ID E2J049_WNV Unreviewed; 3433 AA.
AC E2J049;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Precursor;
GN Name=GP1 {ECO:0000313|EMBL:ANW69046.1};
GN ORFNames=MZ11_62992gpGP1 {ECO:0000313|EMBL:ANW69046.1};
OS West Nile virus (WNV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Orthoflavivirus; Orthoflavivirus nilense.
OX NCBI_TaxID=11082 {ECO:0000313|EMBL:ADK62514.1, ECO:0000313|Proteomes:UP000143326};
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=8495; Alligator.
OH NCBI_TaxID=34610; Amblyomma variegatum (Tropical bont tick).
OH NCBI_TaxID=8782; Aves (birds).
OH NCBI_TaxID=53527; Culex.
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=34627; Hyalomma marginatum.
OH NCBI_TaxID=308735; Mansonia uniformis.
OH NCBI_TaxID=308737; Mimomyia.
OH NCBI_TaxID=9940; Ovis aries (Sheep).
OH NCBI_TaxID=34630; Rhipicephalus.
OH NCBI_TaxID=34861; Sciurus niger (Eastern fox squirrel).
RN [1] {ECO:0000313|EMBL:ADK62514.1, ECO:0000313|Proteomes:UP000143326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WNV-1/US/BID-V4095/2007 {ECO:0000313|EMBL:ADK62514.1};
RG Broad Institute Genome Sequencing Platform;
RG NYS West Nile Virus Surveillance Team;
RA Henn M.R., Newman R.M., Young D., Ciota A., Levin J., Malboeuf C.,
RA Casali M., Russ C., Lennon N., Erlich R., Anderson S., Rizzolo K.,
RA Green L., Ryan E., Yu Q., Young S., Berlin A., Heiman D., Sykes S.,
RA Koehrsen M., Borenstein D., Engels R., Freedman E., Gellesch M.,
RA Heilman E., Howarth C., Jen D., Larson L., Neiman D., Park D., Pearson M.,
RA Roberts A., Sisk P., Stolte C., White J., Alvarado L., Godfrey P.,
RA Shenoy N., Yandava C., Zeng Q., Kramer L., Nusbaum C., Birren B.;
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANW69046.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WNV-1/Corvus brachyrhynchos/USA/07VER01268/2007
RC {ECO:0000313|EMBL:ANW69046.1};
RA Shabman R., Das S.R., Halpin R.A., Shilts M., Fedorova N., Puri V.,
RA Amedeo P., Shrivastava S., Maffei J., Dupuis A., Jones S., Backenson B.,
RA Zink S., Ciota A., Kramer L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 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}.
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DR EMBL; HM756678; ADK62514.1; -; Genomic_RNA.
DR EMBL; KX547371; ANW69046.1; -; Genomic_RNA.
DR Proteomes; UP000143326; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO: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: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: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; 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.
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 STAT2 by virus {ECO:0000256|ARBA:ARBA00022883};
KW Interferon antiviral system evasion {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 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 44..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 743..764
