ID A3EZ70_9FLAV Unreviewed; 3412 AA.
AC A3EZ70;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS Saint Louis encephalitis virus.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Orthoflavivirus; Orthoflavivirus louisense.
OX NCBI_TaxID=11080 {ECO:0000313|EMBL:ABN11824.1};
RN [1] {ECO:0000313|EMBL:ABN11824.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FL 79-411 {ECO:0000313|EMBL:ABN11824.1};
RX PubMed=18374605; DOI=10.1016/j.ympev.2008.02.015;
RA Baillie G.J., Kolokotronis S.O., Waltari E., Maffei J.G., Kramer L.D.,
RA Perkins S.L.;
RT "Phylogenetic and evolutionary analyses of St. Louis encephalitis virus
RT genomes.";
RL Mol. Phylogenet. Evol. 47:717-728(2008).
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; EF158062; ABN11824.1; -; 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: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; 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; 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 741..762
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 769..789
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1139..1161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1173..1195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1215..1236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1266..1284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1305..1324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1336..1361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1396..1414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1470..1493
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2171..2190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2197..2214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2220..2237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2249..2266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2308..2329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2336..2355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2375..2394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2445..2461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1369..1499
FT /note="Flavivirus NS2B"
FT /evidence="ECO:0000259|PROSITE:PS51527"
FT DOMAIN 1500..1677
FT /note="Peptidase S7"
FT /evidence="ECO:0000259|PROSITE:PS51528"
FT DOMAIN 1680..1836
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1847..2011
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2525..2790
FT /note="MRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000259|PROSITE:PS51591"
FT DOMAIN 3054..3206
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 2771..2791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1550
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT ACT_SITE 1574
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT ACT_SITE 1634
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT BINDING 2580
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2610
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2611
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2628
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2629
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2655
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2656
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2744
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2964
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
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 2973
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 2976
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 3241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 3257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 3376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT DISULFID 291..318
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 348..404
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 362..393
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 380..409
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 478..576
