ID DNMT1_ARATH Reviewed; 1534 AA. AC P34881; Q0WLP5; Q0WPP9; Q5C994; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 24-JAN-2024, entry version 167. DE RecName: Full=DNA (cytosine-5)-methyltransferase 1; DE EC=2.1.1.37; DE AltName: Full=DNA methyltransferase 01; DE AltName: Full=DNA methyltransferase 2; DE AltName: Full=DNA methyltransferase AthI; DE Short=DNA Metase AthI; DE Short=M.AthI; DE AltName: Full=DNA methyltransferase DDM2; DE AltName: Full=Protein DECREASED DNA METHYLATION 2; GN Name=DMT1; Synonyms=ATHIM, DDM2, DMT01, MET1, MET2; GN OrderedLocusNames=At5g49160; ORFNames=K21P3.3; 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 [MRNA]. RC STRAIN=cv. Columbia; RX PubMed=8389441; DOI=10.1093/nar/21.10.2383; RA Finnegan E.J., Dennis E.S.; RT "Isolation and identification by sequence homology of a putative cytosine RT methyltransferase from Arabidopsis thaliana."; RL Nucleic Acids Res. 21:2383-2388(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10048488; DOI=10.1093/dnares/5.6.379; RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence RT features of the regions of 1,081,958 bp covered by seventeen physically RT assigned P1 and TAC clones."; RL DNA Res. 5:379-391(1998). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1517. RC STRAIN=cv. C24; RA Chang S., Pikaard C.S.; RT "Identification of suppressors of transgene silencing in Arabidopsis."; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 932-1534 AND 1371-1534. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., RA Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [6] RP FUNCTION. RX PubMed=12456661; DOI=10.1093/emboj/cdf657; RA Soppe W.J.J., Jasencakova Z., Houben A., Kakutani T., Meister A., RA Huang M.S., Jacobsen S.E., Schubert I., Fransz P.F.; RT "DNA methylation controls histone H3 lysine 9 methylation and RT heterochromatin assembly in Arabidopsis."; RL EMBO J. 21:6549-6559(2002). RN [7] RP FUNCTION, AND MUTAGENESIS OF GLU-1272 AND GLY-1465. RX PubMed=14667411; DOI=10.1016/s1534-5807(03)00361-7; RA Xiao W., Gehring M., Choi Y., Margossian L., Pu H., Harada J.J., RA Goldberg R.B., Pennell R.I., Fischer R.L.; RT "Imprinting of the MEA Polycomb gene is controlled by antagonism between RT MET1 methyltransferase and DME glycosylase."; RL Dev. Cell 5:891-901(2003). RN [8] RP FUNCTION, AND MUTAGENESIS OF GLY-1101 AND PRO-1300. RX PubMed=12663548; DOI=10.1093/genetics/163.3.1109; RA Kankel M.W., Ramsey D.E., Stokes T.L., Flowers S.K., Haag J.R., RA Jeddeloh J.A., Riddle N.C., Verbsky M.L., Richards E.J.; RT "Arabidopsis MET1 cytosine methyltransferase mutants."; RL Genetics 163:1109-1122(2003). RN [9] RP FUNCTION. RX PubMed=12669067; DOI=10.1038/ng1138; RA Saze H., Mittelsten Scheid O., Paszkowski J.; RT "Maintenance of CpG methylation is essential for epigenetic inheritance RT during plant gametogenesis."; RL Nat. Genet. 34:65-69(2003). RN [10] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=17012404; DOI=10.1104/pp.106.088849; RA Xiao W., Brown R.C., Lemmon B.E., Harada J.J., Goldberg R.B., Fischer R.L.; RT "Regulation of seed size by hypomethylation of maternal and paternal RT genomes."; RL Plant Physiol. 142:1160-1168(2006). RN [11] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=16531498; DOI=10.1105/tpc.105.038836; RA Xiao W., Custard K.D., Brown R.C., Lemmon B.E., Harada J.J., Goldberg R.B., RA Fischer R.L.; RT "DNA methylation is critical for Arabidopsis embryogenesis and seed RT viability."; RL Plant Cell 18:805-814(2006). RN [12] RP FUNCTION. RX PubMed=18820427; RA Kim M., Ohr H., Lee J.W., Hyun Y., Fischer R.L., Choi Y.; RT "Temporal and spatial downregulation of Arabidopsis MET1 activity results RT in global DNA hypomethylation and developmental defects."; RL Mol. Cells 26:611-615(2008). CC -!