ID CMT2_ARATH Reviewed; 1295 AA. AC Q94F87; O49415; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 08-FEB-2011, sequence version 3. DT 24-JAN-2024, entry version 146. DE RecName: Full=DNA (cytosine-5)-methyltransferase CMT2; DE EC=2.1.1.37; DE AltName: Full=Chromomethylase 2; DE AltName: Full=Protein CHROMOMETHYLASE 2; GN Name=CMT2; OrderedLocusNames=At4g19020; ORFNames=F13C5.190; 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]. RC STRAIN=cv. Wassilewskija; RX PubMed=11459824; DOI=10.1101/gad.905701; RA Bartee L., Malagnac F., Bender J.; RT "Arabidopsis cmt3 chromomethylase mutations block non-CG methylation and RT silencing of an endogenous gene."; RL Genes Dev. 15:1753-1758(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., RA Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."; RL Nature 402:769-777(1999). 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 [LARGE SCALE MRNA] OF 1153-1295. RC STRAIN=cv. Columbia; RX PubMed=14993207; DOI=10.1101/gr.1515604; RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., RA Weissenbach J., Salanoubat M.; RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a RT combined approach to evaluate and improve Arabidopsis genome annotation."; RL Genome Res. 14:406-413(2004). 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 -!- 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=AAK69757.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=BX828439; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305}; CC Sequence=CAA16759.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAB78904.1; 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; AF383171; AAK69757.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL021711; CAA16759.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL161549; CAB78904.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002687; AEE84126.1; -; Genomic_DNA. DR EMBL; BX828439; -; NOT_ANNOTATED_CDS; mRNA. DR PIR; T05039; T05039. DR RefSeq; NP_193637.2; NM_118020.5. DR AlphaFoldDB; Q94F87; -. DR SMR; Q94F87; -. DR BioGRID; 12933; 3. DR DIP; DIP-60718N; -. DR STRING; 3702.Q94F87; -. DR REBASE; 3168; M.AthCMT2. DR iPTMnet; Q94F87; -. DR PaxDb; 3702-AT4G19020-1; -. DR ProteomicsDB; 220476; -. DR EnsemblPlants; AT4G19020.1; AT4G19020.1; AT4G19020. DR GeneID; 827640; -. DR Gramene; AT4G19020.1; AT4G19020.1; AT4G19020. DR KEGG; ath:AT4G19020; -. DR Araport; AT4G19020; -. DR TAIR; AT4G19020; CMT2. DR eggNOG; ENOG502QW29; Eukaryota. DR HOGENOM; CLU_004921_1_0_1; -. DR InParanoid; Q94F87; -. DR OrthoDB; 1215065at2759; -. DR PhylomeDB; Q94F87; -. DR PRO; PR:Q94F87; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; Q94F87; 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; IMP:TAIR. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0032183; F:SUMO binding; IPI:TAIR. DR GO; GO:0034605; P:cellular response to heat; IMP:TAIR. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0010426; P:DNA methylation on cytosine within a CHH sequence; 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; IPR023780; Chromo_domain. DR InterPro; IPR017198; DNMT1-like. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1. DR PANTHER; PTHR10629:SF34; DNA (CYTOSINE-5)-METHYLTRANSFERASE CMT2; 1. DR Pfam; PF01426; BAH; 1. DR Pfam; PF00385; Chromo; 1. DR Pfam; PF00145; DNA_methylase; 1. DR PIRSF; PIRSF037404; DNMT1; 1. DR PRINTS; PR00105; C5METTRFRASE. 