ID CMT1_ARATH Reviewed; 791 AA. AC O49139; O49137; O49138; O49141; O50057; O50073; Q38940; Q7G196; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 2. DT 27-MAR-2024, entry version 164. DE RecName: Full=Putative DNA (cytosine-5)-methyltransferase CMT1; DE EC=2.1.1.37; DE AltName: Full=Chromomethylase 1; DE AltName: Full=Protein CHROMOMETHYLASE 1; GN Name=CMT1; OrderedLocusNames=At1g80740; ORFNames=F23A5.9; 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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND TISSUE RP SPECIFICITY. RC STRAIN=cv. Columbia, cv. Kl-0, cv. Landsberg erecta, cv. Metz-0, cv. RC Nd-0, cv. Nd-1, and cv. RLD; RX PubMed=9584105; DOI=10.1093/genetics/149.1.307; RA Henikoff S., Comai L.; RT "A DNA methyltransferase homolog with a chromodomain exists in multiple RT polymorphic forms in Arabidopsis."; RL Genetics 149:307-318(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Columbia; RA Goodman H.M., Gallant P., Keifer-Higgins S., Rubenfield M., Church G.M.; RT "A 37.5 Kb sequence from Arabidopsis thaliana chromosome I."; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., RA Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."; RL Nature 408:816-820(2000). RN [4] 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). CC -!- FUNCTION: May be involved in the CpXpG methylation and in gene CC silencing. {ECO:0000250}. 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O49139-1; Sequence=Displayed; CC Name=2; CC IsoId=O49139-2; Sequence=VSP_019857, VSP_019858; CC -!- TISSUE SPECIFICITY: Expressed in flowers. Not detected in leaves, CC roots, seedlings and plants prior formation of flower buds. CC {ECO:0000269|PubMed:9584105}. CC -!- MISCELLANEOUS: [Isoform 2]: Alternative splice site used 50% of the CC time in cv. Columbia. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE- CC ProRule:PRU01016}. CC -!- CAUTION: Could be the product of a pseudogene. The protein is severely CC truncated in several ecotypes and the gene even harbors a complete CC retrotransposon in 3 ecotypes. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA98912.1; 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; AF039364; AAB95485.1; -; mRNA. DR EMBL; AF039366; AAC02659.1; -; Genomic_DNA. DR EMBL; AF039367; AAC02660.1; -; Genomic_DNA. DR EMBL; AF039368; AAC02661.1; -; Genomic_DNA. DR EMBL; AF039369; AAC02662.1; -; Genomic_DNA. DR EMBL; AF039370; AAC02663.1; -; Genomic_DNA. DR EMBL; AF039371; AAC02665.1; -; Genomic_DNA. DR EMBL; AF039372; AAC02667.1; -; Genomic_DNA. DR EMBL; AF039373; AAC02668.1; -; Genomic_DNA. DR EMBL; U53501; AAA98912.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC011713; AAF14662.1; -; Genomic_DNA. DR EMBL; CP002684; AEE36442.1; -; Genomic_DNA. DR PIR; H96839; H96839. DR RefSeq; NP_565245.1; NM_106722.2. [O49139-1] DR AlphaFoldDB; O49139; -. DR SMR; O49139; -. DR STRING; 3702.O49139; -. DR REBASE; 3261; M.AthCMT1P. DR PaxDb; 3702-AT1G80740-1; -. DR EnsemblPlants; AT1G80740.1; AT1G80740.1; AT1G80740. [O49139-1] DR GeneID; 844413; -. DR Gramene; AT1G80740.1; AT1G80740.1; AT1G80740. [O49139-1] DR KEGG; ath:AT1G80740; -. DR Araport; AT1G80740; -. DR TAIR; AT1G80740; CMT1. DR eggNOG; ENOG502QW29; Eukaryota. DR HOGENOM; CLU_004921_0_0_1; -. DR InParanoid; O49139; -. DR OMA; PPCDLYY; -. DR OrthoDB; 1215065at2759; -. DR PhylomeDB; O49139; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; O49139; 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:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0009294; P:DNA-mediated transformation; IMP:TAIR. DR CDD; cd04716; BAH_plantDCM_I; 1. DR CDD; cd18635; CD_CMT3_like; 1. DR Gene3D; 2.30.30.490; -; 1. DR Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2. DR InterPro; IPR001025; BAH_dom. DR InterPro; IPR043151; BAH_sf. DR InterPro; IPR001525; C5_MeTfrase. DR InterPro; IPR016197; Chromo-like_dom_sf. DR InterPro; IPR000953; Chromo/chromo_shadow_dom. DR InterPro; IPR017984; Chromo_dom_subgr. DR InterPro; IPR023780; Chromo_domain. DR InterPro; IPR023779; Chromodomain_CS. