ID A0A078IHK3_BRANA Unreviewed; 1431 AA.
AC A0A078IHK3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=DNA (cytosine-5)-methyltransferase {ECO:0000256|PIRNR:PIRNR037404};
DE EC=2.1.1.37 {ECO:0000256|PIRNR:PIRNR037404};
GN Name=BnaA09g42250D {ECO:0000313|EMBL:CDY49442.1};
GN ORFNames=GSBRNA2T00093026001 {ECO:0000313|EMBL:CDY49442.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY49442.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY49442.1, ECO:0000313|Proteomes:UP000028999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
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; LK032833; CDY49442.1; -; Genomic_DNA.
DR STRING; 3708.A0A078IHK3; -.
DR PaxDb; 3708-A0A078IHK3; -.
DR EnsemblPlants; CDY49442; CDY49442; GSBRNA2T00093026001.
DR Gramene; CDY49442; CDY49442; GSBRNA2T00093026001.
DR OMA; GAVIQME; -.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:UniProtKB-UniRule.
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; 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; IPR006058; 2Fe2S_fd_BS.
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; 3.
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; PS00197; 2FE2S_FER_1; 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:UP000028999};
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 632..770
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 810..947
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..590
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1096
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-1,
FT ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 1431 AA; 162099 MW; CD06A3AB6C03D149 CRC64;
MVRNGTKAGE QKKRPLPEIK ADSDGEDLST RHTRPKRAAA CTNFKEKSVR ISEKSATVET
KQHQTVEDEV EKGRGVKCDG FGRVENWSIS GYDDGYPVVW FSTELADYDC GKPATSYKKM
YDYFYQKAFA SVEVYKRVAK SAGGDSGVSL DELLVAVSRS MSLESKCFST DFLVIRNFLI
RQGEFIYNQL AGLDETAKKD EASFAEIPVL VALRDENSRL DNGAVIQMEG RPSNGVLRID
GVSEAAKCEA LISDQEMVDE DQRYARIMQD EEDRKTMQRP KRNNGAALAS NKGYVKTTED
EIAGDYPLPA YYKNFKDEAD ELIVADDYEV NYEDLPRRML HNWALYNSDS RFISLELLPM
KPCADIDVTI FGQIKEWMIE WGCSTISISI RTDVAWYRLG KPSKQYAPWF EPVLKTARVT
IGIFGLLEEQ TRMSKLSFED VTKRVSEFQK NDKAFISSDR LAVNRFLVGH GQIILQMFSE
FPKKDIQRCS FVSDLARKRA ERHNTRWTIK KKKILFKVNC NPRAGMAPVV SKRKAMQATT
TRLINRIWGE FYSNYSPEEP VQAVGVENEE EEVEEEGEIE EDDAEETVPE PVEEVEKFHT
PLKKIRGVSG KTESSWSGES LGKTSAGEPL YRQALVGEEI VAVGGAVVLE DEGNEVIYFV
EYMFEKSNNC KMLHGRLLQR GCDTVLGNAA NERELFLTNE CKTVSLKEIK GTVSFEIRSR
PWGHQFRKEN TTADKLDRAR AEERKTKDLP TEYFCKSLYS PERGGFFSLP LNDMGCASGT
CSSCRIREDE EKKTEIKLNS SKTGFSCNGV DYSDDDYVYV KPEDIDGSKE ANGRFKSGRN
IGLRPFVVCQ ILEIIVLKES RKASFEVKVR RLYRPEDVSD EKAYASDIQE LYYSEDTDVL
QPEALEGKCE VRKKIDMPSR REYPISDNIF FCEQIYDPSK GSLKQLPVNI KPKYTTVKDE
ALLRKRKGKG LVTETDSVTD KPEEVSKETR LATLDIFAGC GGLSQGLEQA GVSATKWAIE
YEEPAGKAFR KNHPETTVFV DNCNVILRAI MEKCGDQDEC ISTKEANELA EKLDEDQKRT
LPLPGQVDFI NGGPPCQGFS GMNRFNQSSW SKVQCEMILA FLSFADYFRP RYFLLENVRT
FVSFNKGQTF QLTLASLLEM GYQVRFGILE AGAYGVSQSR KRAFIWAAAP DEVLPEWPEP
MHVFGVPELK ISLSKGVHYA AVRSTQYGAP FRPITVRDTI GDLPSVVNGE SNTKREYKSQ
PISWFQKEIR GDNIALTDHI CKEMNELNLI RCKKIPKRPG ADWRDLPEEK VTLSKGQVVD
LIPWCLPNTA KRHNQWKGLF GRLDWEGNFP TSITDPQPMG KVGMCFHPDQ DRIITVRECA
RSQGFPDSYV FQGNIIHKHR QIGNAVPPPL AFALGRKLKE AVQLKSVTKT N
//