ID A0A3B6HR94_WHEAT Unreviewed; 930 AA.
AC A0A3B6HR94;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN ORFNames=CFC21_051583 {ECO:0000313|EMBL:KAF7041849.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS4A02G077400.1};
RN [1] {ECO:0000313|EMBL:KAF7041849.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7041849.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS4A02G077400.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS4A02G077400.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS4A02G077400.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7041849.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7041849.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CM022220; KAF7041849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6HR94; -.
DR SMR; A0A3B6HR94; -.
DR STRING; 4565.A0A3B6HR94; -.
DR PaxDb; 4565-Traes_4AS_0194CD713-1; -.
DR EnsemblPlants; TraesCS4A02G077400.1; TraesCS4A02G077400.1; TraesCS4A02G077400.
DR Gramene; TraesCS4A02G077400.1; TraesCS4A02G077400.1; TraesCS4A02G077400.
DR Gramene; TraesCS4A03G0156400.1; TraesCS4A03G0156400.1.CDS; TraesCS4A03G0156400.
DR OMA; FRNTKEP; -.
DR OrthoDB; 1215065at2759; -.
DR Proteomes; UP000019116; Chromosome 4A.
DR Proteomes; UP000815260; Chromosome 4A.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; 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:SF60; DNA (CYTOSINE-5)-METHYLTRANSFERASE CMT1; 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:UP000019116};
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 197..321
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 464..520
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 1..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..67
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 542
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 930 AA; 104151 MW; 3B0353E217641D82 CRC64;
MASMSPVTPA AAEPRRSTRL LSNTKPADAD ADADAEAEVE RERSTSRGGK RRRKAAGKGT
GARKRAAKGK RKEPESAAGA MEVEDAGSGI NGDVYPEEPD SEEMKLIEEE EQADHGEEGS
AETRGARKRV APPRAQRRPE ASADHFVGEP IPDDKARRLW PSRYETKDSD SRSRRSNDPE
EEIGAQCHYT SACVDDAIFN LNDDVYVKAG PNEENYIGRI TEFFEGTDHV LYFTCRWFFR
AEDTVISPNL LEVHDHEHDQ KRVFLSEEKN DNMIESIISK LNIIYVDPSK TPQERDQLIS
NSDLYYDMSY SVAYSTFANI PAENDGATDS EVASDISCEE GKPVADPVGS SDARRETATL
LDLYSGCGAM STGLCLGAAL SGIKLNTKWA VDMNEYACNS LKHNHPGTQV RNEKAEDFLA
LLQHWNALCQ KYVVHSSNSS GSDLAQMSND DEDDENEALP NDLFEVERLL DICYGDPNKT
GKDGLWFKVR WKTYDPSHDS WEPIDGLSDS PECIKEFVQR GYRESILPLP GSVDVICGGP
PCQGISGLNR FRNYNEPLED DRNKQLVVFM DVVNYLRPKY VLMENVVDIL KFADGFLGRY
ALSRLVSMRY QARLGLMVAG CYGLPQFRMR AFLWGALPSR VLPKFPLPTH DVVKRGVVPN
AFSQCLVAYD EIDDKRLKKA LVLQDALSDL PKVPNYQPND LMENRINPKT EFQRYIRLSR
KDMEDYSFGD ATPSPKACQL FDHQPLELST DDYQRVKQIP FRKGANFRDL KGVQVGENNT
VEFNPHIPRV FLPSGKPLVP YYAMTYIKGK SPKPFGRLWW DETVPTVVTR AEPHNQIILH
PNQHRVLTVR ENARLQGFPD YYRLFGPIKQ KYIQVGNAVA VPVARALGYS LGQAYRGALV
GGQPLFELPE NFASVGQAAA TASPVGVVEK
//
