ID A0A1M4XA19_9FIRM Unreviewed; 279 AA.
AC A0A1M4XA19;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=SAMN02745784_02179 {ECO:0000313|EMBL:SHE90330.1};
OS Tissierella praeacuta DSM 18095.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Tissierellaceae;
OC Tissierella.
OX NCBI_TaxID=1123404 {ECO:0000313|EMBL:SHE90330.1, ECO:0000313|Proteomes:UP000184114};
RN [1] {ECO:0000313|Proteomes:UP000184114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18095 {ECO:0000313|Proteomes:UP000184114};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) 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; FQTY01000010; SHE90330.1; -; Genomic_DNA.
DR RefSeq; WP_072976256.1; NZ_FQTY01000010.1.
DR AlphaFoldDB; A0A1M4XA19; -.
DR STRING; 1123404.SAMN02745784_02179; -.
DR Proteomes; UP000184114; 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; 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; 2.
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:UP000184114};
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 74
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 279 AA; 31582 MW; 653DA20FA6B93525 CRC64;
MNKQFKFIDL FSGIGGFHYG LAQCGGQCVL ASDIDSSARK TYEINFGIQP AGDICELKSN
EIPEFDLLCA GFPCQSFSNI GTKRGLKDPR GALIYEVIRI LNDCSPKAFI LENVKGLLTH
DKGNTFRIIK SLLENCEYNV FYNILEAKDY GVPQIRKRLF IVGIKKEYDI KFNYPKPTGC
IKKLSDILGG DTEREYSFTI RIGGRRSGID NRFNWDCYNV NGQPHYLQVE ECLELQGFPR
DFHLFGNQSE KFKQVGNAVP TVIVRALGEE LIKTKIFSL
//
