DRM3_ARATH
ID DRM3_ARATH Reviewed; 710 AA.
AC Q8H1E8; Q949U6; Q9LUU0;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable inactive DNA (cytosine-5)-methyltransferase DRM3 {ECO:0000305};
DE AltName: Full=Protein DOMAINS REARRANGED METHYLTRANSFERASE 3 {ECO:0000303|PubMed:21060858};
GN Name=DRM3 {ECO:0000303|PubMed:21060858};
GN OrderedLocusNames=At3g17310 {ECO:0000312|Araport:AT3G17310};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION.
RX PubMed=21060858; DOI=10.1371/journal.pgen.1001182;
RA Henderson I.R., Deleris A., Wong W., Zhong X., Chin H.G., Horwitz G.A.,
RA Kelly K.A., Pradhan S., Jacobsen S.E.;
RT "The de novo cytosine methyltransferase DRM2 requires intact UBA domains
RT and a catalytically mutated paralog DRM3 during RNA-directed DNA
RT methylation in Arabidopsis thaliana.";
RL PLoS Genet. 6:E1001182-E1001182(2010).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25316414; DOI=10.1186/1756-0500-7-721;
RA Costa-Nunes P., Kim J.Y., Hong E., Pontes O.;
RT "The cytological and molecular role of domains rearranged
RT methyltransferase3 in RNA-dependent DNA methylation of Arabidopsis
RT thaliana.";
RL BMC Res. Notes 7:721-721(2014).
RN [7]
RP FUNCTION, AND INTERACTION WITH POL V.
RX PubMed=25561521; DOI=10.1073/pnas.1423603112;
RA Zhong X., Hale C.J., Nguyen M., Ausin I., Groth M., Hetzel J.,
RA Vashisht A.A., Henderson I.R., Wohlschlegel J.A., Jacobsen S.E.;
RT "Domains rearranged methyltransferase3 controls DNA methylation and
RT regulates RNA polymerase V transcript abundance in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:911-916(2015).
CC -!- FUNCTION: Catalytically inactive DNA methyltransferase that acts as
CC regulatory factor for DRM2-mediated DNA methylation. Required for
CC maintenance of non-CpG DNA methylation. Required for normal
CC establishment and maintenance of RNA-directed DNA methylation (RdDM)
CC and accumulation of specific repeat-associated small interfering RNAs
CC (siRNAs) (PubMed:21060858, PubMed:25316414, PubMed:25561521). Required
CC for nucleolus organizer region (NOR) nuclear organization during
CC interphase (PubMed:25316414). Acts downstream of the production of
CC siRNAs. May promote RNA polymerase V (Pol V) transcriptional elongation
CC or assist in the stabilization of Pol V transcripts (PubMed:25561521).
CC {ECO:0000269|PubMed:21060858, ECO:0000269|PubMed:25316414,
CC ECO:0000269|PubMed:25561521}.
CC -!- SUBUNIT: Interacts with Pol V. {ECO:0000269|PubMed:25561521}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25316414}.
CC Note=Colocalizes with AGO4 in perinucleolar region.
CC {ECO:0000269|PubMed:25316414}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. DRM-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01017}.
CC -!- CAUTION: Lacks the conserved tripeptide Ser-Pro-Cys in position 672
CC necessary for the methyltransferase activity in DRM protein (AC
CC Q9M548).
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02735.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB022216; BAB02735.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75935.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75936.1; -; Genomic_DNA.
DR EMBL; AY050882; AAK92819.1; -; mRNA.
DR EMBL; AY150440; AAN12982.1; -; mRNA.
DR EMBL; AK316724; BAH19451.1; -; mRNA.
DR RefSeq; NP_566573.1; NM_112609.3.
DR RefSeq; NP_850603.1; NM_180272.2.
DR AlphaFoldDB; Q8H1E8; -.
DR SMR; Q8H1E8; -.
DR IntAct; Q8H1E8; 1.
DR STRING; 3702.AT3G17310.1; -.
DR REBASE; 12266; M.AthDRM3.
DR REBASE; 4601; M.AthDRM2.
DR PaxDb; Q8H1E8; -.
DR PRIDE; Q8H1E8; -.
DR ProteomicsDB; 224354; -.
DR EnsemblPlants; AT3G17310.1; AT3G17310.1; AT3G17310.
DR EnsemblPlants; AT3G17310.2; AT3G17310.2; AT3G17310.
DR GeneID; 820994; -.
DR Gramene; AT3G17310.1; AT3G17310.1; AT3G17310.
DR Gramene; AT3G17310.2; AT3G17310.2; AT3G17310.
DR KEGG; ath:AT3G17310; -.
DR Araport; AT3G17310; -.
DR TAIR; locus:2089075; AT3G17310.
DR eggNOG; ENOG502QS8G; Eukaryota.
DR HOGENOM; CLU_006805_3_1_1; -.
DR InParanoid; Q8H1E8; -.
DR OMA; DHTQPLE; -.
DR OrthoDB; 412711at2759; -.
DR PhylomeDB; Q8H1E8; -.
DR PRO; PR:Q8H1E8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8H1E8; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006306; P:DNA methylation; IMP:TAIR.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR030380; SAM_MeTfrase_DRM.
DR SUPFAM; SSF53335; SSF53335; 2.
DR PROSITE; PS51680; SAM_MT_DRM; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Methyltransferase; Nucleus; Reference proteome; Repeat;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..710
FT /note="Probable inactive DNA (cytosine-5)-methyltransferase
FT DRM3"
FT /id="PRO_0000438155"
FT DOMAIN 52..92
FT /note="UBA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 198..242
FT /note="UBA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 379..710
FT /note="SAM-dependent MTase DRM-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01017"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 77
FT /note="N -> S (in Ref. 4; AAK92819)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 710 AA; 79731 MW; A744D7722CB80AE6 CRC64;
MADMRRRNGS GGSSNHERNE QILFPKPETL DFDLPCDTSF PQQIGDNAAS SSGSNVKSLL
IEMGFCPTLV QKAIDENGQD DFELLLEILT KSTETEPPGP SFHGLMEPKP EPDIEYETDR
IRIALLTMKF PENLVDFALD RLGKDTPIDE MVDFIVAAQL AEKYAEESED SLDGAEINEE
DEDVTPVTAR GPEVPNEQLF ETMDKTLRLL EMGFSNDEIS MAIEKIGTKG QISVLAESIV
TGEFPAECHD DLEDIEKKVS AAAPAVNRTC LSKSWRFVGV GAQKEDGGGG SSSGTANIKP
DPGIESFPFP ATDNVGETSR GKRPKDEDEN AYPEEYTGYD DRGKRLRPED MGDSSSFMET
PWMQDEWKDN TYEFPSVMQP RLSQSLGPKV ARRPYFFYGQ LGELSPSWWS KISGFLFGIH
PEHVDTRLCS ALRRTEGYLH NLPTVNRFNT LPNPRLTIQD AMPHMRSWWP QWDIRKHFNS
GTCSNMKDAT LLCERIGRRI AECKGKPTQQ DQTLILRHCH TSNLIWIAPN ILSPLEPEHL
ECIMGYPMNH TNIGGGRLAE RLKLFDYCFQ TDTLGYHLSV LKSMFPQGLT VLSLFSGIGG
AEIALDRLGI HLKGVVSVES CGLSRNILKR WWQTSGQTGE LVQIEEIKSL TAKRLETLMQ
RFGGFDFVIC QNPSTPLDLS KEISNSEACE FDYTLFNEFA RVTKRVRDMM
