ID A0A1T4R669_9ENTE Unreviewed; 386 AA.
AC A0A1T4R669;
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=SAMN02745116_02454 {ECO:0000313|EMBL:SKA11582.1};
OS Pilibacter termitis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Pilibacter.
OX NCBI_TaxID=263852 {ECO:0000313|EMBL:SKA11582.1, ECO:0000313|Proteomes:UP000190328};
RN [1] {ECO:0000313|EMBL:SKA11582.1, ECO:0000313|Proteomes:UP000190328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1030 {ECO:0000313|EMBL:SKA11582.1,
RC ECO:0000313|Proteomes:UP000190328};
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; FUXI01000040; SKA11582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4R669; -.
DR STRING; 263852.SAMN02745116_02454; -.
DR OrthoDB; 9813719at2; -.
DR Proteomes; UP000190328; 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 CDD; cd00315; Cyt_C5_DNA_methylase; 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; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR031303; C5_meth_CS.
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; 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; PS00095; C5_MTASE_2; 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:UP000190328};
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 111
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 386 AA; 43995 MW; 927EA69A4327BEC2 CRC64;
MPSSYFNLNY NTVDTKKIEV DEATKPLNVV SLFSGAGGMD LGFRGGFEYL GEEYDKNPFN
LVFANDIFQQ AADVYEANFE HKVERRSIAD LDMKKDMPDI DVDIILGGFP CQTFSYSGKR
AGLSDERGQL YLQMIRVIDH YKPKMFIAEN VDGIRNSKKN VEGENVDKSA LSVILDDFEE
HGYDVQYRVL TAADYGVPQM RRRVIIMGIR KDLGGVDNEF YPQQLFDETG ELTGRVWRTS
KDGIDDLWDK VNNPNIPNHT LKDISRAKFY PGKKMQGNNR ISENRPAPTI RAEHHGNIEA
HYRTTVEDET DMSGWRRLSV RECARLQSFP DSFNFVTSAS SAYKAVGNAV PPVMAWHIAR
SVFFTLQQLD QIEFKKVNEH ELVATK
//
