JMJ25_ARATH
ID JMJ25_ARATH Reviewed; 1027 AA.
AC Q9SSE9;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Lysine-specific demethylase JMJ25 {ECO:0000303|PubMed:18713399};
DE EC=1.14.11.65 {ECO:0000269|PubMed:18218897};
DE AltName: Full=Jumonji domain-containing protein 25 {ECO:0000303|PubMed:18713399};
DE Short=AtJMJ25 {ECO:0000303|PubMed:18713399};
DE Short=Protein JUMONJI 25 {ECO:0000303|PubMed:18713399};
DE AltName: Full=Lysine-specific histone demethylase JMJ25 {ECO:0000303|PubMed:18713399};
DE AltName: Full=Protein INCREASE IN BONSAI METHYLATION 1 {ECO:0000303|PubMed:22580822};
DE AltName: Full=[histone H3]-dimethyl-L-lysine(9) monodemethylase JMJ25 {ECO:0000305};
GN Name=JMJ25 {ECO:0000303|PubMed:18713399};
GN Synonyms=IBM1 {ECO:0000303|PubMed:22580822};
GN OrderedLocusNames=At3g07610 {ECO:0000312|Araport:AT3G07610};
GN ORFNames=MLP3.6 {ECO:0000312|EMBL:AAF13079.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
RX PubMed=18713399; DOI=10.1111/j.1744-7909.2008.00692.x;
RA Lu F., Li G., Cui X., Liu C., Wang X.-J., Cao X.;
RT "Comparative analysis of JmjC domain-containing proteins reveals the
RT potential histone demethylases in Arabidopsis and rice.";
RL J. Integr. Plant Biol. 50:886-896(2008).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP GLY-672.
RX PubMed=18218897; DOI=10.1126/science.1150987;
RA Saze H., Shiraishi A., Miura A., Kakutani T.;
RT "Control of genic DNA methylation by a jmjC domain-containing protein in
RT Arabidopsis thaliana.";
RL Science 319:462-465(2008).
RN [5]
RP FUNCTION.
RX PubMed=19262562; DOI=10.1038/emboj.2009.59;
RA Miura A., Nakamura M., Inagaki S., Kobayashi A., Saze H., Kakutani T.;
RT "An Arabidopsis jmjC domain protein protects transcribed genes from DNA
RT methylation at CHG sites.";
RL EMBO J. 28:1078-1086(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-679 AND ASP-681.
RX PubMed=20834229; DOI=10.1038/emboj.2010.227;
RA Inagaki S., Miura-Kamio A., Nakamura Y., Lu F., Cui X., Cao X., Kimura H.,
RA Saze H., Kakutani T.;
RT "Autocatalytic differentiation of epigenetic modifications within the
RT Arabidopsis genome.";
RL EMBO J. 29:3496-3506(2010).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22580822; DOI=10.1038/emboj.2012.141;
RA Rigal M., Kevei Z., Pelissier T., Mathieu O.;
RT "DNA methylation in an intron of the IBM1 histone demethylase gene
RT stabilizes chromatin modification patterns.";
RL EMBO J. 31:2981-2993(2012).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22772985; DOI=10.1093/nar/gks647;
RA Fan D., Dai Y., Wang X., Wang Z., He H., Yang H., Cao Y., Deng X.W., Ma L.;
RT "IBM1, a JmjC domain-containing histone demethylase, is involved in the
RT regulation of RNA-directed DNA methylation through the epigenetic control
RT of RDR2 and DCL3 expression in Arabidopsis.";
RL Nucleic Acids Res. 40:8905-8916(2012).
RN [9]
RP INDUCTION BY ASI1.
RC STRAIN=cv. Columbia;
RX PubMed=24003136; DOI=10.1073/pnas.1315399110;
RA Wang X., Duan C.-G., Tang K., Wang B., Zhang H., Lei M., Lu K.,
RA Mangrauthia S.K., Wang P., Zhu G., Zhao Y., Zhu J.-K.;
RT "RNA-binding protein regulates plant DNA methylation by controlling mRNA
RT processing at the intronic heterochromatin-containing gene IBM1.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:15467-15472(2013).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY ASI1.
RX PubMed=24404182; DOI=10.1371/journal.pone.0084687;
RA Coustham V., Vlad D., Deremetz A., Gy I., Cubillos F.A., Kerdaffrec E.,
RA Loudet O., Bouche N.;
RT "SHOOT GROWTH1 maintains Arabidopsis epigenomes by regulating IBM1.";
RL PLoS ONE 9:E84687-E84687(2014).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=27697902; DOI=10.1242/dev.129932;
RA Wang Y., Xue X., Zhu J.-K., Dong J.;
RT "Demethylation of ERECTA receptor genes by IBM1 histone demethylase affects
RT stomatal development.";
RL Development 143:4452-4461(2016).