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1. DR PANTHER; PTHR10629:SF59; DNA (CYTOSINE-5)-METHYLTRANSFERASE CMT1-RELATED; 1. DR Pfam; PF01426; BAH; 1. DR Pfam; PF00385; Chromo; 1. DR Pfam; PF00145; DNA_methylase; 1. DR PRINTS; PR00105; C5METTRFRASE. DR PRINTS; PR00504; CHROMODOMAIN. DR SMART; SM00439; BAH; 1. DR SMART; SM00298; CHROMO; 1. DR SUPFAM; SSF54160; Chromo domain-like; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS51038; BAH; 1. DR PROSITE; PS00598; CHROMO_1; 1. DR PROSITE; PS50013; CHROMO_2; 1. DR PROSITE; PS51679; SAM_MT_C5; 1. DR Genevisible; O49139; AT. PE 5: Uncertain; KW Alternative splicing; Chromatin regulator; Coiled coil; DNA-binding; KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine; KW Transcription; Transcription regulation; Transferase. FT CHAIN 1..791 FT /note="Putative DNA (cytosine-5)-methyltransferase CMT1" FT /id="PRO_0000246691" FT DOMAIN 79..199 FT /note="BAH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370" FT DOMAIN 225..768 FT /note="SAM-dependent MTase C5-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016" FT DOMAIN 339..404 FT /note="Chromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053" FT REGION 37..59 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 308..333 FT /evidence="ECO:0000255" FT ACT_SITE 417 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016" FT VAR_SEQ 568..570 FT /note="VTN -> CCR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9584105" FT /id="VSP_019857" FT VAR_SEQ 571..791 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9584105" FT /id="VSP_019858" FT VARIANT 148 FT /note="D -> G (in strain: cv. Metz-0)" FT VARIANT 196 FT /note="T -> I (in strain: cv. Kl-0)" FT VARIANT 198 FT /note="A -> T (in strain: cv. No-0)" FT VARIANT 249..791 FT /note="Missing (in strain: cv. Metz-0)" FT VARIANT 560 FT /note="D -> V (in strain: cv. Landsberg erecta, cv. No-0 FT and cv. RLD)" FT VARIANT 561..791 FT /note="Missing (in strain: cv. Landsberg erecta, cv. No-0 FT and cv. RLD)" FT VARIANT 604 FT /note="F -> C (in strain: cv. Nd-1, Nd-0 and cv. Kl-0)" SQ SEQUENCE 791 AA; 89219 MW; A5ECFDBC274B215C CRC64; MAARNKQKKR AEPESDLCFA GKPMSVVEST IRWPHRYQSK KTKLQAPTKK PANKGGKKED EEIIKQAKCH FDKALVDGVL INLNDDVYVT GLPGKLKFIA KVIELFEADD GVPYCRFRWY YRPEDTLIER FSHLVQPKRV FLSNDENDNP LTCIWSKVNI AKVPLPKITS RIEQRVIPPC DYYYDMKYEV PYLNFTSADD GSDASSSLSS DSALNCFENL HKDEKFLLDL YSGCGAMSTG FCMGASISGV KLITKWSVDI NKFACDSLKL NHPETEVRNE AAEDFLALLK EWKRLCEKFS LVSSTEPVES ISELEDEEVE ENDDIDEAST GAELEPGEFE VEKFLGIMFG DPQGTGEKTL QLMVRWKGYN SSYDTWEPYS GLGNCKEKLK EYVIDGFKSH LLPLPGTVYT VCGGPPCQGI SGYNRYRNNE APLEDQKNQQ LLVFLDIIDF LKPNYVLMEN VVDLLRFSKG FLARHAVASF VAMNYQTRLG MMAAGSYGLP QLRNRVFLWA AQPSEKLPPY PLPTHEVAKK FNTPKEFKDL QVGRIQMEFL KLDNALTLAD AISDLPPVTN YVANDVMDYN DAAPKTEFEN FISLKRSETL LPAFGGDPTR RLFDHQPLVL GDDDLERVSY IPKQKGANYR DMPGVLVHNN KAEINPRFRA KLKSGKNVVP AYAISFIKGK SKKPFGRLWG DEIVNTVVTR AEPHNQCVIH PMQNRVLSVR ENARLQGFPD CYKLCGTIKE KYIQVGNAVA VPVGVALGYA FGMASQGLTD DEPVIKLPFK YPECMQAKDQ I //