ID H6VBW8_WNV Unreviewed; 3397 AA.
AC H6VBW8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS West Nile virus (WNV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Orthoflavivirus; Orthoflavivirus nilense.
OX NCBI_TaxID=11082 {ECO:0000313|EMBL:AEZ56183.1};
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:AEZ56183.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WNV-1/BID-V5041 {ECO:0000313|EMBL:AEZ56183.1};
RG Broad Institute Genome Sequencing Platform;
RA Henn M.R., Newman R.M., Levin J., Malboeuf C., Casali M., Russ C.,
RA Lennon N., Erlich R., Anderson S., Rizzolo K., Green L., Ryan E., Yu Q.,
RA Young S., Berlin A., Heiman D., Sykes S., Koehrsen M., Borenstein D.,
RA Engels R., Freedman E., Gellesch M., Heilman E., Howarth C., Jen D.,
RA Larson L., Neiman D., Park D., Pearson M., Roberts A., Sisk P., Stolte C.,
RA White J., Alvarado L., Godfrey P., Shenoy N., Yandava C., Zeng Q., Ebel G.,
RA Nusbaum C., Birren B.;
RL Submitted (JUN-2011) 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}.
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; JN819314; AEZ56183.1; -; Genomic_RNA.
DR MEROPS; S07.003; -.
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: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 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 707..728
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 735..755
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1143..1161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1181..1202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1209..1225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1245..1269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1276..1294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1306..1330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1342..1360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1366..1384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1436..1462
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2138..2159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2168..2186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2192..2209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2221..2243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2276..2293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2314..2337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2343..2362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2410..2429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1339..1470
FT /note="Flavivirus NS2B"
FT /evidence="ECO:0000259|PROSITE:PS51527"
FT DOMAIN 1470..1647
FT /note="Peptidase S7"
FT /evidence="ECO:0000259|PROSITE:PS51528"
FT DOMAIN 1650..1806
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1817..1982
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2493..2758
FT /note="MRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000259|PROSITE:PS51591"
FT DOMAIN 3022..3174
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT ACT_SITE 1520
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT ACT_SITE 1544
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT ACT_SITE 1604
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT BINDING 2548
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2578
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2579
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2596
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2597
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2623
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2624
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2712
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2932
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 2941
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 2944
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 3209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 3225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 3344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT DISULFID 257..284
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 314..370
