ID W1W157_9FIRM Unreviewed; 318 AA.
AC W1W157;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 13-SEP-2023, entry version 44.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=Q620_VSAPLC00001G0020 {ECO:0000313|EMBL:ETJ11751.1};
OS Veillonella sp. DORA_A_3_16_22.
OG Plasmid pVSAPL_DORA_A_3_16_22 {ECO:0000313|EMBL:ETJ11751.1,
OG ECO:0000313|Proteomes:UP000050220}.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=1403932 {ECO:0000313|EMBL:ETJ11751.1, ECO:0000313|Proteomes:UP000050220};
RN [1] {ECO:0000313|EMBL:ETJ11751.1, ECO:0000313|Proteomes:UP000050220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC PLASMID=pVSAPL_DORA_A_3_16_22 {ECO:0000313|EMBL:ETJ11751.1,
RC ECO:0000313|Proteomes:UP000050220};
RA Brown C.T., Sharon I., Thomas B.C., Castelle C.J., Morowitz M.J.,
RA Banfield J.F.;
RT "A Varibaculum cambriense genome reconstructed from a premature infant gut
RT community with otherwise low bacterial novelty that shifts toward anaerobic
RT metabolism during the third week of life.";
RL Submitted (DEC-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETJ11751.1}.
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DR EMBL; AZMK01001387; ETJ11751.1; -; Genomic_DNA.
DR AlphaFoldDB; W1W157; -.
DR Proteomes; UP000050220; Plasmid pVSAPL_DORA_A_3_16_22.
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; 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; 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}; Plasmid {ECO:0000313|EMBL:ETJ11751.1};
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 73
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 318 AA; 35932 MW; 8BD61AF2D91877C7 CRC64;
MYSVASFFAG VGGIDLGFEL TKQARTIYAN EIDPYPIQTF EANFPIKVDQ RDICDVKASE
VPNIDIILGG FPCQAFSIAG YRKGFEDEKG RGTLFFEILR IIKAKKPKAI LLENVKNLVS
HDNGNTFRVI LEALKDAGYH VRYAVLNAME YGNIPQNRER IYIVGFKSKK VFEKFTFPEP
IPLKKTIHDV IDFINPVDEK YLYTKGKYKG DIYDKLVAAM DDSNAVYQWR RKYVRKNMSG
VVPTLTANQG EGGHNVCLVK TRQGIRKMTP KECFNTQGFP ESFVLPNIAD GRLYKQAGNS
VCVSVVKRIA EQILVAMK
//
