ID A0A1T4KQY6_9FIRM Unreviewed; 376 AA.
AC A0A1T4KQY6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=SAMN02745110_00524 {ECO:0000313|EMBL:SJZ44812.1};
OS Eubacterium ruminantium.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=42322 {ECO:0000313|EMBL:SJZ44812.1, ECO:0000313|Proteomes:UP000189857};
RN [1] {ECO:0000313|EMBL:SJZ44812.1, ECO:0000313|Proteomes:UP000189857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17233 {ECO:0000313|EMBL:SJZ44812.1,
RC ECO:0000313|Proteomes:UP000189857};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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|RuleBase:RU000417};
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; FUXA01000004; SJZ44812.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4KQY6; -.
DR OrthoDB; 9813719at2; -.
DR Proteomes; UP000189857; Unassembled WGS sequence.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.90.120.30; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00675; dcm; 1.
DR PANTHER; PTHR46098; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR46098:SF1; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Reference proteome {ECO:0000313|Proteomes:UP000189857};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
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 ACT_SITE 80
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 376 AA; 43253 MW; 96AFE8F59E62598C CRC64;
MSKRPRYKTI DLCAGIGGIR RGFEMTGRYV NVLSAEIDKY ACQTYERLFG VNPFNDLTSE
DFKKKVASVE YDVLLAGFPC QTFSRVGLQK GFNDEEKGQI FFHISEIIRS NRPKAIFLEN
VDRLITHDEG KTFEKIIDVL VNDLDYHVVG VDRDDNGQIR YDKDSFIRNS RFFGMPQNRP
RTYIVCFDKK RYDDKVKKAV PVATPDKGSM MVYENLDELL SHDVDDKYYL SSGYWNTLKE
HRKRQEKKGY GYGYRIVNMP DDGVHIANTI LATGGSGKER NLLIDYKDGV SGKSIVGKKT
PLNDEYVRVM TPTEWGKLQG FINYGFIDKD GKDQFEFPEG MSDAQKYKQF GNSVTIPVIK
EFAVFIDRCL KKLEES
//