CHR35_ARATH
ID CHR35_ARATH Reviewed; 888 AA.
AC Q9SIW2;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protein CHROMATIN REMODELING 35 {ECO:0000303|PubMed:16547115, ECO:0000303|PubMed:23770592};
DE AltName: Full=Protein DEFECTIVE IN MERISTEM SILENCING 1 {ECO:0000303|PubMed:18425128};
DE AltName: Full=Protein DEFECTIVE IN RNA-DIRECTED DNA METHYLATION 1 {ECO:0000303|PubMed:15120073};
GN Name=DRD1 {ECO:0000303|PubMed:15120073};
GN Synonyms=CHR35 {ECO:0000303|PubMed:16547115, ECO:0000303|PubMed:23770592},
GN DMS1 {ECO:0000303|PubMed:18425128};
GN OrderedLocusNames=At2g16390 {ECO:0000312|Araport:AT2G16390};
GN ORFNames=F16F14.11 {ECO:0000312|EMBL:AEC06492.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-357; GLY-494;
RP ARG-807 AND ARG-810.
RC STRAIN=cv. Columbia;
RX PubMed=15120073; DOI=10.1016/j.cub.2004.04.037;
RA Kanno T., Mette M.F., Kreil D.P., Aufsatz W., Matzke M., Matzke A.J.M.;
RT "Involvement of putative SNF2 chromatin remodeling protein DRD1 in RNA-
RT directed DNA methylation.";
RL Curr. Biol. 14:801-805(2004).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=15947783; DOI=10.1038/sj.embor.7400446;
RA Kanno T., Aufsatz W., Jaligot E., Mette M.F., Matzke M., Matzke A.J.M.;
RT "A SNF2-like protein facilitates dynamic control of DNA methylation.";
RL EMBO Rep. 6:649-655(2005).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=15924141; DOI=10.1038/ng1580;
RA Kanno T., Huettel B., Mette M.F., Aufsatz W., Jaligot E., Daxinger L.,
RA Kreil D.P., Matzke M., Matzke A.J.M.;
RT "Atypical RNA polymerase subunits required for RNA-directed DNA
RT methylation.";
RL Nat. Genet. 37:761-765(2005).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16839878; DOI=10.1016/j.cell.2006.05.031;
RA Pontes O., Li C.F., Nunes P.C., Haag J., Ream T., Vitins A., Jacobsen S.E.,
RA Pikaard C.S.;
RT "The Arabidopsis chromatin-modifying nuclear siRNA pathway involves a
RT nucleolar RNA processing center.";
RL Cell 126:79-92(2006).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=16724114; DOI=10.1038/sj.emboj.7601150;
RA Huettel B., Kanno T., Daxinger L., Aufsatz W., Matzke A.J.M., Matzke M.;
RT "Endogenous targets of RNA-directed DNA methylation and Pol IV in
RT Arabidopsis.";
RL EMBO J. 25:2828-2836(2006).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16547115; DOI=10.1534/genetics.105.051664;
RA Shaked H., Avivi-Ragolsky N., Levy A.A.;
RT "Involvement of the Arabidopsis SWI2/SNF2 chromatin remodeling gene family
RT in DNA damage response and recombination.";
RL Genetics 173:985-994(2006).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16741558; DOI=10.1371/journal.pgen.0020083;
RA Chan S.W.-L., Henderson I.R., Zhang X., Shah G., Chien J.S.-C.,
RA Jacobsen S.E.;
RT "RNAi, DRD1, and histone methylation actively target developmentally
RT important non-CG DNA methylation in arabidopsis.";
RL PLoS Genet. 2:E83-E83(2006).
RN [10]
RP REVIEW.
RX PubMed=17381327; DOI=10.1101/sqb.2006.71.028;
RA Matzke M., Kanno T., Huettel B., Daxinger L., Matzke A.J.M.;
RT "RNA-directed DNA methylation and Pol IVb in Arabidopsis.";
RL Cold Spring Harb. Symp. Quant. Biol. 71:449-459(2006).
