ID C8YMC5_9FLAV Unreviewed; 3434 AA.
AC C8YMC5;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Lammi virus.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae.
OX NCBI_TaxID=649187 {ECO:0000313|EMBL:ACR56717.1, ECO:0000313|Proteomes:UP000172483};
RN [1] {ECO:0000313|EMBL:ACR56717.1, ECO:0000313|Proteomes:UP000172483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19570865; DOI=10.1128/JVI.00529-09;
RA Huhtamo E., Putkuri N., Kurkela S., Manni T., Vaheri A., Vapalahti O.,
RA Uzcategui N.Y.;
RT "Characterization of a novel flavivirus from mosquitoes in northern europe
RT that is related to mosquito-borne flaviviruses of the tropics.";
RL J. Virol. 83:9532-9540(2009).
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 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; FJ606789; ACR56717.1; -; Genomic_RNA.
DR MEROPS; S07.001; -.
DR Proteomes; UP000172483; 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: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; 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 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 107..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 740..761
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 768..789
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1144..1163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1175..1194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1272..1291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1298..1321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1341..1363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1375..1393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1399..1416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1470..1495
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2176..2195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2224..2242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2254..2271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2363..2390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2443..2459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1371..1501
FT /note="Flavivirus NS2B"
FT /evidence="ECO:0000259|PROSITE:PS51527"
FT DOMAIN 1498..1680
FT /note="Peptidase S7"
FT /evidence="ECO:0000259|PROSITE:PS51528"
FT DOMAIN 1683..1839
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1850..2015
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2523..2792
FT /note="MRNA cap 0-1 NS5-type MT"
FT /evidence="ECO:0000259|PROSITE:PS51591"
FT DOMAIN 3056..3208
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT ACT_SITE 1552
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT ACT_SITE 1576
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT ACT_SITE 1637
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT BINDING 2582
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2612
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2613
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2630
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2631
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2657
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2658
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2747
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT BINDING 2966
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 2970
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 2975
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 2978
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 3243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 3259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT BINDING 3378
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT DISULFID 294..321
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 351..407
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 365..396
FT /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT DISULFID 383..412
