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Database: UniProt
Entry: A0A0D9WE21_9ORYZ
LinkDB: A0A0D9WE21_9ORYZ
Original site: A0A0D9WE21_9ORYZ 
ID   A0A0D9WE21_9ORYZ        Unreviewed;      1256 AA.
AC   A0A0D9WE21;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   22-FEB-2023, entry version 28.
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:LPERR05G06410.2, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR05G06410.2, 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:LPERR05G06410.2, 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:LPERR05G06410.2}
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; A0A0D9WE21; -.
DR   EnsemblPlants; LPERR05G06410.1; LPERR05G06410.1; LPERR05G06410.
DR   EnsemblPlants; LPERR05G06410.2; LPERR05G06410.2; LPERR05G06410.
DR   Gramene; LPERR05G06410.1; LPERR05G06410.1; LPERR05G06410.
DR   Gramene; LPERR05G06410.2; LPERR05G06410.2; LPERR05G06410.
DR   Proteomes; UP000032180; Chromosome 5.
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   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; 2.
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; IPR031303; C5_meth_CS.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10629:SF34; DNA (CYTOSINE-5)-METHYLTRANSFERASE CMT2; 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; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS00598; CHROMO_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          592..709
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   DOMAIN          852..905
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..304
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        930
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   1256 AA;  137279 MW;  64ED647DC34FAB35 CRC64;
     METPPPDENP VSPPAAADDS PPGGGGGGGG GDGDDGAEEA GGFRAGLEPL WTVLFGSPEE
     LEPMWSPPRG FEFDAAPEVE PDMDVAGAWD GLPWRSTGLV AGEGAGFAEF GGEIGTSAGA
     NSVDAAPEVS ALDSGADCSP ELPLSSSSPP VDLELRAFEP VDDSAPATDS RIPTSVASSE
     ANLDGRMVEC TLNSVPSPPF PSPDDIGLGA EDTIKDCSPL EKVALGTLAS VDMDVEDPQM
     NAAGNCMTGA SGTVDTSLRR SPRIAKVKSE AAASSIPLNQ NADSPRVSKR NLTDSKKRRS
     SEGSKLPVFA RPVSLNTNDL INGVEIEGLR DIVAVRSKSS SYENKNNECL HNQVVVALPA
     VNSDKGASVH SPRKTRPASK ALVNSDRVSA ISPMVNGGPP VQKSDSYTPT KRHKLAVAEC
     LPNLDGVVGG GGGIVSCNSR LKSAKPQVVN KMPQGRGGRS SQPPKTKRGK TLSVKYLEKL
     KRAENANGSK FGSPRVTVMS ELSTKHKLIL DKQLTDSDMF EMDDGSCFFV GDAVPDDEAR
     KQWPHRYEIN DQIMKKFSTL NDERISGQTF ANVGKPVLDV KCHYLQAKVS RYTFCIGDCA
     FIKGPEGKPN YIGRLLEFFE TKAGEYYFGV QWFFRAEDTV MEKQAQSHDP RRLFYSDLTD
     DNLLDCIVSK VTIVQVPPSM DGKSKSDTSF DYYYDMKYSM DYSTFSTIEM GSANNVVQSS
     YTGINNDKMK INVNEKHKSP TLEKRDLSLL DLYCGCGGMS TGLCLGARGG GVNLSARWAI
     DVDEIACESL RHNHPETRVR NETTDDFLQL LKEWEKLCKT YLKHSKAKAC PDSTTESNNE
     TPDCSTAPPE EFEVWKLVDI CFGDPNNVSK RCLYFKVRWK GYSLHYDTWE PVEGLRNCKE
     AIRDFVIEGH KHKILPLPGD VDVVCGGPPC QGISGYNRNR EFEEPFKSRL GIMAAGCYGL
     PQFRMRVFLL GCHSKEKLPP FPLPTHEAIV KNGCPLAFER NLVGWPNNTP MQLAKPIVLE
     DILSDLPEVA NGESRDEMLY VKGPQTEFQR YIRSFNAEVP GPKARVAKDS KLSKLYDHRP
     LALDNDNYQR VLQIPKKKGA NFRDLPGVIV GPDNVARLDP TRERILLSSG RPLVLDCILS
     YENGKCLRPF GRVWWDEVVG TVLTVPNIRM QALIHPAQDR VLTIRESARL QGFPDNYRFC
     GTVKDRYRQI GNAVAIPVGR ALGYALAMAY LKKAGDDPLM VLPPNFAFSH DIGGFT
//
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