ID   C3V005_9FLAV            Unreviewed;      3392 AA.
AC   C3V005;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS   Chimeric Tick-borne encephalitis virus/Dengue virus 4.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Flavivirus.
OX   NCBI_TaxID=638787 {ECO:0000313|EMBL:ACO82049.1, ECO:0000313|Proteomes:UP000163390};
RN   [1] {ECO:0000313|EMBL:ACO82049.1, ECO:0000313|Proteomes:UP000163390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1438242; DOI=10.1073/pnas.89.21.10532;
RA   Pletnev A.G., Bray M., Huggins J., Lai C.J.;
RT   "Construction and characterization of chimeric tick-borne
RT   encephalitis/dengue type 4 viruses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:10532-10536(1992).
RN   [2] {ECO:0007829|PDB:1K4R}
RP   STRUCTURE BY ELECTRON MICROSCOPY (24.00 ANGSTROMS) OF 284-678, AND
RP   DISULFIDE BONDS.
RX   PubMed=11893341; DOI=10.1016/S0092-8674(02)00660-8;
RA   Kuhn R.J., Zhang W., Rossmann M.G., Pletnev S.V., Corver J., Lenches E.,
RA   Jones C.T., Mukhopadhyay S., Chipman P.R., Strauss E.G., Baker T.S.,
RA   Strauss J.H.;
RT   "Structure of dengue virus: implications for flavivirus organization,
RT   maturation, and fusion.";
RL   Cell 108:717-725(2002).
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}.
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; FJ828987; ACO82049.1; -; Other_RNA.
DR   PDB; 1K4R; EM; 24.00 A; A/B/C=284-678.
DR   PDBsum; 1K4R; -.
DR   SMR; C3V005; -.
DR   MEROPS; S07.001; -.
DR   EvolutionaryTrace; C3V005; -.
DR   Proteomes; UP000163390; 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; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1K4R};
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        104..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        731..752
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1162..1182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1202..1223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1291..1310
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1322..1341
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1446..1473
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2152..2170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2177..2195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2201..2218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2230..2247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1350..1479
FT                   /note="Flavivirus NS2B"
FT                   /evidence="ECO:0000259|PROSITE:PS51527"
FT   DOMAIN          1480..1657
FT                   /note="Peptidase S7"
FT                   /evidence="ECO:0000259|PROSITE:PS51528"
FT   DOMAIN          1659..1815
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1810..1991
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          2494..2756
FT                   /note="MRNA cap 0-1 NS5-type MT"
FT                   /evidence="ECO:0000259|PROSITE:PS51591"