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 593..624
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT NON_TER 3412
FT /evidence="ECO:0000313|EMBL:ABN11824.1"
SQ SEQUENCE 3412 AA; 378519 MW; 8DC8B09005AF5C25 CRC64;
MSKKPGKPGR NRVVNMLKRG VSRVNPLTGL KRILGSLLDG RGPVRFILAI LTFFRFTALQ
PTEALKRRWR AVDKRTALKH LNGFKRDLGS MLDTINRRPS KKRGGTRSLL GLAALIGLAS
SLQLSTYQGK VLMSINKTDA QSAINIPSAN GANTCIVRAL DVGVMCKDDI TYLCPVLSAG
NDPEDIDCWC DIEEVWVHYG RCTRMGHSRR SRRSISVQHH GDSTLATKNT PWLDTVKTTK
YLTKVENWVL RNPGYALVAL AIGWMLGSNN TQRVVFVIML MLIAPAYSFN CLGTSNRDFV
EGASGATWID LVLEGGSCVT VMAPEKPTLD FKVMKMEATE LATVREYCYE ATLDTLSTVA
RCPTTGEAHN TKRSDPTFVC KRDVVDRGWG NGCGLFGKGS IDTCAKFTCK NKATGKTILR
ENIKYEVAIF VHGSTDSTSH GNYSEQIGKN QAARFTISPQ APSFTANMGE YGTVTIDCEA
RSGINTEDYY VFTVKEKSWL VNRDWFHDLN LPWTSPATTD WRNRETLVEF EEPHATKQTV
VALGSQEGAL HTALAGAIPA TVSSSTLTLQ SGHLKCRAKL DKVKIKGTTY GMCDSAFTFS
KNPTDTGHGT VIVELQYTGS NGPCRVPISV TANLMDLTPV GRLVTVNPFI STGGANNKVM
IEVEPPFGDS YIVVGRGTTQ INYHWHKEGS SIGKALATTW KGAQRLAVLG DTAWDFGSIG
GVFNSIGKAV HQVFGGAFRT LFGGMSWITQ GLLGALLLWM GLQARDRSIS LTLLAVGGIL
IFLATSVQAD SGCAIDLQRR ELKCGGGIFV YNDVEKWKSD YKYFPLTPTG LARVIQEAHA
NGICGIRSTS RLEHLMWENI QRELNAIFED NEIDLSVVVQ EDPKYYKRAP RRLKKLEDEL
DYGWKKWGKT LFVEPRLGNN TFVVDGPETK ECPTANRAWN SFKVEDFGFG MVFTRLWLTI
REENTTECDS AIIGTAIKGD RAVHSDLSYW IESKKNETWQ LERAVMGEVK SCTWPETHTL
WGDGVVESEM IIPVTLGGPK SHHNKRNGYH TQTKGPWSEG EITLDFDYCP GTTVTVTEHC
GNRGASLRTT TASGKLVTDW CCRSCSLPPL RYTTKDGCWY GMEIRPVKEE EAKLVKSRVT
AGVAGGMEPF QLGLLVAFIA TQEVLKRRWT GKLTLTSLAV CLALLIFGNL TYMDLVRYLV
LVGTAFAEMN TGGDVIHLAL VAVFKVQPAF LVGLFLRMQW SNQENILMVI GAAFLQMAAN
DLKLEVLPIL NAMSIAWMLI RAMKEGKVAM YALPILCALT PGMRMAGLDV IRCLLLIIGI
VTLLNERRES VAKKKGGYLL AAALCQAGVC SPLIMMGGLI LAHPNGKRSW PASEVLTGVG
LMCALAGGLL EFEETSMVVP FAIAGLMYIT YTVSGKAAEM WIEKAADITW EQNAEITGTS
PRLDVDLDSH GNFKLLNDPG APVHLFALRF ILLGLSARFH WFIPFGVLGF WLLGKHSKRG
GALWDVPSPK VYPKCETKPG IYRIMTRGIL GTFQAGVGVM HEGVFHTMWH ATEGAVLRNG
EGRLDPYAGD VRNDLISYGG PWKLSATWDG TEEVQMIAVA PGKPAVNVQT TPGVFKTPFG
TIGAVTLDFP KGTSGSPIIN KKGEIIGLYG NGVLIGQGEY VSGIIQGERT EEPIPDAYNE
EMLRKRKLTV LELHPGAGKT RKVLPQIIKD CIQKRLRTAV LAPTRVVACE IAEALKGLPI
RYLTPAVRNE HQGNEIVDVM CHATLTQKLL TPTRVPNYQV YIMDEAHFID PASIAARGYI
STKVELGEAA AIFMTATPPG TNDPFPDSNS PILDVEAQVP DKAWSTGYEW ITNFTGRTVW
FVPSVKSGNE IAICLQKAGK RVIQLNRKSF DTEYPKTKNN EWDFVVTTDI SEMGANFGAH
RVIDSRKCVK PVILEDDDRV ILNGPMAITS ASAAQRRGRI GRNPSQIGDE YHYGGATNED
DHDLANWTEA KILLDNIYLP NGLVAQMYQP ERDKVFTMDG EFRLRGEERK NFVELMRNGD
LPVWLAYKVA SNGHSYQDRS WCFTGQTNNT ILEDNNEVEV FTKTGDRKIL RPKWMDARVC
CDYQALKSFK EFAAGKRSAL GMMEVMGRMP NHFWEKTVAA ADTLYLLGTS EANSRAHKEA
LAELPDSLET LLLIGMLCVM SMGTFIFLMN RKGVGKMGLG AFVMTLATAL LWAAEVPGTQ
IAGVLLIVFL LMIVLIPEPE KQRSQTDNQL AVFLICIMTL MGVVAANEMG LLEKTKSDIA
KLFGSQPGSV GFATRTTPWD ISLDIKPATA WALYAAATMV MTPLIKHLIT TQYVNFSLTA
IASQAGVLLG LTNGMPFTAM DLSVPLLVLG CWNQMTLPSL AVAVMLLAIH YAFMIPGWQA
EAMRAAQRRT AAGIMKNAVV DGIVATDIPD LSPATPMTEK KMGQILLIAA AVLAVLVRPG
ICSIKEFGVL GSAALVTLIE GTAGVVWNCT TAVGLCNLMR GGWLAGMSIT WTVYKNVDKP
KGKRGGGKGA TLGEIWKSRL NQLTRAEFMA YRKDGIVEVD RAPARKARRE GRLTGGHPVS
RGSAKLRWIT ERGFVKPMGK VVDLGCGRGG WSYYCATLKH VQEVKGFTKG GPGHEEPQLM
QSYGWNLVHM KSGVDVFHKP AEPADTVLCD IGESNPSCEV EEARTARVLD MVEEWLKKGA
TEFCIKVLCP YTPKIIEKLE KLQRKYGGGL VRVPLSRNST HEMYWVSGAA GNIIHAVSMT
SQVLMGRMDK QNRSGPRYEE DVNLGSGTRS VGKLTEKPDL RKVGERIRRL REEYQQTWTY
DHNNPYRTWN YHGSYEVKPT GSASSMVNGV VRLLSKPWDM ITNVTTMAMT DTTPFGQQRV
FKEKVDTKAP EPPLGVAQIM DVTTDWLWDF VAREKKPRVC TPEEFKAKVN SHAALGAMFE
EQNQWSSARE AVEDPRFWEM VDEEREAHLK GECHTCIYNM MGKREKKTGE FGKAKGSRAI
WYMWLGARFL EFEALGFLNE DHWMSRENSY GGVEGKGLQK LGYILQEISQ ISGGKMYADD
TAGWDTRITK EDLKNEAKIT KRMEERHRKL AEAIIDLTYR HKVVKVMRPG PDGKTYMDVI
SREDQRGSGQ VVTYALNTFT NLAVQLIRCM EAEGVVDEDD ITRVRLGRLA KAVEWLRKNG
PERLSRMAVS GDDCVVKPID DRFATALHFL NNMSKIRKDI QEWKPSTGWH NWQEVPFCSH
HFNELMLKDG RTIVVPCRSQ DELIGRARIS PGAGWNVKET ACLSKSYAQM WLLMYFHRRD
LRMMANAICS AVPVNWVPTG RTTWSIHGKG EWMTTEDMLS VWNRVWIEEN EYMKDKTPLA
AWNDIPYLGK REDIWCGSLI GTRTRATWAE NIYAPIMQIR NLIGEEEYRD YM
//