RN [12]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=28400174; DOI=10.1016/j.gep.2017.04.001;
RA Audonnet L., Shen Y., Zhou D.-X.;
RT "JMJ24 antagonizes histone H3K9 demethylase IBM1/JMJ25 function and
RT interacts with RNAi pathways for gene silencing.";
RL Gene Expr. Patterns 25:1-7(2017).
RN [13]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=33986281; DOI=10.1038/s41467-021-22995-3;
RA Butel N., Yu A., Le Masson I., Borges F., Elmayan T., Taochy C.,
RA Gursanscky N.R., Cao J., Bi S., Sawyer A., Carroll B.J., Vaucheret H.;
RT "Contrasting epigenetic control of transgenes and endogenous genes promotes
RT post-transcriptional transgene silencing in Arabidopsis.";
RL Nat. Commun. 12:2787-2787(2021).
CC -!- FUNCTION: Histone demethylase that demethylates 'Lys-9' (H3K9me) of
CC histone H3 with a specific activity for H3K9me2 and H3K9me1. No
CC activity on H3K9me3, H3K4me3/2/1, H3K27me3/2/1 and H3K36me3/2/1.
CC Counteracts the DNA methylation of endogenous genes (PubMed:33986281).
CC Involved in the control of several developmental processes by
CC protecting genes from silencing. Demethylates H3K9me2 in the promoter
CC regions of RDR2 and DCL3 and mediates the repression of ectopic non-CpG
CC methylation at RDR2, DCL3 and APC13 loci (PubMed:24404182). Protects
CC also a large number of transcribed genes from non-CpG methylation. May
CC regulate gene expression via a pathway involving indirect silencing of
CC gene expression through small RNA-directed DNA methylation (RdDM)-
CC directed repression. Modulates stomatal development by regulating the
CC methylation-mediated silencing of ERECTA receptor genes (e.g. ER, ERL1
CC and ERL2) and preventing cell divisions (PubMed:27697902).
CC {ECO:0000269|PubMed:18218897, ECO:0000269|PubMed:19262562,
CC ECO:0000269|PubMed:20834229, ECO:0000269|PubMed:22580822,
CC ECO:0000269|PubMed:22772985, ECO:0000269|PubMed:24404182,
CC ECO:0000269|PubMed:27697902, ECO:0000269|PubMed:33986281}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] +
CC O2 = CO2 + formaldehyde + N(6)-methyl-L-lysyl(9)-[histone H3] +
CC succinate; Xref=Rhea:RHEA:60192, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC COMP:15542, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929,
CC ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:18218897};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60193;
CC Evidence={ECO:0000269|PubMed:18218897};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(6)-methyl-L-lysyl(9)-[histone H3] + O2 =
CC CO2 + formaldehyde + L-lysyl(9)-[histone H3] + succinate;
CC Xref=Rhea:RHEA:60196, Rhea:RHEA-COMP:15542, Rhea:RHEA-COMP:15546,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61929; Evidence={ECO:0000269|PubMed:18218897};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60197;
CC Evidence={ECO:0000269|PubMed:18218897};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(9)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:60188, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.65;
CC Evidence={ECO:0000269|PubMed:18218897};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60189;
CC Evidence={ECO:0000269|PubMed:18218897};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q8GUI6};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8GUI6};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:20834229, ECO:0000269|PubMed:22772985}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SSE9-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in inflorescences, roots, siliques,
CC leaves and stems. {ECO:0000269|PubMed:18713399}.
CC -!- INDUCTION: Promoted by the RNA-binding protein ASI1 via its association
CC with an intronic heterochromatic repeat element and epigenetic
CC regulation. {ECO:0000269|PubMed:24003136, ECO:0000269|PubMed:24404182}.
CC -!- DISRUPTION PHENOTYPE: Small and narrow leaves, arrest in flower
CC development, degenerated pollen grains and reduced fertility leading to
CC few viable seeds. Non-CpG hypermethylation at APC13, RDR2 and DCL3 loci
CC (PubMed:24404182). Overproduction of stomatal lineage cells due to
CC increased cell divisions and associated with DNA hypermethylation and
CC silencing of ERECTA receptor genes such as ER, ERL1 and ERL2
CC (PubMed:27697902). Growth defects are partially complemented by the
CC loss of JMJ24 mostly at vegetative stage, but the double mutant jmj24-3
CC ibm1-4 has synergistic effect on root growth (PubMed:28400174). Broad
CC spectrum of up-regulated and down-regulated genes (PubMed:28400174).
CC {ECO:0000269|PubMed:18218897, ECO:0000269|PubMed:22580822,
CC ECO:0000269|PubMed:22772985, ECO:0000269|PubMed:24404182,
CC ECO:0000269|PubMed:27697902, ECO:0000269|PubMed:28400174}.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000305}.
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DR EMBL; AC009176; AAF13079.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74573.1; -; Genomic_DNA.
DR RefSeq; NP_187418.1; NM_111640.2. [Q9SSE9-1]
DR AlphaFoldDB; Q9SSE9; -.
