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Database: UniProt
Entry: R0GKG5_9BRAS
LinkDB: R0GKG5_9BRAS
Original site: R0GKG5_9BRAS 
ID   R0GKG5_9BRAS            Unreviewed;      1531 AA.
AC   R0GKG5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=DNA (cytosine-5)-methyltransferase {ECO:0000256|PIRNR:PIRNR037404};
DE            EC=2.1.1.37 {ECO:0000256|PIRNR:PIRNR037404};
GN   ORFNames=CARUB_v10025739mg {ECO:0000313|EMBL:EOA12790.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA12790.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
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|PIRNR:PIRNR037404,
CC         ECO:0000256|RuleBase:RU000417};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR037404}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family.
CC       {ECO:0000256|PIRNR:PIRNR037404, ECO:0000256|PROSITE-ProRule:PRU01016,
CC       ECO:0000256|RuleBase:RU000416}.
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DR   EMBL; KB870812; EOA12790.1; -; Genomic_DNA.
DR   RefSeq; XP_006279892.1; XM_006279830.1.
DR   STRING; 81985.R0GKG5; -.
DR   GeneID; 17876824; -.
DR   KEGG; crb:17876824; -.
DR   eggNOG; ENOG502QPKK; Eukaryota.
DR   OrthoDB; 317994at2759; -.
DR   Proteomes; UP000029121; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003682; F:chromatin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   CDD; cd04712; BAH_DCM_I; 1.
DR   CDD; cd04708; BAH_plantDCM_II; 1.
DR   Gene3D; 2.30.30.490; -; 2.
DR   Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 2.
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; IPR031303; C5_meth_CS.
DR   InterPro; IPR022702; Cytosine_MeTrfase1_RFD.
DR   InterPro; IPR017198; DNMT1-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR   Pfam; PF01426; BAH; 2.
DR   Pfam; PF00145; DNA_methylase; 2.
DR   Pfam; PF12047; DNMT1-RFD; 2.
DR   PIRSF; PIRSF037404; DNMT1; 5.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SMART; SM00439; BAH; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51038; BAH; 2.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR037404};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|PIRNR:PIRNR037404};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037404};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRNR:PIRNR037404};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037404}.
FT   DOMAIN          736..870
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   DOMAIN          910..1050
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   REGION          657..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        657..687
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..708
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1195
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037404-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   1531 AA;  172295 MW;  2863043147BD50A5 CRC64;
     MVENGVKAMN GKKRALPEIK ETEDVPRTRR PRRAAACTDF KEKSVRLCEK SATIELKKQQ
     TVDEEIVAIM LTAKEGGDAE PRPTRRLNDF VLFDSEGDLQ PVEMLEISDI FVSGAILPSD
     VCSDKEKEKG VRCPSFGRVE NWSISGYEDG SPVIWISTEL ADYDCCKPAA RYKKVYDYFY
     QKACASVAVY KKLSKSSGGD PDICLDELLA AVARSMSGSK YFSSGGAIQD FVISQGEFIY
     NQLAGLDETA KKHETSYAEI PVLVALRDES SKIDKAAQIQ GRPSNGVLRI DGVSEVAVTN
     ALTSKQLVDG ADDDRRYAKL LQDEEYRKSM QRPRKNSSSA SASNKFYIKI NENEIASDYP
     LPSYYKNTKE ETDELMLSDA LYELDAEDLP QRMLHNWTLY NSDSRMISLE LLPMKHCDDT
     DVSIFGSGMV TDDNLCWFSP DDPDSGSHSE DPDGMSIFLS QIKEWKIEYG GEYISISIRT
     DMAWYRLGKP SKQYAPWYKP VLKTATVGIS ILTLLNEQSR LARFSFADVT KRLSGLQTND
     KAYISSDLLS VQRFLIVHGQ IIIQLFAAYP NKKFIKCPFV VGLSSKLEDR HHTKWIIKNK
     KILQKQLNLN PRAEMAPVVS KRKAMRATTT RLVHRIWGEF YSNYSPEDSL QAIGAANEEE
     EVEDQGENGE EEVEEEGENE DVTEETVPEP VEVQKPHTPK KIRASSGKRE IRWDGESLGK
     TSAGEPLYRQ ALVGGETVVV GGAVALEIDV SDELLAIYFV EYMFESTDHC KMLHGRFLQR
     GSATVLGNAS NERELFLTNE CMTVQLKDIK GVVGFEIRSR PWGHQYRKEN IAADKLDRER
     ALERKAKDLP TEYYCKSLYS PERGGFFSLP LSDIGRSSGF CYSCKIREDE EERSTTKLNV
     SNTGFFSNGI EYSIEDFVYV NPDSIDGLKE GSKTVFKSGR NIGLRAYVVC QLLEIVPKES
     RKADLGSFDV KVRRFYRPED VSAEKAYASD IQELYYSQDT DVLHPGALEG KCEVRKKNDM
     PLCREYPISD HIFFCELFFD SSKGSLKQMP ANMKVKFSTI KDDTLLRKKK GKGVEGETES
     GIVKPKEMRL ATLDIFAGCG GLSQGLEKAG VSDTKWAIEY EEPAGQAFRQ NHPASTVFVD
     NCNVILRAIM EKGGDQKDCV STTEADELAA KLSEDQKKTL PLPGQVDFIN GGPPCQGFSG
     MNRFNQSSWS KVQCEMILAF LSFADYFRPR YFLLENVRTF VSFNKGQTFQ LTLASLLEMG
     YQVRFGILEA GAYGVSQSRK RAFIWAAAPE EVLPEWPEPM HVFGVPKLKI SLSQGLHYAA
     VRSTAPGAPF RPITVRDTIG DLPAVENGES RINKEYKAEP VSWFQKEIRG DMISLTDHIC
     KEMNEINLIR CKIIPKRPGA DWRDLPDEKV KLSTGQVVEM IPWCLPNTAK RHNQWKGLYG
     RLDWQGNFPT SITDPQPMGK VGMCFHPDQD RILTVRECAR SQGFPDSYQF FGNIIHKHRQ
     IGNAVPPPLA FALGRKLKEA LQLKNSLQHQ P
//
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