RN [11]
RP REVIEW.
RX PubMed=17381329; DOI=10.1101/sqb.2006.71.046;
RA Pikaard C.S.;
RT "Cell biology of the Arabidopsis nuclear siRNA pathway for RNA-directed
RT chromatin modification.";
RL Cold Spring Harb. Symp. Quant. Biol. 71:473-480(2006).
RN [12]
RP REVIEW.
RX PubMed=17449119; DOI=10.1016/j.bbaexp.2007.03.001;
RA Huettel B., Kanno T., Daxinger L., Bucher E., van der Winden J.,
RA Matzke A.J.M., Matzke M.;
RT "RNA-directed DNA methylation mediated by DRD1 and Pol IVb: a versatile
RT pathway for transcriptional gene silencing in plants.";
RL Biochim. Biophys. Acta 1769:358-374(2007).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19013275; DOI=10.1016/j.cell.2008.09.035;
RA Wierzbicki A.T., Haag J.R., Pikaard C.S.;
RT "Noncoding transcription by RNA polymerase Pol IVb/Pol V mediates
RT transcriptional silencing of overlapping and adjacent genes.";
RL Cell 135:635-648(2008).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18425128; DOI=10.1038/ng.119;
RA Kanno T., Bucher E., Daxinger L., Huettel B., Boehmdorfer G., Gregor W.,
RA Kreil D.P., Matzke M., Matzke A.J.;
RT "A structural-maintenance-of-chromosomes hinge domain-containing protein is
RT required for RNA-directed DNA methylation.";
RL Nat. Genet. 40:670-675(2008).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19204117; DOI=10.1101/gad.1765209;
RA He X.-J., Hsu Y.-F., Pontes O., Zhu J., Lu J., Bressan R.A., Pikaard C.,
RA Wang C.-S., Zhu J.-K.;
RT "NRPD4, a protein related to the RPB4 subunit of RNA polymerase II, is a
RT component of RNA polymerases IV and V and is required for RNA-directed DNA
RT methylation.";
RL Genes Dev. 23:318-330(2009).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19825647; DOI=10.1093/mp/ssp017;
RA Luo C., Durgin B.G., Watanabe N., Lam E.;
RT "Defining the functional network of epigenetic regulators in Arabidopsis
RT thaliana.";
RL Mol. Plant 2:661-674(2009).
RN [17]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=19825650; DOI=10.1093/mp/ssp006;
RA Pontes O., Costa-Nunes P., Vithayathil P., Pikaard C.S.;
RT "RNA polymerase V functions in Arabidopsis interphase heterochromatin
RT organization independently of the 24-nt siRNA-directed DNA methylation
RT pathway.";
RL Mol. Plant 2:700-710(2009).
RN [18]
RP SUBUNIT.
RX PubMed=20409711; DOI=10.1016/j.cub.2010.03.062;
RA Law J.A., Ausin I., Johnson L.M., Vashisht A.A., Zhu J.-K.,
RA Wohlschlegel J.A., Jacobsen S.E.;
RT "A protein complex required for polymerase V transcripts and RNA-directed
RT DNA methylation in Arabidopsis.";
RL Curr. Biol. 20:951-956(2010).
RN [19]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21771120; DOI=10.1111/j.1365-313x.2011.04714.x;
RA Dong L., Liu M., Fang Y.-Y., Zhao J.-H., He X.-F., Ying X.-B., Zhang Y.-Y.,
RA Xie Q., Chua N.-H., Guo H.-S.;
RT "DRD1-Pol V-dependent self-silencing of an exogenous silencer restricts the
RT non-cell autonomous silencing of an endogenous target gene.";
RL Plant J. 68:633-645(2011).
RN [20]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=22242006; DOI=10.1371/journal.pgen.1002434;
RA Lopez A., Ramirez V., Garcia-Andrade J., Flors V., Vera P.;
RT "The RNA silencing enzyme RNA polymerase v is required for plant
RT immunity.";
RL PLoS Genet. 7:E1002434-E1002434(2011).
