ID A0A1V2SNW2_9STRE Unreviewed; 451 AA.
AC A0A1V2SNW2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=BVE84_04245 {ECO:0000313|EMBL:ONK29897.1};
OS Streptococcus azizii.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1579424 {ECO:0000313|EMBL:ONK29897.1, ECO:0000313|Proteomes:UP000188946};
RN [1] {ECO:0000313|EMBL:ONK29897.1, ECO:0000313|Proteomes:UP000188946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-5202 {ECO:0000313|EMBL:ONK29897.1,
RC ECO:0000313|Proteomes:UP000188946};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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}.
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:ONK29897.1}.
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DR EMBL; MSPR01000006; ONK29897.1; -; Genomic_DNA.
DR RefSeq; WP_000670052.1; NZ_MSPT01000007.1.
DR AlphaFoldDB; A0A1V2SNW2; -.
DR SMR; A0A1V2SNW2; -.
DR STRING; 1579424.BVE84_04245; -.
DR GeneID; 83690494; -.
DR OrthoDB; 9813719at2; -.
DR Proteomes; UP000188946; 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; 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}; 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 77
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 451 AA; 51147 MW; C8C151B89F608185 CRC64;
MKFLDLFAGI GGFRLGMESQ GHKCLGFCEI DKFARTSYKA MFNTEGEIEY HDIKEVTDHD
FRQFRGQVDI ICGGFPCQAF SLAGRRLGFE DTRGTLFFEI ARAAKQIQPR FLFLENVKGL
LNHDEGRTFA TILSTLDELG YDVEWQVLNS KDFQVPQNRE RVFIIGHSRR YRSRFIFPLR
REDSPAHLER LGNINPSKHG LNGEVYLTSG LAPTLTRGKG EGAKIAIPVL TPDRLEKRQH
GRRFKDNQDP MFTLTSQDKH GVVVAGNLPT SFDQTGRVFD ISGLSPTLTT MQGGDKVPKI
LLREELPFLK IKEATKTGYA KATLGDSVNL AYPDSTKRRG RVGKGISNTL TTSDNMGVVV
AALEYRQDKW YEVTGIVLEG KLYRLRIRRL TPRECFRLQG FPDWAYERAE SVSSKSQLYK
QAGNSVTVTV IEAIAREFRR TEEEEKHELT T
//
