ID A0A0E0EV60_9ORYZ Unreviewed; 931 AA.
AC A0A0E0EV60;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
OS Oryza meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI10G00140.1};
RN [1] {ECO:0000313|EnsemblPlants:OMERI10G00140.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI10G00140.1};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI10G00140.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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:0000256|ARBA:ARBA00000743};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01016}.
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DR AlphaFoldDB; A0A0E0EV60; -.
DR STRING; 40149.A0A0E0EV60; -.
DR EnsemblPlants; OMERI10G00140.1; OMERI10G00140.1; OMERI10G00140.
DR Gramene; OMERI10G00140.1; OMERI10G00140.1; OMERI10G00140.
DR eggNOG; ENOG502QW29; Eukaryota.
DR HOGENOM; CLU_004921_0_0_1; -.
DR Proteomes; UP000008021; Chromosome 10.
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; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0044027; P:negative regulation of gene expression via CpG island methylation; IEA:EnsemblPlants.
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; 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 PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10629:SF59; DNA (CYTOSINE-5)-METHYLTRANSFERASE CMT1-RELATED; 1.
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; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01016};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01016}.
FT DOMAIN 170..295
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 435..489
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 1..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..85
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 511
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 931 AA; 104140 MW; 3D7B81EE7C88F1A8 CRC64;
MAPSSPSSAA APTRTSTRKR AASAKGTDEP STKRTRRPKA DPKPRRNKDE VKEEEKPPVE
DDACGEEPDA EEMALGEEAE AEEAEAEQKQ LDAPAPAPGV ARKRVAQPSR VRHGSDGDHD
PEFVGDPFPA KEARDKWPQR YQRNAATRRP DEEEDIKARC HYSSAKVDGT LYCLHDDVYV
KAEEDKADYI GRITEFFEGT DHCRYFTCRW FFRAEDTVIS SIMMENADDE KHDLKRVFLS
EEKNDNVLDC IISKVKIVHI DPNMDPEAKA QRLADCDLYY DMSYTVAYST FANIPLENGA
SGSDTASDIS SDDVDSSKGK VISDSEASSV GKATLLDLYS GCGGMSTGLC LGAALAGLNL
ETRWAVDFNS FACESLKYNH PRTEVRNEKA DEFLALLKGW HSLCDEYVKK DIDFSSAGAS
ENEEDDDEPL EKDEFVVEKL AGICYGGSGR EDGLYFKVQW KGYGREEDTW EPIENLRDCP
LKIKEFVQEG YRRKILPLPG DVDVICGGPP CQGISGFNRF RNRKEPLKDE KNKQMVTFMD
IVAYLKPKYV LMENVVDILK FADGYLGRYA LSRLVAMKYQ ARLGMMVAGC YGLPQFRMRV
FLWGALPAMV LPKYPLPTHN VVVRGGAPNA FSQSIVAYDE TQKPTLKNAL LLGDAISDLP
EVNNHQPNEV MEYGSSPKTE FQRYIRLSRK EMLDSSFEGK DGPDLGKLLD HQPLKLNKDD
HERVQQIPVK KGANFRDLKG VRVGANNIVE WDPDIPRVYL SSGKPLVPDY AMSFIKGRSL
KPFGRLWWDE TVPTVVTRAE PHNQVQLSRK YNNFYISASF LNVSECASLQ IILHPNQARV
LTVRENARLQ GFPDYYKMFG PIKEKYIQVG NAVAVPVARA LGYSLGLAYQ RESEGSSPLF
VLPDSFTEVG RQAAPARASS VGIPVGEVVE Q
//