RN [21]
RP REVIEW.
RX PubMed=23567894; DOI=10.1101/sqb.2013.77.014803;
RA Pikaard C.S., Haag J.R., Pontes O.M., Blevins T., Cocklin R.;
RT "A transcription fork model for Pol IV and Pol V-dependent RNA-directed DNA
RT methylation.";
RL Cold Spring Harb. Symp. Quant. Biol. 77:205-212(2012).
RN [22]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22647529; DOI=10.4161/epi.20290;
RA Lee T.F., Gurazada S.G., Zhai J., Li S., Simon S.A., Matzke M.A., Chen X.,
RA Meyers B.C.;
RT "RNA polymerase V-dependent small RNAs in Arabidopsis originate from small,
RT intergenic loci including most SINE repeats.";
RL Epigenetics 7:781-795(2012).
RN [23]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
RX PubMed=22864289; DOI=10.1038/nsmb.2354;
RA Zhong X., Hale C.J., Law J.A., Johnson L.M., Feng S., Tu A., Jacobsen S.E.;
RT "DDR complex facilitates global association of RNA polymerase V to
RT promoters and evolutionarily young transposons.";
RL Nat. Struct. Mol. Biol. 19:870-875(2012).
RN [24]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=23540698; DOI=10.1016/j.cell.2013.02.033;
RA Zemach A., Kim M.Y., Hsieh P.-H., Coleman-Derr D., Eshed-Williams L.,
RA Thao K., Harmer S.L., Zilberman D.;
RT "The Arabidopsis nucleosome remodeler DDM1 allows DNA methyltransferases to
RT access H1-containing heterochromatin.";
RL Cell 153:193-205(2013).
RN [25]
RP GENE FAMILY.
RX PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA Xu R., Zhang S., Huang J., Zheng C.;
RT "Genome-wide comparative in silico analysis of the RNA helicase gene family
RT in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza
RT sativa.";
RL PLoS ONE 8:E78982-E78982(2013).
RN [26]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=23770592; DOI=10.1016/j.plaphy.2013.05.001;
RA Hu Y., Zhu N., Wang X., Yi Q., Zhu D., Lai Y., Zhao Y.;
RT "Analysis of rice Snf2 family proteins and their potential roles in
RT epigenetic regulation.";
RL Plant Physiol. Biochem. 70:33-42(2013).
RN [27]
RP INTERACTION WITH SUVH2.
RX PubMed=24463519; DOI=10.1038/nature12931;
RA Johnson L.M., Du J., Hale C.J., Bischof S., Feng S., Chodavarapu R.K.,
RA Zhong X., Marson G., Pellegrini M., Segal D.J., Patel D.J., Jacobsen S.E.;
RT "SRA- and SET-domain-containing proteins link RNA polymerase V occupancy to
RT DNA methylation.";
RL Nature 507:124-128(2014).
RN [28]
RP REVIEW.
RX PubMed=24498436; DOI=10.1371/journal.pone.0088190;
RA Sasaki T., Lorkovic Z.J., Liang S.-C., Matzke A.J.M., Matzke M.;
RT "The ability to form homodimers is essential for RDM1 to function in RNA-
RT directed DNA methylation.";
RL PLoS ONE 9:E88190-E88190(2014).
RN [29]
RP INTERACTION WITH SUVH2.
RC STRAIN=cv. Columbia;
RX PubMed=24465213; DOI=10.1371/journal.pgen.1003948;
RA Liu Z.-W., Shao C.-R., Zhang C.-J., Zhou J.-X., Zhang S.-W., Li L.,
RA Chen S., Huang H.-W., Cai T., He X.-J.;
RT "The SET domain proteins SUVH2 and SUVH9 are required for Pol V occupancy
RT at RNA-directed DNA methylation loci.";
RL PLoS Genet. 10:E1003948-E1003948(2014).