FT   DOMAIN          3020..3170
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   ACT_SITE        1530
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT   ACT_SITE        1554
FT                   /note="Charge relay system; for serine protease NS3
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-1"
FT   ACT_SITE        1614
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         2711
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-2"
FT   BINDING         2930
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT   BINDING         2934
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         2942
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT   BINDING         3205
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT   BINDING         3221
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT   BINDING         3340
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-4"
FT   DISULFID        286..313
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-3,
FT                   ECO:0007829|PDB:1K4R"
FT   DISULFID        343..404
FT                   /evidence="ECO:0007829|PDB:1K4R"
FT   DISULFID        343..399
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT   DISULFID        357..388
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-3,
FT                   ECO:0007829|PDB:1K4R"
FT   DISULFID        375..404
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-3"
FT   DISULFID        375..399
FT                   /evidence="ECO:0007829|PDB:1K4R"
FT   DISULFID        469..573
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-3,
FT                   ECO:0007829|PDB:1K4R"
FT   DISULFID        590..621
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003817-3,
FT                   ECO:0007829|PDB:1K4R"
SQ   SEQUENCE   3392 AA;  378138 MW;  0C7C70F2A34E4418 CRC64;
     MNQRKKVVRP PFNMLKRERN RVSTPQGLVK RFSTGLFSGK GPLRMVLAFI TFLRVLSIPP
     TAGILKRWGQ LKKNKAIKIL IGFRKEIGRM LNILNGRKRS AVDWTGWLLV VVLLGVTLAA
     TVRKERDGTT VIRAEGKDAA TQVRVENGTC VILATDMGSW CDDSLTYECV TIDQGEEPVD
     VDCFCRNVDG VYLEYGRCGK QEGSRTRRSV LIPSHAQGDL TGRGHKWLEG DSLRTHLTRV
     EGWVWKNKVL TLAVIAVVWL TVESVVTRVA VVVVLLCLAP VYASRCTHLE NRDFVTGTQG
     TTRVTLVLEL GGCVTITAEG KPSMDVWLDS IYQENPAKTR EYCLHAKLSD TKVAARCPTM
     GPATLAEEHQ SGTVCKRDQS DRGWGNHCGL FGKGSIVTCV KASCEAKKKA TGHVYDANKI
     VYTVKVEPHT GDYVAANETH SGRKTASFTV SSERTILTMG DYGDVSLLCR VASGVDLAQT
     VILELDKTSE HLPTAWQVHR DWFNDLALPW KHEGAQNWNN AERLVEFGAP HAVKMDVYNL
     GDQTGVLLKS LAGVPVAHID GTKYHLKSGH VTCEVGLEKL KMKGLTYTMC DKTKFTWKRI
     PTDSGHDTVV MEVAFSGTKP CRIPVRAVAH GSPDVNVAML ITPNPTIENN GGGFIEMQLP
     PGDNIIYVGE LSHQWFQKGS SIGRVFQKTR KGIERLTVIG EHAWDFGSTG GFLTSVGKAL
     HTVLGGAFNS LFGGVGFLPK ILVGVVLAWL GLNSRNTSMA MTCIAVGGIT LFLGFTVQAD
     MGCVASWSGK ELKCGSGIFV VDNVHTWTEQ YKFQPESPAR LASAILNAHK DGVCGIRSTT
     RLENVMWKQI TNELNYVLWE GGHDLTVVAG DVKGVLTKGK RALTPPVSDL KYSWKTWGKA