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 328..359
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 346..375
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 444..542
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 559..590
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEZ56183.1"
SQ SEQUENCE 3397 AA; 377294 MW; 07A94AD38D393B8D CRC64;
LIDGKGPIRF VLALLAFFRF TAIAPTRAVL DRWRGVDKQT AMKHLLSFKK ELGTLTSAIN
RRSSKQKKRG GKTGIAVMIG LIASVGAVTL SNFQGKVMMT VNATDVTDVI TIPTAAGKNL
CIVRAMDVGY MCDDTITYEC PVLSAGNDPE DIDCWCTKSA VYVRYGRCTK TRHSRRSRRS
LTVQTHGEST LANKKGAWMD STKATRYLVK TESWILRNPG YALVAAVIGW MLGSNTMQRV
VFVVLLLLVA PAYSFNCLGM SNRDFLEGVS GATWVDLVLE GDSCVTIMSK DKPTIDVKMM
NMEAANLAEV RSYCYLATVS DLSTKAACPT MGEAHNDKRA DPAFVCRQGV VDRGWGNGCG
LFGKGSIDTC AKFACSTKAI GRTILKENIK YEVAIFVHGP TTVESHGNYS TQAGATQAGR
FSITPAAPSY TLKLGEYGEV TVDCEPRSGI DTNAYYVMTV GTKTFLVHRE WFMDLNLPWS
SAGSTVWRNR ETLMEFEEPH ATKQSVIALG SQEGALHQAL AGAIPVEFSS NTVKLTSGHL
KCRVKMEKLQ LKGTTYGVCS KAFKFLGTPA DTGHGTVVLE LQYTGTDGPC KVPISSVASL
NDLTPVGRLV TVNPFVSVAT ANAKVLIELE PPFGDSYIVV GRGEQQINHH WHKSGSSIGK
AFTTTLKGAQ RLAALGDTAW DFGSVGGVFT SVGKAVHQVF GGAFRSLFGG MSWITQGLLG
ALLLWMGINA RDRSIALTFL AVGGVLLFLS VNVHADTGCA IDISRQELRC GSGVFIHNDV
EAWMDRYKYY PETPQGLAKI IQKAHKEGVC GLRSVSRLEH QMWEAVKDEL NTLLKENGVD
LSVVVEKQEG MYKSAPKRLT ATTEKLEIGW KAWGKSILFA PELANNTFVV DGPETKECPT
QNRAWNSLEV EDFGFGLTST RMFLKVRESN TTECDSKIIG TAVKNNLAIH SDLSYWIESR
LNDTWKLERA VLGEVKSCTW PETHTLWGDG ILESDLIIPV TLAGPRSNHN RRPGYKTQNQ
GPWDEGRVEI DFDYCPGTTV TLSESCGHRG PATRTTTESG KLITDWCCRS CTLPPLRYQT
DSGCWYGMEI RPQRHDEKTL VQSQVNAYNA DMIDPFQLGL LVVFLATQEV LRKRWTAKIS
MPAILIALLV LVFGGITYTD VLRYVILVGA AFAESNSGGD VVHLALMATF KIQPVFMVAS
FLKARWTNQE NILLMLAAVF FQMAYHDARQ ILLWEIPDVL NSLAVAWMIL RAITFTTTSN
VVVPLLALLT PGLRCLNLDV YRILLLMVGI GSLIREKRSA AAKKKGASLL CLALASTGLF
NPMILAAGLI ACDPNRKRGW PATEVMTAVG LMFAIVGGLA ELDIDSMAIP MTIAGLMFAA
FVISGKSTDM WIERTADISW ESDAEITGSS ERVDVRLDDD GNFQLMNDPG APWKIWMLRM
VCLAISAYTP WAILPSVVGF WITLQYTKRG GVLWDTPSPK EYKKGDTTTG VYRIMTRGLL
GSYQAGAGVM VEGVFHTLWH TTKGAALMSG EGRLDPYWGS VKEDRLCYGG PWKLQHKWNG
QDEVQMIVVE PGKNVKNVQT KPGVFKTPEG EIGAVTLDFP TGTSGSPIVD KNGDVIGLYG
NGVIMPNGSY ISAIVQGERM DEPIPAGFEP EMLRKKQITV LDLHPGAGKT RRILPQIIKE
AINRRLRTAV LAPTRVVAAE MAEALRGLPI RYQTSAVPRE HNGNEIVDVM CHATLTHRLM
SPHRVPNYNL FVMDEAHFTD PASIAARGYI STKVELGEAA AIFMTATPPG TSDPFPESNS
PISDLQTEIP DRAWNSGYEW ITEYTGKTVW FVPSVKMGNE IALCLQRAGK KVVQLNRKSY
ETEYPKCKND DWDFVITTDI SEMGANFKAS RVIDSRKSVK PTIITEGEGR VILGEPSAVT
AASAAQRRGR IGRNPSQVGD EYCYGGHTNE DDSNLAHWTE ARIMLDNINM PNGLIAQFYQ
PEREKVYTMD GEYRLRGEER KNFLELLRTA DLPVWLAYKV AAAGVSYHDR RWCFDGPRTN
TILEDNNEVE VITKLGERKI LRPRWIDARV YSDHQALKAF KDFASGKRSQ IGLIEVLGKM
PEHFMGKTWE ALDTMYVVAT AEKGGRAHRM ALEELPDALQ TIALIALLSV MTMGVFFLLM
QRKGIGKIGL GGAVLGVATF FCWMAEVPGT KIAGMLLLSL LLMIVLIPEP EKQRSQTDNQ
LAVFLICVMT LVSAVAANEM GWLDKTKSDI SSLFGQRIEV KENFSMGEFL LDLRPATAWS
LYAVTTAVLT PLLKHLITSD YINTSLTSIN VQASALFTLA RGFPFVDVGV SALLLAAGCW
GQVTLTVTVT AATLLFCHYA YMVPGWQAEA MRSAQRRTAA GIMKNAVVDG IVATDVPELE
RTTPIMQKKV GQIMLILVSL AAVVVNPSVK TVREAGILIT AAAVTLWENG ASSVWNATTA
IGLCHIMRGG WLSCLSITWT LIKNMEKPGL KRGGAKGRTL GEVWKERLNQ MTKEEFTRYR
KEAIIEVDRS AAKHARKEGN VTGGHPVSRG TAKLRWLVER RFLEPVGKVI DLGCGRGGWC
YYMATQKRVQ EVRGYTKGGP GHEEPQLVQS YGWNIVTMKS GVDVFYRPSE CCDTLLCDIG
ESSSSAEVEE HRTIRVLEMV EDWLHRGPRE FCVKVLCPYM PKVIEKMELL QRRYGGGLVR
NPLSRNSTHE MYWVSRASGN VVHSVNMTSQ VLLGRMEKRT WKGPQYEEDV NLGSGTRAVG
KPLLNSDTSK IKNRIERLRR EYSSTWHHDE NHPYRTWNYH GSYDVKPTGS ASSLVNGVVR
LLSKPWDTIT NVTTMAMTDT TPFGQQRVFK EKVDTKAPEP PEGVKYVLNE TTNWLWAFLA
REKRPRMCSR EEFIRKVNSN AALGAMFEEQ NQWRSAREAV EDPKFWEMVD EEREAHLRGE
CHTCIYNMMG KREKKPGEFG KAKGSRAIWF MWLGARFLEF EALGFLNEDH WLGRKNSGGG
VEGLGLQKLG YILREVGTRP GGRIYADDTA GWDTRITRAD LENEAKVLEL LDGEHRRLAR
AIIELTYRHK VVKVMRPAAD GRTVMDVISR EDQRGSGQVV TYALNTFTNL AVQLVRMMEG
EGVIGPDDVE KLTKGKGPKV RTWLFENGEE RLSRMAVSGD DCVVKPLDDR FATSLHFLNA
MSKVRKDIQE WKPSTGWYDW QQVPFCSNHF TELIMKDGRT LVVPCRGQDE LVGRARISPG
AGWNVRDTAC LAKSYAQMWL LLYFHRRDLR LMANAICSAV PVNWVPTGRT TWSIHAGGEW
MTTEDMLEVW NRVWIEENEW MEDKTPVEKW SDVPYSGKRE DIWCGSLIGT RARATWAENI
QVAINQVRAI IGDEKYVDYM SSLKRYEDTT LVEDTVL
//