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1179..1197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1217..1238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1245..1261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1281..1305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1312..1330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1342..1366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1378..1396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1402..1420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1472..1498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2174..2195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2204..2222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2228..2245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2257..2279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2312..2329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2350..2373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2379..2398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2446..2465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1375..1506
FT /note="Flavivirus NS2B"
FT /evidence="ECO:0000259|PROSITE:PS51527"
FT DOMAIN 1506..1683
FT /note="Peptidase S7"
FT /evidence="ECO:0000259|PROSITE:PS51528"
FT DOMAIN 1686..1842
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1853..2018
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2529..2794
FT /note="MRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000259|PROSITE:PS51591"
FT DOMAIN 3058..3210
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT ACT_SITE 1556
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT ACT_SITE 1580
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT ACT_SITE 1640
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT BINDING 2584
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 2615
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 2633
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 2660
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2748
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2968
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 2972
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 2977
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 2980
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 3245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 3261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 3380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT DISULFID 293..320
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 350..406
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 364..395
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 382..411
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 480..578
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 595..626
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
SQ SEQUENCE 3433 AA; 381150 MW; EF1F7A860AC41996 CRC64;
MSKKPGGPGK SRAVNMLKRG MPRVLSLIGL KRAMLSLIDG KGPIRFVLAL LAFFRFTAIA
PTRAVLDRWR GVNKQTAMKH LLSFKKELGT LTSAINRRSS KQKKRGGKTG IAVMIGLIAS
VGAVTLSNFQ GKVMMTVNAT DVTDFITIPT AAGKNLCIVR AMDVGYMCDD TITYECPVLS
AGNDPEDIDC WCTKSAVYVR YGRCTKTRHS RRSRRSLTVQ THGESTLANK KGAWMDSTKA
TRYLVKTESW ILRNPGYALV AAVIGWMLGS NTMQRVVLVV LLLLVAPAYS FNCLGMSNRD
FLEGVSGATW VDLVLEGDSC VTIMSKDKPT IDVKMMNMEA ANLAEVRSYC YLATVSDLST
KAACPTMGEA HNDKRADPAF VCRQGVVDRG WGNGCGLFGK GSIDTCAKFA CSTKAIGRTI
LKENIKYEVA IFVHGPTTVE SHGNYSTQAG ATQAGRFSIT PAAPSYTLKL GEYGEVTVDC
