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Database: UniProt
Entry: B9S1U5_RICCO
LinkDB: B9S1U5_RICCO
Original site: B9S1U5_RICCO 
ID   B9S1U5_RICCO            Unreviewed;       734 AA.
AC   B9S1U5;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE            EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN   ORFNames=RCOM_0868250 {ECO:0000313|EMBL:EEF42564.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
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         ECO:0000256|RuleBase:RU000417};
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, ECO:0000256|RuleBase:RU000416}.
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DR   EMBL; EQ973844; EEF42564.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9S1U5; -.
DR   STRING; 3988.B9S1U5; -.
DR   eggNOG; ENOG502QT36; Eukaryota.
DR   InParanoid; B9S1U5; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; IBA:GO_Central.
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; 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; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00675; dcm; 1.
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; PS50013; CHROMO_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:EEF42564.1};
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:UP000008311};
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          2..120
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   DOMAIN          272..328
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   ACT_SITE        350
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   734 AA;  83320 MW;  0277DEC7AECA6D0C CRC64;
     MNKFYGNDLH YDQLLQGEGG QKHVGRIVEF FKTTDGEDYF RVQWFYRAED TVIKEEAGFH
     DKKRLFYSTI MNDNPIDCII SKVRIVQLPS MIGSKSSIRS TDFYFDMEYN VDYSSFRTLL
     IGKHFCLRDN SSSPNVVEAV STTGGNTSLE NMRSSESNKA ELALLDLFSG CGGMSTGLCL
     GAKVSCVDLV TRWALDSNKS ACESLKLNHP ETNVRNEAAE DFLELLKVWE KLCKRYAVKD
     IKSMQQSRSI ASRVAEENDN SLSDNDITPG EYEVSKLVDL CYGDPDNIGK RGLKFKVHWK
     GYSTSEDTWE PVEGLRNCQE CIRDFVRKGF KSKILPLPGD VDVICGGPPC QGISGYNRFR
     NVNAPLSDER NRQIVVFMDI VQFLKPKFVL MENVVDILKF DKASFARYAL SRLVHMKYQA
     RLGTIAAGCY GLPQFRLRVF LWGAHPSEKL PQFPLPTHDV IVRYWPPNEF ERNTVAYDEG
     QPRELEKAAV LQDAISDLPP VTTHETREEM AYEKPPETEF QRFIRSTEHE MTGSSQRGTT
     QMNNLLSDHR PYALTEEDCA RVCLIPKRKG ANFRDLPGIL VGNDNVVRRD PTKEQVLLPS
     GKPLVPDFAF TFEQGKSKRP YARLWWDETV PTVVTYPSIH SQAMLHPEQD RALTIRECAR
     LQGFPDYYRF SGTVKERYRQ IGNAVAVPVG RALGYALGMA FLKLSGDGPL MTLPPKFSHS
     TNLQLAKSLF QKTD
//
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