CMT2_MAIZE
ID CMT2_MAIZE Reviewed; 915 AA.
AC Q9ARI6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=DNA (cytosine-5)-methyltransferase 2;
DE EC=2.1.1.37;
DE AltName: Full=Chromomethylase 2;
DE AltName: Full=DNA cytosine methyltransferase MET5;
DE AltName: Full=Zea methyltransferase5;
DE Short=Zmet5;
GN Name=ZMET5;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11487702; DOI=10.2307/3871328;
RA Papa C.M., Springer N.M., Muszynski M.G., Meeley R., Kaeppler S.M.;
RT "Maize chromomethylase Zea methyltransferase2 is required for CpNpG
RT methylation.";
RL Plant Cell 13:1919-1928(2001).
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 Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
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}.
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DR EMBL; AY027539; AAK15805.1; -; mRNA.
DR AlphaFoldDB; Q9ARI6; -.
DR SMR; Q9ARI6; -.
DR PRIDE; Q9ARI6; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q9ARI6; baseline and differential.
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; -; 1.
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; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00145; DNA_methylase; 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; PS00094; C5_MTASE_1; 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..915
FT /note="DNA (cytosine-5)-methyltransferase 2"
FT /id="PRO_0000246695"
FT DOMAIN 188..313
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DOMAIN 345..876
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT DOMAIN 445..508
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 1..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..107
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 521
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
SQ SEQUENCE 915 AA; 101641 MW; 4BA29AC625D076B2 CRC64;
MAPSSPSSAR PTRASGRERS AMAEEIHQNQ EEEEEVVAAS TAKRRRKAAS SGKKPKPTPK
QAKPAVAGMK KKGETEKTEP VVDDVCAEEP DEEELAMGEE EAEAEEQAMQ EVVAAVAAGS
PGKKRVGRRS AAASGDHVPE FIGSPVGAAE AHSNWPKRYE RSTAANKPEE DDELKARCHY
RSAKVDNIVY CLGDDVYVKA GENEADYIGR ITEFFEGTDR CHYFTCRWFF RAEDTVINSL
VSINVDGHKH DPRRVFLSEE KNDNVLDCII SKVKIVHVDP NMDPKAKAQL IEHCDLYYDM
SYSVAYSTFA NISSENGQSG SETASGISSD DAGLETSSNM PERTATLLDL YSGCGGMSTG
LCLGAALSGL KLETRWAVDL NSFACQSLKY NHPQTEVRNE KADEFLALLK EWAVLCEKYV
HQDVDSNLAG SEDQEDADTL DKDEFVVQKL IGIRYDGTGR KKGVYFKVQW EEYGPEEDTW
EPIDNLSDCP LKIREFVQEG RKRKILPLPG DVDVICGGPP CQGISGFNRF RNRDEPLKDE
KNKQMVTFMD IVAYLKPKYV LMENVVDILK FADGYLGKYA LSCLVAMKYQ ARLGMMVAGC
YGLPQFRMRV FLWGALSSMV LPKYPLPTYD VVVRGGAPNA FSQCMVAYDE TQRPSLKKAL
LLGDAFSDLP KVENHQPNDV MEYGGSPKTE FQRYIRLGRK DMLDWSFGEE AGPDEGKLLD
HQPLRLNNDD YERVKQIPVK KGANFRDLKG VKVGANNVVE WDPEVERVYL SSGKPLVPDY
AMSFIKGKSL KPFGRLWWDQ TVPTVVTRAE PHNQVILHPT QARVLTIREN ARLQGFPDYY
RLFGPIKEKY IQVGNAVAVP VARALGYCLG QAYLGESDGS QPLYQLPASF TSVGRTAVQA
NAASVGTPAG EVVEQ
