CMT2_ARATH
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 03-AUG-2022, entry version 139.
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};
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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.AT4G19020.1; -.
DR REBASE; 3168; M.AthCMT2.
DR iPTMnet; Q94F87; -.
DR PaxDb; Q94F87; -.
DR PRIDE; Q94F87; -.
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; locus:2117104; AT4G19020.
DR eggNOG; ENOG502QW29; Eukaryota.
DR HOGENOM; CLU_004921_1_0_1; -.
DR InParanoid; Q94F87; -.
DR OrthoDB; 898916at2759; -.
DR PhylomeDB; Q94F87; -.
DR PRO; PR:Q94F87; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94F87; baseline and differential.
DR Genevisible; Q94F87; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.40.50.150; -; 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 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; SSF53335; SSF53335; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
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