CC -!- FUNCTION: Subunit of the chromatin-remodeling complex (DDR complex)
CC that mediates RNA polymerases IV and V (Pol IV and Pol V) recruitment
CC to chromatin (PubMed:19013275, PubMed:22864289). Cooperates with Pol IV
CC and Pol V to regulates RNA- and RNAi- (RNA interference) directed non-
CC CpG de novo DNA methylation on cytosine of genes targeted for silencing
CC and enhancers, also known as siRNA-directed DNA methylation (RdDM),
CC thus leading to epigenetic modification of the genome and
CC promoting/maintaining heterochromatin (PubMed:15120073,
CC PubMed:15947783, PubMed:15924141, PubMed:16724114, PubMed:16741558,
CC PubMed:19204117, PubMed:19825647, PubMed:22647529, PubMed:18425128). In
CC collaboration with Pol V, mediates/maintains, in cis, methylation-
CC associated self-silencing of exogenous transgene transcribing inverted-
CC repeat (exo-IR) silencer (exo-Pdsi) to restrain exo-IR dsRNA
CC accumulation and subsequent inappropriate silencing of active protein-
CC coding genes (e.g. PDS) by exo-IR-derivating 24-nt siRNAs
CC (PubMed:21771120). Also required to mediate loss of CpG methylation
CC when the silencing inducer is withdrawn (PubMed:15947783). Required for
CC the maintenance of retrotransposon large terminal repeats (LTRs) and
CC transposable elements (TE) edges silencing mediated by cytosine
CC methylation (PubMed:16724114, PubMed:23540698). Required for
CC transcriptional repression of specific classes of pericentromeric 180-
CC bp repeats by promoting condensation and histone H3 lysine 9
CC dimethylation (H3K9me2) at chromocenters (PubMed:19825650). Required
CC for basal resistance against the necrotrophic fungal pathogen
CC Plectosphaerella cucumerina (PubMed:22242006).
CC {ECO:0000269|PubMed:15120073, ECO:0000269|PubMed:15924141,
CC ECO:0000269|PubMed:15947783, ECO:0000269|PubMed:16724114,
CC ECO:0000269|PubMed:16741558, ECO:0000269|PubMed:18425128,
CC ECO:0000269|PubMed:19013275, ECO:0000269|PubMed:19204117,
CC ECO:0000269|PubMed:19825647, ECO:0000269|PubMed:19825650,
CC ECO:0000269|PubMed:21771120, ECO:0000269|PubMed:22242006,
CC ECO:0000269|PubMed:22647529, ECO:0000269|PubMed:22864289,
CC ECO:0000269|PubMed:23540698}.
CC -!- SUBUNIT: Part of the chromatin-remodeling complex (DDR complex) that
CC contains at least DRD1, DMS3 and RDM1. The DDR complex
CC recruits/activates the RNA polymerases V and acts during siRNA-directed
CC DNA methylation (RdDM) (PubMed:20409711, PubMed:22864289). Interacts
CC with SUVH2 (PubMed:24463519, PubMed:24465213).
CC {ECO:0000269|PubMed:20409711, ECO:0000269|PubMed:22864289,
CC ECO:0000269|PubMed:24463519, ECO:0000269|PubMed:24465213}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:16839878}. Note=Excluded from the nucleolus.
CC Colocalizes with endogenous repeat loci. {ECO:0000269|PubMed:16839878}.
