DRM1L_ARATH
ID DRM1L_ARATH Reviewed; 624 AA.
AC Q9LXE5; Q6QPM0; Q9LXE6;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=DNA (cytosine-5)-methyltransferase DRM1;
DE EC=2.1.1.37;
DE AltName: Full=Protein DOMAINS REARRANGED METHYLASE 1;
GN Name=DRM1; OrderedLocusNames=At5g15380/At5g15370;
GN ORFNames=F8M21.270/F8M21.260;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 [GENOMIC DNA] OF 264-570.
RC STRAIN=cv. Columbia;
RX PubMed=14871304; DOI=10.1111/j.0960-7412.2003.01999.x;
RA Comai L., Young K., Till B.J., Reynolds S.H., Greene E.A., Codomo C.A.,
RA Enns L.C., Johnson J.E., Burtner C., Odden A.R., Henikoff S.;
RT "Efficient discovery of DNA polymorphisms in natural populations by
RT Ecotilling.";
RL Plant J. 37:778-786(2004).
RN [4]
RP FUNCTION.
RX PubMed=12151602; DOI=10.1073/pnas.162371599;
RA Cao X., Jacobsen S.E.;
RT "Locus-specific control of asymmetric and CpNpG methylation by the DRM and
RT CMT3 methyltransferase genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16491-16498(2002).
RN [5]
RP FUNCTION.
RX PubMed=12121623; DOI=10.1016/s0960-9822(02)00925-9;
RA Cao X., Jacobsen S.E.;
RT "Role of the arabidopsis DRM methyltransferases in de novo DNA methylation
RT and gene silencing.";
RL Curr. Biol. 12:1138-1144(2002).
RN [6]
RP FUNCTION.
RX PubMed=14680640; DOI=10.1016/j.cub.2003.11.052;
RA Cao X., Aufsatz W., Zilberman D., Mette M.F., Huang M.S., Matzke M.,
RA Jacobsen S.E.;
RT "Role of the DRM and CMT3 methyltransferases in RNA-directed DNA
RT methylation.";
RL Curr. Biol. 13:2212-2217(2003).
CC -!- FUNCTION: Involved in de novo DNA methylation. Controls asymmetric and
CC CpNpG methylation. Required for FWA gene silencing but not for the
CC maintenance of SUP gene silencing. Functionally redundant to CMT3 to
CC maintain non-CpG methylation. Involved in RNA-directed DNA methylation.
CC {ECO:0000269|PubMed:12121623, ECO:0000269|PubMed:12151602,
CC ECO:0000269|PubMed:14680640}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01017};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: DRM2 is expressed at much higher levels than DRM1, which
CC is scarcely detected, suggesting that DRM2 is the predominant de novo
CC methylase.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. DRM-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01017}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB89347.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At5g15370 and At5g15380.; Evidence={ECO:0000305};
CC Sequence=CAB89348.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At5g15370 and At5g15380.; Evidence={ECO:0000305};
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DR EMBL; AL353993; CAB89347.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL353993; CAB89348.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92154.1; -; Genomic_DNA.
DR EMBL; AY530748; AAS45433.1; -; Genomic_DNA.
DR PIR; T49972; T49972.
DR PIR; T49973; T49973.
DR RefSeq; NP_197042.2; NM_121542.3.
DR AlphaFoldDB; Q9LXE5; -.
DR SMR; Q9LXE5; -.
DR STRING; 3702.AT5G15380.1; -.
DR REBASE; 15559; M.AthDRM1.
DR PaxDb; Q9LXE5; -.
DR PRIDE; Q9LXE5; -.
DR ProteomicsDB; 224351; -.
DR EnsemblPlants; AT5G15380.1; AT5G15380.1; AT5G15380.
DR GeneID; 831390; -.
DR Gramene; AT5G15380.1; AT5G15380.1; AT5G15380.
DR KEGG; ath:AT5G15380; -.
DR Araport; AT5G15380; -.
DR TAIR; locus:2150991; AT5G15380.
DR eggNOG; ENOG502QVZV; Eukaryota.
DR HOGENOM; CLU_006805_2_0_1; -.
DR InParanoid; Q9LXE5; -.
DR OMA; EPMMILE; -.
DR OrthoDB; 412711at2759; -.
DR PhylomeDB; Q9LXE5; -.
DR PRO; PR:Q9LXE5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LXE5; baseline and differential.
DR Genevisible; Q9LXE5; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IMP:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IGI:TAIR.
DR GO; GO:0006306; P:DNA methylation; IMP:TAIR.
DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin assembly; IMP:UniProtKB.
DR GO; GO:0051567; P:histone H3-K9 methylation; IGI:TAIR.
DR Gene3D; 3.40.50.150; -; 2.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR030380; SAM_MeTfrase_DRM.
DR InterPro; IPR015940; UBA.
DR Pfam; PF00145; DNA_methylase; 1.
DR SUPFAM; SSF53335; SSF53335; 2.
DR PROSITE; PS51680; SAM_MT_DRM; 1.
DR PROSITE; PS50030; UBA; 2.
PE 3: Inferred from homology;
KW DNA-binding; Methyltransferase; Nucleus; Reference proteome; Repeat;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..624
FT /note="DNA (cytosine-5)-methyltransferase DRM1"
FT /id="PRO_0000381941"
FT DOMAIN 57..100
FT /note="UBA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 108..149
FT /note="UBA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 188..231
FT /note="UBA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 291..622
FT /note="SAM-dependent MTase DRM-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01017"
FT REGION 160..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..187
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 624 AA; 70918 MW; 9B3BBE10CAE68AB7 CRC64;
MVMSHIFLIS QIQEVEHGDS DDVNWNTDDD ELAIDNFQFS PSPVHISATS PNSIQNRISD
ETVASFVEMG FSTQMIARAI EETAGANMEP MMILETLFNY SASTEASSSK SKVINHFIAM
GFPEEHVIKA MQEHGDEDVG EITNALLTYA EVDKLRESED MNININDDDD DNLYSLSSDD
EEDELNNSSN EDRILQALIK MGYLREDAAI AIERCGEDAS MEEVVDFICA AQMARQFDEI
YAEPDKKELM NNNKKRRTYT ETPRKPNTDQ LISLPKEMIG FGVPNHPGLM MHRPVPIPDI
ARGPPFFYYE NVAMTPKGVW AKISSHLYDI VPEFVDSKHF CAAARKRGYI HNLPIQNRFQ
IQPPQHNTIQ EAFPLTKRWW PSWDGRTKLN CLLTCIASSR LTEKIREALE RYDGETPLDV
QKWVMYECKK WNLVWVGKNK LAPLDADEME KLLGFPRDHT RGGGISTTDR YKSLGNSFQV
DTVAYHLSVL KPLFPNGINV LSLFTGIGGG EVALHRLQIK MNVVVSVEIS DANRNILRSF
WEQTNQKGIL REFKDVQKLD DNTIERLMDE YGGFDLVIGG SPCNNLAGGN RHHRVGLGGE
HSSLFFDYCR ILEAVRRKAR HMRR