EPRSGIDTNA YYVMTVGTKT FLVHREWFMD LNLPWSSAGS TVWRNRETLM EFEEPHATKQ
SVIALGSQEG ALHQALAGAI PVEFSSNTVK LTSGHLKCRV KMEKLQLKGT TYGVCSKAFK
FLGTPADTGH GTVVLELQYT GTDGPCKVPI SSVASLNDLT PVGRLVTVNP FVSVATANAK
VLIELEPPFG DSYIVVGRGE QQINHHWHKS GSSIGKAFTT TLKGAQRLAA LGDTAWDFGS
VGGVFTSVGK AVHQVFGGAF RSLFGGMSWI TQGLLGALLL WMGINARDRS IALTFLAVGG
VLLFLSVNVH ADTGCAIDIS RQELRCGSGV FIHNDVEAWM DRYKYYPETP QGLAKIIQKA
HKEGVCGLRS VSRLEHQMWE AVKDELNTLL KENGVDLSVV VEKQEGMYKS APKRLTATTE
KLEIGWKAWG KSILFAPELA NNTFVVDGPE TKECPTQNRA WNSLEVEDFG FGLTSTRMFL
KVRESNTTEC DSKIIGTAVK NNLAIHSDLS YWIESRLNDT WKLERAVLGE VKSCTWPETH
TLWGDGILES DLIIPVTLAG PRSNHNRRPG YKTQNQGPWD EGRVEIDFDY CPGTTVTLSE
SCGHRGPATR TTTESGKLIT DWCCRSCTLP PLRYQTDSGC WYGMEIRPQR HDEKTLVQSQ
VNAYNADMID PFQLGLLVVF LATQEVLRKR WTAKISMPAI LIALLVLVFG GITYTDVLRY
VILVGAAFAE SNSGGDVVHL ALMATFKIQP VFMVASFLKA RWTNQENILL MLAAVFFQMA
YHDARQILLW EIPDVLNSLA VAWMILRAIT FTTTSNVVVP LLALLTPGLR CLNLDVYRIL
LLMVGIGSLI REKRSAAAKK KGASLLCLAL ASTGLFNPMI LAAGLIACDP NRKRGWPATE
VMTAVGLMFA IVGGLAELDI DSMAIPMTIA GLMFAAFVIS GKSTDMWIER TADISWESDA
EITGSSERVD VRLDDDGNFQ LMNDPGAPWK IWMLRMVCLA ISAYTPWAIL PSVVGFWITL
QYTKRGGVLW DTPSPKEYKK GDTTTGVYRI MTRGLLGSYQ AGAGVMVEGV FHTLWHTTKG
AALMSGEGRL DPYWGSVKED RLCYGGPWKL QHKWNGQDEV QMIVVEPGKN VKNVQTKPGV
FKTPEGEIGA VTLDFPTGTS GSPIVDKNGD VIGLYGNGVI MPNGSYISAI VQGERMDEPI
PAGFEPEMLR KKQITVLDLH PGAGKTRRIL PQIIKEAINR RLRTAVLAPT RVVAAEMAEA
LRGLPIRYQT SAVPREHNGN EIVDVMCHAT LTHRLMSPHR VPNYNLFVMD EAHFTDPASI
AARGYISTKV ELGEAAAIFM TATPPGTSDP FPESNSPISD LQTEIPDRAW NSGYEWITEY
TGKTVWFVPS VKMGNEIALC LQRAGKKVVQ LNRKSYETEY PKCKNDDWDF VITTDISEMG
ANFKASRVID SRKSVKPTII TEGEGRVILG EPSAVTAASA AQRRGRIGRN PSQVGDEYCY
GGHTNEDDSN FAHWTEARIM LDNINMPNGL IAQFYQPERE KVYTMDGEYR LRGEERKNFL
ELLRTADLPV WLAYKVAAAG VSYHDRRWCF DGPRTNTILE DNNEVEVITK LGERKILRPR
WIDARVYSDH QALKAFKDFA SGKRSQIGLI EVLGKMPEHF MGKTWEALDT MYVVATAEKG
GRAHRMALEE LPDALQTIAL IALLSVMTMG VFFLLMQRKG IGKIGLGGAV LGVATFFCWM
AEVPGTKIAG MLLLSLLLMI VLIPEPEKQR SQTDNQLAVF LICVMTLVSA VAANEMGWLD
KTKSDISSLF GQRIEVKENF SMGEFLLDLR PATAWSLYAV TTAVLTPLLK HLITSDYINT
SLTSINVQAS ALFTLARGFP FVDVGVSALL LAAGCWGQVT LTVTVTAATL LFCHYAYMVP
GWQAEAMRSA QRRTAAGIMK NAVVDGIVAT DVPELERTTP IMQKKVGQIM LILVSLAAVV
VNPSVKTVRE AGILITAAAV TLWENGASSV WNATTAIGLC HIMRGGWLSC LSMTWTLIKN
MEKPGLKRGG AKGRTLGEVW KERLNQMTKE EFTRYRKEAI IEVDRSAAKH ARKEGNVTGG
HPVSRGTAKL RWLVERRFLE PVGKVIDLGC GRGGWCYYMA TQKRVQEVRG YTKGGPGHEE
PQLVQSYGWN IVTMKSGVDV FYRPSECCDT LLCDIGESSS SAEVEEHRTI RVLEMVEDWL
HRGPREFCVK VLCPYMPKVI EKMELLQRRY GGGLVRNPLS RNSTHEMYWV SRASGNVVHS
VNMTSQVLLG RMEKRTWKGP QYEEDVNLGS GTRAVGKPLL NSDTSKIKNR IERLRREYSS
TWHHDENHPY RTWNYHGSYD VKPTGSASSL VNGVVRLLSK PWDTITNVTT MAMTDTTPFG
QQRVFKEKVD TKAPEPPEGV KYVLNETTNW LWAFLAREKR PRMCSREEFI RKVNSNAALG
AMFEEQNQWR SAREAVEDPK FWEMVDEERE AHLRGECHTC IYNMMGKREK KPGEFGKAKG
SRAIWFMWLG ARFLEFEALG FLNEDHWLGR KNSGGGVEGL GLQKLGYILR EVGTRPGGKI
YADDTAGWDT RITRADLENE AKVLELLDGE HRRLARAIIE LTYRHKVVKV MRPAADGRTV
MDVISREDQR GSGQVVTYAL NTFTNLAVQL VRMMEGEGVI GPDDVEKLAK GKGPKVRTWL
FENGEERLSR MAVSGDDCVV KPLDDRFATS LHFLNAMSKV RKDIQEWKPS TGWYDWQQVP
FCSNHFTELI MKDGRTLVVP CRGQDELVGR ARISPGAGWN VRDTACLAKS YAQMWLLLYF
HRRDLRLMAN AICSAVPVNW VPTGRTTWSI HAGGEWMTTE DMLEVWNRVW IEENEWMEDK
TPVEKWSDVP YSGKREDIWC GSLIGTRARA TWAENIQVAI NQVRAIIGDE KYVDYMSSLK
RYEDTTLVED TVL
//
