CMT3_MAIZE
ID CMT3_MAIZE Reviewed; 915 AA.
AC Q8LPU5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=DNA (cytosine-5)-methyltransferase 3;
DE EC=2.1.1.37;
DE AltName: Full=Chromomethylase 3;
DE AltName: Full=DNA methyltransferase 105;
GN Name=DMT105;
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].
RA Chandler V.L., Kaeppler S.M., Kaeppler H.F., Cone K.C.;
RT "Sequences from the plant chromatin consortium.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bergstrom D., Springer N.M., Schmitt L.T., Guthrie E., Sidorenko L.,
RA Selinger D., Kaeppler S.M., Cone K.C.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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; AY093416; AAM28227.1; -; mRNA.
DR RefSeq; NP_001105167.2; NM_001111697.2.
DR AlphaFoldDB; Q8LPU5; -.
DR SMR; Q8LPU5; -.
DR STRING; 4577.GRMZM2G005310_P02; -.
DR REBASE; 5016; M.ZmaV.
DR PaxDb; Q8LPU5; -.
DR PRIDE; Q8LPU5; -.
DR GeneID; 542060; -.
DR KEGG; zma:542060; -.
DR eggNOG; ENOG502QW29; Eukaryota.
DR OrthoDB; 898916at2759; -.
DR Proteomes; UP000007305; Chromosome 2.
DR ExpressionAtlas; Q8LPU5; baseline and differential.
DR Genevisible; Q8LPU5; ZM.
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 3"
FT /id="PRO_0000246696"
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..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..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; 101611 MW; D1F4031F729C6A56 CRC64;
MAPSSPSSAR PTRASGRKRS AMAEEIHQNQ EEEEEVVAAS TAKRRRKAAS SGKKPKPTPK
QAKPAVAGMK KKGETEKTEP VVDDVCAEEP DEEELAMGEE EAEAEEQAMQ EVVAAVAAGS
PGKKRVGRRS AAASGDHVPE FIGSPVAAAE 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 EGYGPEEDTW
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 KPFGRLWWDE TVPTVVTRAE PHNQVILHPT QARVLTIREN ARLQGFPDYY
RLFGPIKEKY IQVGNAVAVP VARALGYCLG QAYLGESDGS QPLYQLPASF TSVGRTAVQA
NAVSVGTPAG EVVEQ