- FUNCTION: Maintains chromatin CpG methylation that plays a role in CC genomic imprinting, regulation of embryogenesis and seed viability. CC Required for proper patterns of CG DNA methylation in dividing cells. CC Required for MEA promoter methylation in seeds. CC {ECO:0000269|PubMed:12456661, ECO:0000269|PubMed:12663548, CC ECO:0000269|PubMed:12669067, ECO:0000269|PubMed:14667411, CC ECO:0000269|PubMed:16531498, ECO:0000269|PubMed:17012404, CC ECO:0000269|PubMed:18820427}. 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:PRU10018}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed in flowers, embryos and endosperm. CC {ECO:0000269|PubMed:17012404}. CC -!- DISRUPTION PHENOTYPE: Late-flowering phenotype caused by ectopic CC expression of FWA gene. Asymmetric zygote division and abnormal CC embryos. Displays genome hypomethylation, strong reduction of CpG CC methylation in centromeric repeats, reduction of heterochromatin and CC chromocenter size and gametes with fully demethylated and CC hemidemethylated DNA. {ECO:0000269|PubMed:16531498}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE- CC ProRule:PRU01016}. CC -!- SEQUENCE CAUTION: CC Sequence=AAX22756.1; Type=Erroneous gene model prediction; 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; L10692; AAA32829.1; -; mRNA. DR EMBL; AB016872; BAB10334.1; -; Genomic_DNA. DR EMBL; CP002688; AED95777.1; -; Genomic_DNA. DR EMBL; AY699012; AAX22756.1; ALT_SEQ; Genomic_DNA. DR EMBL; AK229013; BAF00900.1; -; mRNA. DR EMBL; AK230148; BAF01962.1; -; mRNA. DR PIR; S59604; S59604. DR RefSeq; NP_199727.1; NM_124293.4. DR AlphaFoldDB; P34881; -. DR SMR; P34881; -. DR BioGRID; 20221; 5. DR STRING; 3702.P34881; -. DR REBASE; 11752; M.AthMET1. DR PaxDb; 3702-AT5G49160-1; -. DR ProteomicsDB; 220525; -. DR EnsemblPlants; AT5G49160.1; AT5G49160.1; AT5G49160. DR GeneID; 834975; -. DR Gramene; AT5G49160.1; AT5G49160.1; AT5G49160. DR KEGG; ath:AT5G49160; -. DR Araport; AT5G49160; -. DR TAIR; AT5G49160; MET1. DR eggNOG; ENOG502QPKK; Eukaryota. DR HOGENOM; CLU_002247_0_0_1; -. DR InParanoid; P34881; -. DR OMA; KINDAEC; -. DR OrthoDB; 317994at2759; -. DR PhylomeDB; P34881; -. DR PRO; PR:P34881; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; P34881; baseline and differential. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003682; F:chromatin binding; IEA:InterPro. DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0008168; F:methyltransferase activity; TAS:TAIR. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; IMP:TAIR. DR GO; GO:0009294; P:DNA-mediated transformation; IMP:TAIR. DR GO; GO:0009910; P:negative regulation of flower development; IMP:TAIR. DR GO; GO:0010069; P:zygote asymmetric cytokinesis in embryo sac; IMP:TAIR. DR CDD; cd04712; BAH_DCM_I; 1. DR CDD; cd04708; BAH_plantDCM_II; 1. DR Gene3D; 2.30.30.490; -; 2. DR Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 2. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR001025; BAH_dom. DR InterPro; IPR043151; BAH_sf. DR InterPro; IPR018117; C5_DNA_meth_AS. DR InterPro; IPR001525; C5_MeTfrase. DR InterPro; IPR031303; C5_meth_CS. DR InterPro; IPR022702; Cytosine_MeTrfase1_RFD. DR InterPro; IPR017198; DNMT1-like. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR NCBIfam; TIGR00675; dcm; 1. DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1. DR PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1. DR Pfam; PF01426; BAH; 2. DR Pfam; PF00145; DNA_methylase; 2. DR Pfam; PF12047; DNMT1-RFD; 2. DR PIRSF; PIRSF037404; DNMT1; 1. DR PRINTS; PR00105; C5METTRFRASE. DR SMART; SM00439; BAH; 2. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS51038; BAH; 2. DR PROSITE; PS00094; C5_MTASE_1; 1. DR PROSITE; PS00095; C5_MTASE_2; 1. DR PROSITE; PS51679; SAM_MT_C5; 1. DR Genevisible; P34881; AT. PE 1: Evidence at protein level; KW Chromatin regulator; DNA-binding; Isopeptide bond; Methyltransferase; KW Nucleus; Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; KW Ubl conjugation. FT CHAIN 1..1534 FT /note="DNA (cytosine-5)-methyltransferase 1" FT /id="PRO_0000088039" FT DOMAIN 735..869 FT /note="BAH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370" FT DOMAIN 909..1049 FT /note="BAH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370" FT DOMAIN 1093..1527 FT /note="SAM-dependent MTase C5-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 321..341 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 647..717 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 657..682 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 689..715 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1198 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016, FT ECO:0000255|PROSITE-ProRule:PRU10018" FT CROSSLNK 599 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:O23273" FT MUTAGEN 1101 FT /note="G->S: In met1-2/ddm2-2; reduced activity." FT /evidence="ECO:0000269|PubMed:12663548" FT MUTAGEN 1272 FT /note="E->K: In met1-5; reduced activity." FT /evidence="ECO:0000269|PubMed:14667411" FT MUTAGEN 1300 FT /note="P->S: In met1-1/ddm2-1; reduced activity." FT /evidence="ECO:0000269|PubMed:12663548" FT MUTAGEN 1465 FT /note="G->E: In met1-7; reduced activity." FT /evidence="ECO:0000269|PubMed:14667411" FT CONFLICT 306 FT /note="L -> M (in Ref. 4; AAX22756)" FT /evidence="ECO:0000305" FT CONFLICT 837 FT /note="W -> R (in Ref. 4; AAX22756)" FT /evidence="ECO:0000305" FT CONFLICT 901 FT /note="K -> R (in Ref. 4; AAX22756)" FT /evidence="ECO:0000305" FT CONFLICT 932 FT /note="K -> N (in Ref. 5; BAF01962)" FT /evidence="ECO:0000305" SQ SEQUENCE 1534 AA; 172431 MW; 23FC944AA7074C5A CRC64; MVENGAKAAK RKKRPLPEIQ EVEDVPRTRR PRRAAACTSF KEKSIRVCEK SATIEVKKQQ IVEEEFLALR LTALETDVED RPTRRLNDFV LFDSDGVPQP LEMLEIHDIF VSGAILPSDV CTDKEKEKGV RCTSFGRVEH WSISGYEDGS PVIWISTELA DYDCRKPAAS YRKVYDYFYE KARASVAVYK KLSKSSGGDP DIGLEELLAA VVRSMSSGSK YFSSGAAIID FVISQGDFIY NQLAGLDETA KKHESSYVEI PVLVALREKS SKIDKPLQRE RNPSNGVRIK EVSQVAESEA LTSDQLVDGT DDDRRYAILL QDEENRKSMQ QPRKNSSSGS ASNMFYIKIN EDEIANDYPL PSYYKTSEEE TDELILYDAS YEVQSEHLPH RMLHNWALYN SDLRFISLEL LPMKQCDDID VNIFGSGVVT DDNGSWISLN DPDSGSQSHD PDGMCIFLSQ IKEWMIEFGS DDIISISIRT DVAWYRLGKP SKLYAPWWKP VLKTARVGIS ILTFLRVESR VARLSFADVT KRLSGLQAND KAYISSDPLA VERYLVVHGQ IILQLFAVYP DDNVKRCPFV VGLASKLEDR HHTKWIIKKK KISLKELNLN PRAGMAPVAS KRKAMQATTT RLVNRIWGEF YSNYSPEDPL QATAAENGED EVEEEGGNGE EEVEEEGENG LTEDTVPEPV EVQKPHTPKK IRGSSGKREI KWDGESLGKT SAGEPLYQQA LVGGEMVAVG GAVTLEVDDP DEMPAIYFVE YMFESTDHCK MLHGRFLQRG SMTVLGNAAN ERELFLTNEC MTTQLKDIKG VASFEIRSRP WGHQYRKKNI TADKLDWARA LERKVKDLPT EYYCKSLYSP ERGGFFSLPL SDIGRSSGFC TSCKIREDEE KRSTIKLNVS KTGFFINGIE YSVEDFVYVN PDSIGGLKEG SKTSFKSGRN IGLRAYVVCQ LLEIVPKESR KADLGSFDVK VRRFYRPEDV SAEKAYASDI QELYFSQDTV VLPPGALEGK CEVRKKSDMP LSREYPISDH IFFCDLFFDT SKGSLKQLPA NMKPKFSTIK DDTLLRKKKG KGVESEIESE IVKPVEPPKE IRLATLDIFA GCGGLSHGLK KAGVSDAKWA IEYEEPAGQA FKQNHPESTV FVDNCNVILR AIMEKGGDQD DCVSTTEANE LAAKLTEEQK STLPLPGQVD FINGGPPCQG FSGMNRFNQS SWSKVQCEMI LAFLSFADYF RPRYFLLENV RTFVSFNKGQ TFQLTLASLL EMGYQVRFGI LEAGAYGVSQ SRKRAFIWAA APEEVLPEWP EPMHVFGVPK LKISLSQGLH YAAVRSTALG APFRPITVRD TIGDLPSVEN GDSRTNKEYK EVAVSWFQKE IRGNTIALTD HICKAMNELN LIRCKLIPTR PGADWHDLPK RKVTLSDGRV EEMIPFCLPN TAERHNGWKG LYGRLDWQGN FPTSVTDPQP MGKVGMCFHP EQHRILTVRE CARSQGFPDS YEFAGNINHK HRQIGNAVPP PLAFALGRKL KEALHLKKSP QHQP //