ID   SETB1_DROME             Reviewed;        1262 AA.
AC   Q32KD2; Q29QW7; Q8IHC9; Q8MMD1; Q960X1; Q9W110;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=Histone-lysine N-methyltransferase eggless;
DE            EC=2.1.1.355;
DE   AltName: Full=SETDB1 homolog;
GN   Name=egg; ORFNames=CG12196;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 378-1262.
RC   STRAIN=Berkeley; TISSUE=Embryo, and Testis;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=17164421; DOI=10.1242/dev.02698;
RA   Clough E., Moon W., Wang S., Smith K., Hazelrigg T.;
RT   "Histone methylation is required for oogenesis in Drosophila.";
RL   Development 134:157-165(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND THR-217, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Histone methyltransferase that specifically trimethylates
CC       'Lys-9' of histone H3 in ovary. H3 'Lys-9' trimethylation represents a
CC       specific tag for epigenetic transcriptional repression by recruiting
CC       Su(var)205/HP1 to methylated histones. Plays a central role during
CC       oogenesis. {ECO:0000269|PubMed:17164421}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC         N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-
CC         COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355;
CC   -!- INTERACTION:
CC       Q32KD2; Q9W123: Pof; NbExp=2; IntAct=EBI-140830, EBI-155974;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17164421}. Chromosome
CC       {ECO:0000305|PubMed:17164421}.
CC   -!- TISSUE SPECIFICITY: Expressed in ovary (at protein level).
CC       {ECO:0000269|PubMed:17164421}.
CC   -!- DEVELOPMENTAL STAGE: Present most strongly at early stages of
CC       oogenesis, in germ cells in the germarium. Present in germ stem cells
CC       and dividing germline cyst cells. Weakly or not expressed in somatic
CC       cells at the tip of the germarium, including the terminal filament,
CC       inner sheath cells, or cap cells, but it is present at low levels in
CC       somatic cells in regions 2 and 3 of the germarium, including the
CC       prefollicular cells and the follicle cells of stage 1 egg chambers.
CC       Soon after egg chambers budd off the germarium, levels increase in the
CC       follicle cells. By mid-oogenesis it decreases in the nurse cells, while
CC       levels continued to increase in the follicle cells (at protein level).
CC       {ECO:0000269|PubMed:17164421}.
CC   -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are
CC       arranged in a triangular cluster; some of these Cys residues contribute
CC       to the binding of two zinc ions within the cluster. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Oogenesis arrests at early stages. This arrest is
CC       accompanied by reduced proliferation of somatic cells required for egg
CC       chamber formation, and by apoptosis in both germ and somatic cell
CC       populations. {ECO:0000269|PubMed:17164421}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. Histone-lysine methyltransferase family. Suvar3-9
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK93223.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAN71064.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=ABC86335.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AE013599; AAF47268.3; -; Genomic_DNA.
DR   EMBL; BT023947; ABB36451.1; -; mRNA.
DR   EMBL; BT024273; ABC86335.1; ALT_INIT; mRNA.
DR   EMBL; AY051799; AAK93223.1; ALT_INIT; mRNA.
DR   EMBL; BT001309; AAN71064.2; ALT_INIT; mRNA.
DR   RefSeq; NP_611966.3; NM_138122.5.
DR   PDB; 7UVE; X-ray; 2.30 A; A=444-700.
DR   PDB; 7UW8; X-ray; 2.50 A; A=444-700.
DR   PDBsum; 7UVE; -.
DR   PDBsum; 7UW8; -.
DR   AlphaFoldDB; Q32KD2; -.
DR   SMR; Q32KD2; -.
DR   BioGRID; 63532; 34.
DR   DIP; DIP-46503N; -.
DR   IntAct; Q32KD2; 8.
DR   STRING; 7227.FBpp0111689; -.
DR   iPTMnet; Q32KD2; -.
DR   PaxDb; 7227-FBpp0111689; -.
DR   DNASU; 37962; -.
DR   EnsemblMetazoa; FBtr0112777; FBpp0111689; FBgn0086908.
