIGRARI SQGAGWSLRE
TACLGKAYAQ MWSLMYFHRR DLRLASNAIC SAIPVHWVPT SRTTWSIHAH HQWMTTEDML
TVWNRVWIED NPWMEDKTPI TTWENVPYLG KREDQWCGSL IGLTSRATWA QNIPTAIQQV
RSLIGNEEFL DYMPSMKRFR KEEESEGAIW
//