CC -!- DISRUPTION PHENOTYPE: Reduced association of NRPE1 with chromatin,
CC leading to altered chromatin binding of the DDR complex
CC (PubMed:19013275, PubMed:22864289). Defective in RNA-directed non-CpG
CC DNA methylation resulting in reactivation of silenced genes and
CC enhancers, whereas methylation of centromeric and rDNA repeats is
CC unaffected (PubMed:15120073, PubMed:15947783, PubMed:15924141,
CC PubMed:16741558, PubMed:19825647, PubMed:18425128). Reduced
CC accumulation of 24-nt siRNAs and reduced DNA methylation of siRNA-
CC directed DNA methylation (RdDM) target loci (PubMed:19204117,
CC PubMed:22647529). Increase in CpG DNA methylation leading to abnormal
CC maintenance of some silenced genes (PubMed:15947783). Derepression of
CC solo retrotransposon large terminal repeats (LTRs) and of transposable
CC elements (TE) edges accompanied by reduced cytosine methylation and
CC transcriptional up-regulation of neighboring sequences, and associated
CC with euchromatic histone modifications but little or no H3K9
CC dimethylation. By contrast, LTRs of retrotransposons that remain silent
CC in disrupted plants despite reduced cytosine methylation lack
CC euchromatic marks and have H3K9 dimethylation (PubMed:16724114,
CC PubMed:23540698). Decondensation of the major pericentromeric repeats
CC and depletion of the heterochromatic mark histone H3 lysine 9
CC dimethylation (H3K9me2) at chromocenters, leading to transcriptional
CC reactivation of specific classes of pericentromeric 180-bp repeats and
CC reduced heterochromatin (PubMed:19825650). Relieved exo-Pdsi self-
CC silencing resulting in accumulation of dsRNA and Pdsi-derivating 21-nt
CC mobile siRNAs which increase non-cell-autonomous silencing of endo-PDS
CC in neighboring cells (PubMed:21771120). Increases susceptibility to the
CC necrotrophic fungal pathogen Plectosphaerella cucumerina
CC (PubMed:22242006). {ECO:0000269|PubMed:15120073,
CC ECO:0000269|PubMed:15924141, ECO:0000269|PubMed:15947783,
CC ECO:0000269|PubMed:16724114, ECO:0000269|PubMed:16741558,
CC ECO:0000269|PubMed:18425128, ECO:0000269|PubMed:19013275,
CC ECO:0000269|PubMed:19204117, ECO:0000269|PubMed:19825647,
CC ECO:0000269|PubMed:19825650, ECO:0000269|PubMed:21771120,
CC ECO:0000269|PubMed:22242006, ECO:0000269|PubMed:22647529,
CC ECO:0000269|PubMed:22864289, ECO:0000269|PubMed:23540698}.
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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DR EMBL; AC007047; AAD22300.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06492.1; -; Genomic_DNA.
DR PIR; G84539; G84539.
DR RefSeq; NP_179232.1; NM_127193.2.
DR PDB; 6OIT; EM; 3.50 A; G=45-99.
DR PDBsum; 6OIT; -.
DR AlphaFoldDB; Q9SIW2; -.
DR SMR; Q9SIW2; -.
DR STRING; 3702.AT2G16390.1; -.
DR iPTMnet; Q9SIW2; -.
DR PaxDb; Q9SIW2; -.
DR PRIDE; Q9SIW2; -.
DR ProteomicsDB; 246963; -.
DR EnsemblPlants; AT2G16390.1; AT2G16390.1; AT2G16390.
DR GeneID; 816136; -.
DR Gramene; AT2G16390.1; AT2G16390.1; AT2G16390.
DR KEGG; ath:AT2G16390; -.
DR Araport; AT2G16390; -.
DR TAIR; locus:2042619; AT2G16390.
DR eggNOG; KOG0390; Eukaryota.
DR HOGENOM; CLU_004404_1_0_1; -.
DR InParanoid; Q9SIW2; -.
DR OMA; WQVEDMP; -.
DR PhylomeDB; Q9SIW2; -.
DR PRO; PR:Q9SIW2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIW2; baseline and differential.
DR Genevisible; Q9SIW2; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005721; C:pericentric heterochromatin; IMP:UniProtKB.
DR GO; GO:0090577; C:RNA polymerase IV transcription regulator complex; IMP:UniProtKB.
DR GO; GO:0000419; C:RNA polymerase V complex; IMP:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0006306; P:DNA methylation; IMP:TAIR.
DR GO; GO:0032776; P:DNA methylation on cytosine; IMP:UniProtKB.
DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin assembly; IMP:UniProtKB.
DR GO; GO:0080188; P:gene silencing by RNA-directed DNA methylation; IMP:UniProtKB.
DR GO; GO:0070828; P:heterochromatin organization; IMP:GO_Central.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IMP:UniProtKB.