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; PS50013; CHROMO_2; 1. DR PROSITE; PS51679; SAM_MT_C5; 1. DR Genevisible; Q94F87; AT. PE 2: Evidence at transcript level; KW Chromatin regulator; DNA-binding; Methyltransferase; Nucleus; KW Reference proteome; S-adenosyl-L-methionine; Transcription; KW Transcription regulation; Transferase. FT CHAIN 1..1295 FT /note="DNA (cytosine-5)-methyltransferase CMT2" FT /id="PRO_0000246692" FT DOMAIN 578..693 FT /note="BAH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370" FT DOMAIN 727..1268 FT /note="SAM-dependent MTase C5-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016" FT DOMAIN 837..902 FT /note="Chromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 52..91 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 249..287 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 814..835 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 58..76 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 265..281 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 814..828 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 915 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016" FT CONFLICT 54..55 FT /note="DN -> ND (in Ref. 1; AAK69757)" FT /evidence="ECO:0000305" FT CONFLICT 110..111 FT /note="AL -> PV (in Ref. 1; AAK69757)" FT /evidence="ECO:0000305" FT CONFLICT 125 FT /note="K -> E (in Ref. 1; AAK69757)" FT /evidence="ECO:0000305" FT CONFLICT 132..133 FT /note="KF -> NS (in Ref. 1; AAK69757)" FT /evidence="ECO:0000305" FT CONFLICT 156 FT /note="F -> S (in Ref. 1; AAK69757)" FT /evidence="ECO:0000305" FT CONFLICT 229 FT /note="R -> K (in Ref. 1; AAK69757)" FT /evidence="ECO:0000305" FT CONFLICT 340 FT /note="K -> N (in Ref. 1; AAK69757)" FT /evidence="ECO:0000305" FT CONFLICT 501 FT /note="K -> N (in Ref. 1; AAK69757)" FT /evidence="ECO:0000305" FT CONFLICT 665 FT /note="V -> A (in Ref. 1; AAK69757)" FT /evidence="ECO:0000305" FT CONFLICT 705 FT /note="C -> W (in Ref. 1; AAK69757)" FT /evidence="ECO:0000305" FT CONFLICT 823 FT /note="G -> E (in Ref. 1; AAK69757)" FT /evidence="ECO:0000305" FT CONFLICT 850 FT /note="H -> P (in Ref. 1; AAK69757)" FT /evidence="ECO:0000305" FT CONFLICT 1132 FT /note="K -> N (in Ref. 1; AAK69757)" FT /evidence="ECO:0000305" FT CONFLICT 1144 FT /note="L -> I (in Ref. 1; AAK69757)" FT /evidence="ECO:0000305" SQ SEQUENCE 1295 AA; 145015 MW; 33CE317C541825A6 CRC64; MLSPAKCESE EAQAPLDLHS SSRSEPECLS LVLWCPNPEE AAPSSTRELI KLPDNGEMSL RRSTTLNCNS PEENGGEGRV SQRKSSRGKS QPLLMLTNGC QLRRSPRFRA LHANFDNVCS VPVTKGGVSQ RKFSRGKSQP LLTLTNGCQL RRSPRFRAVD GNFDSVCSVP VTGKFGSRKR KSNSALDKKE SSDSEGLTFK DIAVIAKSLE MEIISECQYK NNVAEGRSRL QDPAKRKVDS DTLLYSSINS SKQSLGSNKR MRRSQRFMKG TENEGEENLG KSKGKGMSLA SCSFRRSTRL SGTVETGNTE TLNRRKDCGP ALCGAEQVRG TERLVQISKK DHCCEAMKKC EGDGLVSSKQ ELLVFPSGCI KKTVNGCRDR TLGKPRSSGL NTDDIHTSSL KISKNDTSNG LTMTTALVEQ DAMESLLQGK TSACGAADKG KTREMHVNST VIYLSDSDEP SSIEYLNGDN LTQVESGSAL SSGGNEGIVS LDLNNPTKST KRKGKRVTRT AVQEQNKRSI CFFIGEPLSC EEAQERWRWR YELKERKSKS RGQQSEDDED KIVANVECHY SQAKVDGHTF SLGDFAYIKG EEEETHVGQI VEFFKTTDGE SYFRVQWFYR ATDTIMERQA TNHDKRRLFY STVMNDNPVD CLISKVTVLQ VSPRVGLKPN SIKSDYYFDM EYCVEYSTFQ TLRNPKTSEN KLECCADVVP TESTESILKK KSFSGELPVL DLYSGCGGMS TGLSLGAKIS GVDVVTKWAV DQNTAACKSL KLNHPNTQVR NDAAGDFLQL LKEWDKLCKR YVFNNDQRTD TLRSVNSTKE TSGSSSSSDD DSDSEEYEVE KLVDICFGDH DKTGKNGLKF KVHWKGYRSD EDTWELAEEL SNCQDAIREF VTSGFKSKIL PLPGRVGVIC GGPPCQGISG YNRHRNVDSP LNDERNQQII VFMDIVEYLK PSYVLMENVV DILRMDKGSL GRYALSRLVN MRYQARLGIM TAGCYGLSQF RSRVFMWGAV PNKNLPPFPL PTHDVIVRYG LPLEFERNVV AYAEGQPRKL EKALVLKDAI SDLPHVSNDE DREKLPYESL PKTDFQRYIR STKRDLTGSA IDNCNKRTML LHDHRPFHIN EDDYARVCQI PKRKGANFRD LPGLIVRNNT VCRDPSMEPV ILPSGKPLVP GYVFTFQQGK SKRPFARLWW DETVPTVLTV PTCHSQALLH PEQDRVLTIR ESARLQGFPD YFQFCGTIKE RYCQIGNAVA VSVSRALGYS LGMAFRGLAR DEHLIKLPQN FSHSTYPQLQ ETIPH //