DR   GeneID; 37962; -.
DR   KEGG; dme:Dmel_CG12196; -.
DR   AGR; FB:FBgn0086908; -.
DR   CTD; 37962; -.
DR   FlyBase; FBgn0086908; egg.
DR   VEuPathDB; VectorBase:FBgn0086908; -.
DR   eggNOG; KOG1141; Eukaryota.
DR   GeneTree; ENSGT00940000169356; -.
DR   HOGENOM; CLU_003279_0_1_1; -.
DR   InParanoid; Q32KD2; -.
DR   OMA; LLCCDCE; -.
DR   OrthoDB; 2877903at2759; -.
DR   PhylomeDB; Q32KD2; -.
DR   BRENDA; 2.1.1.355; 1994.
DR   Reactome; R-DME-3214841; PKMTs methylate histone lysines.
DR   SignaLink; Q32KD2; -.
DR   BioGRID-ORCS; 37962; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 37962; -.
DR   PRO; PR:Q32KD2; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0086908; Expressed in eye disc (Drosophila) and 47 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046974; F:histone H3K9 methyltransferase activity; IDA:FlyBase.
DR   GO; GO:0140949; F:histone H3K9 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0140947; F:histone H3K9me2 methyltransferase activity; IDA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0040029; P:epigenetic regulation of gene expression; IMP:FlyBase.
DR   GO; GO:0048132; P:female germ-line stem cell asymmetric division; IDA:FlyBase.
DR   GO; GO:0031507; P:heterochromatin formation; IMP:FlyBase.
DR   GO; GO:0070828; P:heterochromatin organization; IMP:FlyBase.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0010629; P:negative regulation of gene expression; IGI:FlyBase.
DR   GO; GO:0048477; P:oogenesis; IDA:FlyBase.
DR   GO; GO:0140966; P:piRNA-mediated heterochromatin formation; IMP:FlyBase.
DR   GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin formation; IMP:FlyBase.
DR   CDD; cd01395; HMT_MBD; 1.
DR   CDD; cd10517; SET_SETDB1; 1.
DR   CDD; cd20382; Tudor_SETDB1_rpt1; 1.
DR   CDD; cd21181; Tudor_SETDB1_rpt2; 1.
DR   Gene3D; 2.30.30.140; -; 2.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR016177; DNA-bd_dom_sf.
DR   InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR047232; SETDB1/2-like_MBD.
DR   InterPro; IPR041292; Tudor_4.
DR   InterPro; IPR041291; TUDOR_5.
DR   PANTHER; PTHR46024; HISTONE-LYSINE N-METHYLTRANSFERASE EGGLESS; 1.
DR   PANTHER; PTHR46024:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE EGGLESS; 1.
DR   Pfam; PF01429; MBD; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF18358; Tudor_4; 1.
DR   Pfam; PF18359; Tudor_5; 1.
DR   SMART; SM00391; MBD; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF54171; DNA-binding domain; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50982; MBD; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS50280; SET; 1.
DR   Genevisible; Q32KD2; DM.
PE   1: Evidence at protein level;
KW   3D-structure; Chromatin regulator; Chromosome; Coiled coil;
KW   Developmental protein; Differentiation; Metal-binding; Methyltransferase;
KW   Nucleus; Oogenesis; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc.