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 3434 AA; 378678 MW; 586B7EFDD678CBFE CRC64;
MANKPKKPAR RAIDIVRRAL PRVSGPKRVL ARASKSIMQS LAGLRATVAY LLYMTFLGNK
VSNATKQKFR NAKKSDVIKI LSGFKRTVTN LLSSVQKRKK NGKRSKTEIS LVVLMLFGAA
MAASMFTRDG KAHLNVSSSD VGKWLQIKTA VGNGTCIVTA TDVGSWCADN VRYLCPRLDN
AADPDDVDCW CNIVSVYVTY GRCKRESSGP RRGKRSVALA PHGTGDLHTG TAPMWKAHSS
AHHYLQRVER WALRKPGYLA ALVAIGWLLG KTKAQKIIYI TLLVLIGPAY SLQCVDTTNR
DFIQGVSGGT WVDVVLDING CVTITAADKP TVDFKLVKLE ITKMAAIRSY CLKASTSDAS
SVSGCPGTGE VHNTKAEDTA FICKSSNPDR GWGNGCGLFG KGSMETCAKF TCDKKLAGHV
ISRENIEAEV DISIHGQSGA ADDNSTKRKT RKELATITIT PQTASAEADM GDYGKIGIDC
SMDIGIDFEQ VVIADAGGRY WMLRKDWYQD LALPWTAPSA NFWHDRDRLI EFGIPHATKQ
GVHNIGDQEG AFHTAAAKAP AVEYHESKVR LPTGLLRCRV KMGNMKLKGT TYSLCTEMFT
FSKRPVDTGH GTVVFQVSYA GNDAPCKIPV AVTEKPNGEP TGRLITAHPI ILKKDDRAVV
EVEPPFGNSY IEIGTATKKI TEVWHKPGSS IGSAFVLSYK GLQRLTVMGE HAWDFGSVGG
FFTSLGKAVH HVFGSVFRTL FGGISWIAKI LIGGLLVWLG ISARDRVLAT TFIIVGSILL
YLATTTVALS EVGCSLDITH REIKCGDGIF IFRDAGGWRD KYIFHPGSPK TLAAAIWRGW
NDGICGVRST TRMEHEMWKQ IENEINGILE ENDIKLSVVV KNANGTYPRG SKMLTRNTTG
LQYGWKSWGK TMFVAVPIAS DTFIVDGNDE GECPSEKRAW NTFKIEEFGT GIMKTKVFLD
LSDAQTEYCD TELLGAAVKG NKSVHGDPAM WLMSSKDSGE WQLDGLSLTE SRRCLWPDSH
TIWGRGVQES KLILPAMFGG PVSHMNTRNG YATQVSGPWN NVPLEMKFEE CPGTKVVVEG
NCTNRGESVR STTDSGKIIP EWCCRKCTMP PMSFRTPDGC WYAMEIRPKK ASEESLIRSK
VSAGTFQGID DFSLGLLILI IFIQEGLKRR MTSKYILLAS LGLLLAAVLG DLTYQDIIRY
VIMVGTAFAE MNTGGDLVHL ALIATFKIQP GYLMPFLLRK IWSPRESTLL ASAAVVLQIG
AVPWQSTKSM QVLNALALGW LYIRAIVVPG AISKAMPLIC MCVPGVMALT PNAIRISMLT
IAAGTMIKGN KGTSVRKHVP YFLGLVGATM GLDPIGMLGY SLLTYTSGKR SWPAGEIMTA
VGLTCAMVGA LSGNAMNDIA GPAAAASLIF VAYAISGRSS DVFLEKAGEI TWCEEAAVSG
SSPRVDVQVT DGGDFRLRHE AETSWLKNGV MAFCLVLAGV HPLAIPVSGL IWFGYVKSGR
RGTVLWDVPH PVATASPTVE DGCYRVMSKR LIGSTQVGVG VMKDSVFHTM WHVTRGASLT
SGEGRMDPYW ADVREDLISY GGPWKLNGTW DGNSEVQLIA VQPQQVPVNV KTTPGRFVMT
DGTEVGAVVL DYPSGTSGSP IIDKDGVVVG LYGNGVMLND STYASAIAQS AGCENITPLV
FHPDMLRKGK LSVMDLHPGA GKTRKVLPII LKDAVAKRLK TLVLAPTRVV AKEMHSALTG
LPVRYQTSAV QGPNTGTELI DVMCHATFTY RQLTPGRMVN YQLYIMDEAH FTDPASIAAR
GIIATRVKLG EAAAIFMTAT PPGSLDAFPE SNAHIEDEER EIPDKAWSSG FEWITDYVGK
TVWFVPSIRT GNIIASCLSR AGKKCVVLNS KTFNDEYPKT KSGTWDYVIT TDISEMGANF
KASRVIDCRT SIKPILTHSP SERVVLGTPK AICSASAAQR RGRVGRDPAQ LGDQYVYGGE
VGEDFSNLVH WKEAKILMDN IMVPGGLYPQ FYEPESHMLS ETDGHFRLDA TKRDVFKDLV
RKADLPIWLA YQVASGGYEY NDRTWCHTGP SGHLIYDDYG QTVEYRLING ERKTLQPKWI
DQRTYQEKTA LRTFIEFAEG RRSYVPLLEV MGRMPQHFTD KTIDAVDTFK TVLTATPGSR
AYRLAIDNLP DAAETFLFVL MIGFMTMGIL VFLMAPKGVT RMSLGFMTIM AASYFLWVSG
MAGYQIAAMQ LVSFIMFVVL VPEPGSQRSV QDNTIAMVLI CILSLAALIA ANETGLLDKT
KGDFAWIKGP APGGGGSWNL DFTVDLRPAT SWSLYVVIAT MLGPVFEHAI VTQFTSISLT
AITQQAGILL SMDKGLPFFN LDWGVILLGI GCWSSITGTT VACAMGLSFV HFTMTLPGVK
AKAAREAQSR TAAGVSKNPI VDGVNTLNVT SPPGMDPMYE RKLGLWMLIL IASVSLAVNK
NLTHFMELGI LGSAALGPLI EGNSSTVWNT AVASSLCNLM RGQYLAGIPL TFTLIRNLSL
KGVPRRGMTI CNTRGMEWKR KLNAMSKDMF QRYKRDGITE VDRTAARDAM KSGNVTGGHA
VSRGSAKLRW LVDKGYLRLM GDVTDLGCGR GGWCYYAAAQ RNVTSVRGFT KGGEGHEEPM
PVQSYGWNIV TLRSKVDVFY MPTHMTDTVL CDIGESSSNM LVEEERTLRV LNMFEEWLRK
AKPTHYCCKI LAPYMPAVLE KLDKLMKIHG GALVRVPLSR NSTHEMYWVS DARGNAMNAV
SSLSRTLLDR MIHSTGKVRW EEDVNLGTGT RAVHSTADEP NWDKIGLRVK KLEQEYKASW
TYDSEHPYKT WTYHGSYETS TTGSASSMIN GVVKELTHPW DVNSGVTNVC MTDTTPFGQQ
RVFKEKVDTK AMEPPSGTRE VMRITNKWLT NYLSRTKRPR MCTPDEFIAK VNSDAALGTM
FNDQGHWPSA REAVRDHGFW KQVDIERQHH LEGRCVSCVY NMMGKREKKL TEFGRAKGSR
AIWYMWLGAR YLEFEALGFL NEDHWLSRDN SKGGVEGIGL QYLGYVLEDI NARQGGQMYA
DDTAGWDTRI TNADLEDEME IIKLMGHTHK KLANAIMDLT YMNKVVRVMR PGKGGKTLMD
IISRKDQRGS GQVVTYPLNT WTNLKVQLIR MAEGEGVILP EDTLALTACS RRNLEMWLTR
NGEERLGRIA ASGDDVVVKP IDDRFAEALH FLNSMSKIRK DINEWRASAG WCSWEGVPFC
SHHFHKLSLK DGRTLTVPCR DQDELIGRAR VSPGAGWTLR ETAGLSKAYA QMWMLIHFHR
RDLRTIAFAI CSAVPKDWVP TGRTTWSIHG RGEWMTNEDM LAVWNRVWIT ENQYMTNKEL
VHDWRDIPYL RKQLDKNCGS MIGVRSRATW ADNIRVSVNQ VRGYIGKNEQ YLDYLQAQNR
FSIPAEFTMG NILV
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