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DNMT2_ARATH
ID   DNMT2_ARATH             Reviewed;        1512 AA.
AC   Q9M0S8;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=DNA (cytosine-5)-methyltransferase 2;
DE            EC=2.1.1.37;
DE   AltName: Full=DNA methyltransferase 2;
DE   AltName: Full=DNA methyltransferase IIb;
GN   Name=MET2; Synonyms=METIIb; OrderedLocusNames=At4g08990; ORFNames=F23J3.20;
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=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   [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   TISSUE SPECIFICITY, AND GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   PubMed=10579493; DOI=10.1023/a:1006347010369;
RA   Genger R.K., Kovac K.A., Dennis E.S., Peacock W.J., Finnegan E.J.;
RT   "Multiple DNA methyltransferase genes in Arabidopsis thaliana.";
RL   Plant Mol. Biol. 41:269-278(1999).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=21257907; DOI=10.1073/pnas.1019273108;
RA   Hsieh T.-F., Shin J., Uzawa R., Silva P., Cohen S., Bauer M.J.,
RA   Hashimoto M., Kirkbride R.C., Harada J.J., Zilberman D., Fischer R.L.;
RT   "Regulation of imprinted gene expression in Arabidopsis endosperm.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:1755-1762(2011).
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       (By similarity). {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         Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in vegetative and floral
CC       organs. {ECO:0000269|PubMed:10579493}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01016}.
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DR   EMBL; AL161513; CAB78023.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82708.1; -; Genomic_DNA.
DR   PIR; G85090; G85090.
DR   RefSeq; NP_192638.1; NM_116968.1.
DR   AlphaFoldDB; Q9M0S8; -.
DR   SMR; Q9M0S8; -.
DR   STRING; 3702.AT4G08990.1; -.
DR   REBASE; 35200; M.AthMET2b.
DR   iPTMnet; Q9M0S8; -.
DR   PaxDb; Q9M0S8; -.
DR   PRIDE; Q9M0S8; -.
DR   EnsemblPlants; AT4G08990.1; AT4G08990.1; AT4G08990.
DR   GeneID; 826477; -.
DR   Gramene; AT4G08990.1; AT4G08990.1; AT4G08990.
DR   KEGG; ath:AT4G08990; -.
DR   Araport; AT4G08990; -.
DR   TAIR; locus:2122313; AT4G08990.
DR   eggNOG; ENOG502QPKK; Eukaryota.
DR   HOGENOM; CLU_002247_0_0_1; -.
DR   InParanoid; Q9M0S8; -.
DR   OMA; YNQEMDE; -.
DR   OrthoDB; 898916at2759; -.
DR   PhylomeDB; Q9M0S8; -.
DR   PRO; PR:Q9M0S8; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9M0S8; baseline and differential.
DR   Genevisible; Q9M0S8; 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; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.30.490; -; 2.
DR   Gene3D; 3.40.50.150; -; 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   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; SSF53335; 1.
DR   TIGRFAMs; TIGR00675; dcm; 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.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; DNA-binding; Methyltransferase; Nucleus;
KW   Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..1512
FT                   /note="DNA (cytosine-5)-methyltransferase 2"
FT                   /id="PRO_0000430011"
FT   DOMAIN          707..841
FT                   /note="BAH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT   DOMAIN          909..1026
FT                   /note="BAH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT   DOMAIN          1071..1505
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          634..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        635..660
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..678
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1176
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   1512 AA;  171155 MW;  D6D9BCC70DFAC0AE CRC64;
     METKVGKQKK RSVDSNDDVS KERRPKRAAA CRNFKEKPLR ISDKSETVEA KKEQNVVEEI
     VAIQLTSSLE SNDDPRPNRR LTDFVLHNSD GVPQPVEMLE LGDIFLEGVV LPLGDDKNEE
     KGVRFQSFGR VENWNISGYE DGSPGIWIST ALADYDCRKP ASKYKKIYDY FFEKACACVE
     VFKSLSKNPD TSLDELLAAV ARSMSGSKIF SSGGAIQEFV ISQGEFIYNQ LAGLDETAKN
     HETCFVENSV LVSLRDHESS KIHKALSNVA LRIDESQLVK SDHLVDGAEA EDVRYAKLIQ
     EEEYRISMER SRNKRSSTTS ASNKFYIKIN EHEIANDYPL PSYYKNTKEE TDELLLFEPG
     YEVDTRDLPC RTLHNWALYN SDSRMISLEV LPMRPCAEID VTVFGSGVVA EDDGSGFCLD
     DSESSTSTQS NVHDGMNIFL SQIKEWMIEF GAEMIFVTLR TDMAWYRLGK PSKQYAPWFE
     TVMKTVRVAI SIFNMLMRES RVAKLSYANV IKRLCGLEEN DKAYISSKLL DVERYVVVHG
     QIILQLFEEY PDKDIKRCPF VTGLASKMQD IHHTKWIIKR KKKILQKGKN LNPRAGLAHV
     VTRMKPMQAT TTRLVNRIWG EFYSIYSPEV PSEAIHEVEE EEIEEDEEED ENEEDDIEEE
     AVEVQKSHTP KKSRGNSEDM EIKWNGEILG ETSDGEPLYG RALVGGETVA VGSAVILEVD
     DPDETPAIYF VEFMFESSDQ CKMLHGKLLQ RGSETVIGTA ANERELFLTN ECLTVHLKDI
     KGTVSLDIRS RPWGHQYRKE NLVVDKLDRA RAEERKANGL PTEYYCKSLY SPERGGFFSL
     PRNDIGLGSG FCSSCKIKEE EEERSKTKLN ISKTGVFSNG IEYYNGDFVY VLPNYITKDG
     LKKGTSRRTT LKCGRNVGLK AFVVCQLLDV IVLEESRKAS NASFQVKLTR FYRPEDISEE
     KAYASDIQEL YYSHDTYILP PEALQGKCEV RKKNDMPLCR EYPILDHIFF CEVFYDSSTG
     YLKQFPANMK LKFSTIKDET LLREKKGKGV ETGTSSGILM KPDEVPKEMR LATLDIFAGC
     GGLSHGLEKA GVSNTKWAIE YEEPAGHAFK QNHPEATVFV DNCNVILRAI MEKCGDVDDC
     VSTVEAAELV AKLDENQKST LPLPGQADFI SGGPPCQGFS GMNRFSDGSW SKVQCEMILA
     FLSFADYFRP KYFLLENVKK FVTYNKGRTF QLTMASLLEI GYQVRFGILE AGTYGVSQPR
     KRVIIWAASP EEVLPEWPEP MHVFDNPGSK ISLPRGLHYD TVRNTKFGAP FRSITVRDTI
     GDLPLVENGE SKINKEYRTT PVSWFQKKIR GNMSVLTDHI CKGLNELNLI RCKKIPKRPG
     ADWRDLPDEN VTLSNGLVEK LRPLALSKTA KNHNEWKGLY GRLDWQGNLP ISITDPQPMG
     KVGMCFHPEQ DRIITVRECA RSQGFPDSYE FSGTTKHKHR QIGNAVPPPL AFALGRKLKE
     ALYLKSSLQH QS
 
 
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