DR GO; GO:0035563; P:positive regulation of chromatin binding; IMP:UniProtKB.
DR GO; GO:1900111; P:positive regulation of histone H3-K9 dimethylation; IMP:UniProtKB.
DR GO; GO:0060964; P:regulation of miRNA-mediated gene silencing; IMP:UniProtKB.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR044567; CLSY/DRD1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45821; PTHR45821; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Plant defense; Reference proteome;
KW RNA-mediated gene silencing.
FT CHAIN 1..888
FT /note="Protein CHROMATIN REMODELING 35"
FT /id="PRO_0000433634"
FT DOMAIN 364..541
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 701..866
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 17..24
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 305..312
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 492..495
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 377..384
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 357
FT /note="G->E: In drd1-3; defective in RNA-directed non-CpG
FT DNA methylation."
FT /evidence="ECO:0000269|PubMed:15120073"
FT MUTAGEN 494
FT /note="G->R: In drd1-1; defective in RNA-directed non-CpG
FT DNA methylation."
FT /evidence="ECO:0000269|PubMed:15120073"
FT MUTAGEN 807
FT /note="R->Q: In drd1-2; defective in RNA-directed non-CpG
FT DNA methylation."
FT /evidence="ECO:0000269|PubMed:15120073"
FT MUTAGEN 810
FT /note="R->Q: In drd1-5; defective in RNA-directed non-CpG
FT DNA methylation."
FT /evidence="ECO:0000269|PubMed:15120073"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:6OIT"
FT TURN 57..62
FT /evidence="ECO:0007829|PDB:6OIT"
FT HELIX 63..83
FT /evidence="ECO:0007829|PDB:6OIT"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:6OIT"
SQ SEQUENCE 888 AA; 100229 MW; D304DE3D5E593430 CRC64;
MGFVYIVMTG YYKNVHKRKQ NQVDDGPEAK RVKSSAKVID YSNPFAVSNM LEALDSGKFG
SVSKELEEIA DMRMDLVKRS IWLYPSLAYT VFEAEKTMDN QQVVEGVINL DDDDDDDTDV
EKKALCVVPS SSEIVLLDSD DEDNERQRPM YQFQSTLVQH QKNQGDVTPL IPQCSFEEVD
LGRGKEMPSA IKAIVEGQTS RGKVLPIENG VVNEKGVYVG VEEDDSDNES EAADEDLGNI
WNEMALSIEC SKDVARETSH KEKADVVEDC EHSFILKDDM GYVCRVCGVI EKSILEIIDV
QFTKAKRNTR TYASETRTKR FGESDNELKF SEEGLMIGGL AAHPTHAAEM KPHQIEGFQF
LCSNLVADDP GGCIMAHAPG SGKTFMIISF MQSFLAKYPQ AKPLVVLPKG ILPTWKKEFV
RWQVEDIPLL DFYSAKAENR AQQLSILKQW MEKKSILFLG YQQFSTIVCD DTTDSLSCQE
ILLKVPSILI LDEGHTPRNE DTNLLQSLAQ VQTPRKVVLS GTLYQNHVKE VFNILNLVRP
KFLKLDTSKS AVKRILAYTP CDVRGRLTGS NSDMASMFNE TVEHTLQKSE DFTVKIKVIQ
DLREMTKKVL HYYKGDFLDE LPGLADFTVV LNLSPKQLNE VKKLRREKRK FKVSAVGSAI
YLHPKLKVFS DKSDDVSDTT MDEMVEKLDL NEGVKAKFFL NLINLCDSAG EKLLVFSQYL
IPLKFLERLA ALAKGWKLGK EVFVLTGNTS SEQREWSMET FNSSPDAKIF FGSIKACGEG
ISLVGASRIL ILDVPLNPSV TRQAIGRAFR PGQKKMVHAY RLIAGSSPEE EDHNTCFKKE
VISKMWFEWN EYCGYQNFEV ETIDVDEAGD TFLESPALRE DIRVLYKR