FT   CHAIN           1..1262
FT                   /note="Histone-lysine N-methyltransferase eggless"
FT                   /id="PRO_0000281822"
FT   DOMAIN          529..602
FT                   /note="Tudor 1"
FT   DOMAIN          629..686
FT                   /note="Tudor 2"
FT   DOMAIN          818..884
FT                   /note="MBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT   DOMAIN          946..1018
FT                   /note="Pre-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT   DOMAIN          1021..1237
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   DOMAIN          1246..1262
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT   REGION          1..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          743..764
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1086..1148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          353..420
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..183
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1093..1109
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1127..1148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         948
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         948
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         950
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         954
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         954
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         960
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         962
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         1000
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         1000
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         1004
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         1006
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         1010
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         1031..1033
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         1069
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         1071
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         1191
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         1194..1195
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         1197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         1250
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         1252
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         1257
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         215
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         217
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   STRAND          466..473
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   STRAND          478..490
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   STRAND          496..506
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   STRAND          512..515
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   HELIX           517..519
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   STRAND          520..524
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   STRAND          535..540
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   STRAND          557..565
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   HELIX           569..571
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   STRAND          575..579
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   STRAND          584..587
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   HELIX           589..591
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   STRAND          592..596
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   HELIX           602..605
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   TURN            608..610
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   HELIX           611..619
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   STRAND          635..640
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   STRAND          643..653
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   STRAND          656..661
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   STRAND          668..672
FT                   /evidence="ECO:0007829|PDB:7UVE"
FT   HELIX           679..686
FT                   /evidence="ECO:0007829|PDB:7UVE"
SQ   SEQUENCE   1262 AA;  141946 MW;  A89DFF1CC6FCED1C CRC64;
     MSGQPTAVDC LESSGSTVED VQETPASREK SYGLPVRKGE NSLESPAEQA AKDVEIEELT
     HSEAIAATGS TRKQCPYGGK APDEPGKLAD ESEDRKGENT KAIASSPVLV AVDSDSSVEL
     IESPVKFSSA NESEKDPPKP DAVNEAAAKE AEEMTDSSIS SPTSESFPEK DEKTNKENEQ
     EPPGMEVDQD VEESISRPAE EYKIENTLKG HKRISLTEIE EHKIVDKKDD VLEVELEKGT
     APKAAEDEKL NALLSDGDVF YDKECVNCNC TKLHKQYVLA NMATLNFYQV LRKSSKQQFL
     CMGCHDTAMD LYEEYAGQLM AKQPLLLKDF HQDHADFVAL DSSDEEEEEK QPEKSDFSKN
     KLQLIEDELD DAIKNVLNKV DFTAQLSWSK TILQAKADHL ERQFALADVE LEKVQTTADK
     MHCALYNSCP VAHKHLPTLD IEPSDYVHEV PPPGEIVRPP IQLGETYYAV KNKAIASWVS
     IKVIEFTEST AINGNTMKSY KIRYLNTPYQ MIKTVTAKHI AYFEPPPVRL TIGTRVIAYF
     DGTTLSRGKD KGVVQSAFYP GIIAEPLKQA NRYRYLIFYD DGYTQYVPHR DVRLVCQASE
     KVWEDVHAAS RDFIQKYVEK YSVDRPMVQC TRGQSMTTES NGTWLYARVI DIDCSLVLMQ
     FEGDKNHTEW IYRGSLRLGP VFRETQNNMN SSSAQQLRVP RRTEPFIRYT KEMESSSKVN
     QQMRAFARKS SASAQNNALA AASSAATPAG GRTNAGGVST SNSASAVRHL NNSTIYVDDE
     NRPKGHVVYF TAKRNLPPKM YKCHECSPNC LFKIVHRLDS YSPLAKPLLS GWERLVMRQK
     TKKSVVYKGP CGKSLRSLAE VHRYLRATEN VLNVDNFDFT PDLKCLAEYS IDPSIVKDTD
     ISKGQEKMAI PLVNYYDNTL PPPCTYAKQR IPTEGVHLNL DEEFLLCCDC EDDCSDKSKC
     ACWQLTVAGV RYCNPKKPIE EIGYQYKRLH EHVPTGIYEC NSRCKCKKNC LNRVVQFSLE
     MKLQVFKTSN RGWGLRCVND IPKGAFICIY AGHLLTETMA NEGGQDAGDE YFADLDYIEV
     AEQLKEGYES EVDHSDPDAE EDNGGPDAED DDDFRPNYHY QRKIKRSSRS GSTQNSSTQS
     SELDSQERAV INFNPNADLD ETVRENSVRR LFGKDEAPYI MDAKTTGNLG RYFNHSCSPN
     LFVQNVFVDT HDLRFPWVAF FSAAHIRSGT ELTWNYNYEV GVVPGKVLYC QCGAPNCRLR
     LL
//