     KIFTPEARNS TFLIDGPDTS ECPNERRAWN SLEVEDYGFG MFTTNIWMKF REGSSEVCDH
     RLMSAAIKDQ KAVHADMGYW IESSKNQTWQ IEKASLIEVK TCLWPKTHTL WSNGVLESQM
     LIPKSYAGPF SQHNYRQGYA TQTVGPWHLG KLEIDFGECP GTTVTIQEDC DHRGPSLRTT
     TASGKLVTQW CCRSCTMPPL RFLGEDGCWY GMEIRPLSEK EENMVKSQVT AGQGTSETFS
     MGLLCLTLFV EECLRRRVTR KHMILVVVIT LCAIILGGLT WMDLLRALIM LGDTMSGRIG
     GQIHLAIMAV FKMSPGYVLG VFLRKLTSRE TALMVIGMAM TTVLSIPHDL MELIDGISLG
     LILLKIVTQF DNTQVGTLAL SLTFIRSTMP LVMAWRTIMA VLFVVTLIPL CRTSCLQKQS
     HWVEITALIL GAQALPVYLM TLMKGASRRS WPLNEGIMAV GLVSLLGSAL LKNDVPLAGP
     MVAGGLLLAA YVMSGSSADL SLEKAANVQW DEMADITGSS PIIEVKQDED GSFSIRDVEE
     TNMITLLVKL ALITVSGLYP LAIPVTMTLW YMWQVKTQRS GALWDVPSPA ATKKAALSEG
     VYRIMQRGLF GKTQVGVGIH MEGVFHTMWH VTRGSVICHE TGRLEPSWAD VRNDMISYGG
     GWRLGDKWDK EEDVQVLAIE PGKNPKHVQT KPGLFKTLTG EIGAVTLDFK PGTSGSPIIN
     RKGKVIGLYG NGVVTKSGDY VSAITQAERI GEPDYEVDED IFRKKRLTIM DLHPGAGKTK
     RILPSIVREA LKRRLRTLIL APTRVVAAEM EEALRGLPIR YQTPAVKSEH TGREIVDLMC
     HATFTTRLLS STRVPNYNLI VMDEAHFTDP SSVAARGYIS TRVEMGEAAA IFMTATPPGA
     TDPFPQSNSP IEDIEREIPE RSWNTGFDWI TDYQGKTVWF VPSIKAGNDI ANCLRKSGKK
     VIQLSRKTFD TEYPKTKLTD WDFVVTTDIS EMGANFRAGR VIDPRRCLKP VILPDGPERV
     ILAGPIPVTP ASAAQRRGRI GRNPAQEDDQ YVFSGDPLKN DEDHAHWTEA KMLLDNIYTP
     EGIIPTLFGP EREKTQAIDG EFRLRGEQRK TFVELMRRGD LPVWLSYKVA SAGISYKDRE
     WCFTGERNNQ ILEENMEVEI WTREGEKKKL RPRWLDARVY ADPMALKDFK EFASGRKSIT
     LDILTEIASL PTYLSSRAKL ALDNIVMLHT TERGGRAYQH ALNELPESLE TLMLVALLGA
     MTAGIFLFFM QGKGIGKLSM GLITIAVASG LLWVAEIQPQ WIAASIILEF FLMVLLIPEP
     EKQRTPQDNQ LIYVILTILT IIGLIAANEM GLIEKTKTDF GFYQVKTETT ILDVDLRPAS
     AWTLYAVATT ILTPMLRHTI ENTSANLSLA AIANQAAVLM GLGKGWPLHR MDLGVPLLAM
     GCYSQVNPTT LTASLVMLLV HYAIIGPGLQ AKATREAQKR TAAGIMKNPT VDGITVIDLE
     PISYDPKFEK QLGQVMLLVL CAGQLLLMRT TWAFCEVLTL ATGPILTLWE GNPGRFWNTT
     IAVSTANIFR GSYLAGAGLA FSLIKNAQTP RRGTGTTGET LGEKWKRQLN SLDRKEFEEY
     KRSGILEVDR TEAKSALKDG SKIKHAVSRG SSKIRWIVER GMVKPKGKVV DLGCGRGGWS
     YYMATLKNVT EVKGYTKGGP GHEEPIPMAT YGWNLVKLHS GVDVFYKPTE QVDTLLCDIG
     ESSSNPTIEE GRTLRVLKMV EPWLSSKPEF CIKVLNPYMP TVIEELEKLQ RKHGGNLVRC
     PLSRNSTHEM YWVSGASGNI VSSVNTTSKM LLNRFTTRHR KPTYEKDVDL GAGTRSVSTE
     TEKPDMTIIG RRLQRLQEEH KETWHYDQEN PYRTWAYHGS YEAPSTGSAS SMVNGVVKLL
     TKPWDVIPMV TQLAMTDTTP FGQQRVFKEK VDTRTPQPKP GTRMVMTTTA NWLWALLGKK
     KNPRLCTREE FISKVRSNAA IGAVFQEEQG WTSASEAVND SRFWELVDKE RALHQEGKCE
     SCVYNMMGKR EKKLGEFGRA KGSRAIWYMW LGARFLEFEA LGFLNEDHWF GRENSWSGVE
     GEGLHRLGYI LEEIDKKDGD LMYADDTAGW DTRITEDDLQ NEELITEQMA PHHKILAKAI
     FKLTYQNKVV KVLRPTPRGA VMDIISRKDQ RGSGQVGTYG LNTFTNMEVQ LIRQMEAEGV
     ITQDDMQNPK GLKERVEKWL KECGVDRLKR MAISGDDCVV KPLDERFGTS LLFLNDMGKV
     RKDIPQWEPS KGWKNWQEVP FCSHHFHKIF MKDGRSLVVP CRNQDELIGR ARISQGAGWS
     LRETACLGKA YAQMWSLMYF HRRDLRLASM AICSAVPTEW FPTSRTTWSI HAHHQWMTTE
     DMLKVWNRVW IEDNPNMTDK TPVHSWEDIP YLGKREDLWC GSLIGLSSRA TWAKNIHTAI
     TQVRNLIGKE EYVDYMPVMK RYSAPSESEG VL
//