DR SMR; Q9SSE9; -.
DR STRING; 3702.AT3G07610.3; -.
DR iPTMnet; Q9SSE9; -.
DR PaxDb; Q9SSE9; -.
DR ProteomicsDB; 232270; -. [Q9SSE9-1]
DR EnsemblPlants; AT3G07610.1; AT3G07610.1; AT3G07610. [Q9SSE9-1]
DR GeneID; 819952; -.
DR Gramene; AT3G07610.1; AT3G07610.1; AT3G07610. [Q9SSE9-1]
DR KEGG; ath:AT3G07610; -.
DR Araport; AT3G07610; -.
DR eggNOG; KOG1356; Eukaryota.
DR HOGENOM; CLU_001811_2_1_1; -.
DR PhylomeDB; Q9SSE9; -.
DR BRENDA; 1.14.11.65; 399.
DR PRO; PR:Q9SSE9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SSE9; baseline and differential.
DR Genevisible; Q9SSE9; AT.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0140683; F:histone H3-di/monomethyl-lysine-9 demethylase activity; IEA:RHEA.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0032776; P:DNA methylation on cytosine; IMP:UniProtKB.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IBA:GO_Central.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010440; P:stomatal lineage progression; IMP:UniProtKB.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR PANTHER; PTHR12549; PTHR12549; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Dioxygenase; Iron;
KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1027
FT /note="Lysine-specific demethylase JMJ25"
FT /id="PRO_0000429998"
FT DOMAIN 635..860
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 155..201
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 280..310
FT /note="B box-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 48..55
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 121..128
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 995..1002
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..935
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1000
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 679
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 681
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 828
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MUTAGEN 672
FT /note="G->E: In ibm1-1; growth and flowering defects, and
FT reduced fertility. Cytosine hypermethylation at the low-
FT copy APC13 locus."
FT /evidence="ECO:0000269|PubMed:18218897"
FT MUTAGEN 679
FT /note="H->A: Loss of activity on H3K9me2/1."
FT /evidence="ECO:0000269|PubMed:20834229"
FT MUTAGEN 681
FT /note="D->A: Loss of activity on H3K9me2/1."
FT /evidence="ECO:0000269|PubMed:20834229"
SQ SEQUENCE 1027 AA; 116253 MW; F46D22F2F066910F CRC64;
MDSVEEEGVV RVEEENGRGG LRRHRRVSTK LANYVDPPTD DEEDGGPKRK GKRGGNRAPK
KTPKKDEEMQ KNEIDEANRV TGLVKEKRAA TKILNRKDSI IEVGEASGSM PKEVKGIRIG
KRKGEIDGEI PTKPGKKPKT TVDPRIIGYR PDNMCHQCQK SDRIVERCQT CNSKRYCHPC
LDTWYPLIAK EDVAKKCMFC SSTCNCRACL RLDTKLKGIN SNLIVSEEEK VQASKFILQS
LLPHLKGIND EQVAEKEVEA KIYGLKFEEV RPQDAKAFPD ERLYCDICKT SIYDLHRNCK
SCSFDICLSC CLEIRNGKAL ACKEDVSWNY INRGLEYEHG QEGKVIEKPA NKLDDKLKDK
LDGKPDDKPK GKPKGRPKGK PDDKPKGKLK GKQDDKPDDK PDEKPVNTDH MKYPSLWKAN
EAGIITCCCG AGELVLKRLL PDGWISELVN RVEKTAEAGE LLNLPETVLE RCPCSNSDRH
IDIDSCNLLK AACREGSEDN YLYSPSVWDV QQDDLKHFQH HWVKGEPVIV RNVLEATSGL
SWEPMVMHRA CRQISHVQHG SLKDVVAVDC LDFCEVKVNL HEFFTGYTDG RYDRMGWPLV
LKLKDWPPAK VFKDNLPRHA EEFLCSLPLK HYTHPVNGPL NLAVKLPQNC LKPDMGPKTY
VASGFAQELG RGDSVTKLHC DMSDAVNILT HISEVPNMQP GIGNLKKKHA EQDLKELYSS
VANKEEMMEI LENSRQQVQN VETDDGALWD IFRREDIPKL ESYIEKHHKE FRHLYCCPVS
QVVHPIHDQN FYLTRYHIMK LKEEYGIEPW TFNQKLGDAV LIPVGCPHQV RNLKSCNKVA
LDFVSPENVS ECLRLTKQYR LLPPNHFAKE DKLGVKKMIV HAVDKALRDL SGEKSPEPEE
KKQNMRGPKK GAAKAVAKAL KDLSPSEKKS SEAAEEEISN GIVNAIDKGL KDLPPSEEKS
SEAKVEISNG IVSAMDKDLE HISSSEKKST EEEGVKRPNI VRTYERRKKL GSEVTNAYID
RLEMEKM
