ID A0A0D9XH79_9ORYZ Unreviewed; 869 AA.
AC A0A0D9XH79;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR10G00200.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR10G00200.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR10G00200.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR10G00200.1}
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; A0A0D9XH79; -.
DR STRING; 77586.A0A0D9XH79; -.
DR EnsemblPlants; LPERR10G00200.1; LPERR10G00200.1; LPERR10G00200.
DR Gramene; LPERR10G00200.1; LPERR10G00200.1; LPERR10G00200.
DR eggNOG; ENOG502QW29; Eukaryota.
DR HOGENOM; CLU_004921_0_0_1; -.
DR Proteomes; UP000032180; 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; 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; 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 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:UP000032180};
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 162..287
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 428..479
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..83
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 504
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 869 AA; 97109 MW; 74E26FF9B568C448 CRC64;
MAPSSPSSDA PSRRASTRKR AASAKVAEAD LDQPSTKRAR KAAAAPKAPA RTKKEKEVED
DVCGEEPDEE EIAMGEEAEA EQEQQLEAPA LPAKKRVAQP SRVRHNADGD HEPEFVGDPI
PANEARAKWP QRYQRGAAAR RPDEEEELKA RCHYRSAKVD NIIYSLGDDV YVKAEEGQVD
YIGRIIELFE GTDLARYFTC RWFFRPEDTV ISSMMMENVH DHKHDLKRVF LSEEKNDNVL
DCIISKVKMV HIDPNMDAEA RAQRVADCQL YYDMSYTVAY STFANIPFEN GASGSDTASG
ISSDDVDSAK GKVASDSEAS SSVGKATLLD LYSGCGGMST GLCLGAALAG LNLETRWAVD
LNSYACESLK YNHPKTEVRN EKADEFLALL REWAKLCDQY IKNDIDSDLA GSSENEEEDD
EPLEKNEFVV EKLSGICYGG NGRDGGLYFK VQWKGYGREE DTWEPIENLS ECPLKIKEFV
QDGYRRKILP QPGDVDVICG GPPCQGISGF NRFRNRKEPL KDEKNKQMVT FMDIVAYLKP
KYVLMENVVD ILKFADGYLG RYALSRLVAM NYQARLGMMV AGCYGLPQFR MRVFLWGALP
TMVLPKYPLP THNVVVRGGA PNAFSVHNNQ PNEVMEYGSS PKTEFQRYIR LSRREMLDTS
FEVGADPNVG KLLDHQPLRL NNDDFERVKQ IPIKKGANFR DLTGVKVGVN NIVEWDPNIE
RVYLSSGKPL VPDYAMSFIK GRSLKPFGRL WWDETVPTVV TRAEPHNQII LHPSQARVLS
VRENARLQGF PDYYKMYGPI KEKYIQVGNA VAVPVARALG YCLGLAYRGE TDESSPLFAL
PDSFTALGQR VAPIVDSSVA IPAGEVVEE
//
