ID A0A1B7M2H3_9MICC Unreviewed; 382 AA.
AC A0A1B7M2H3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=A6F49_04690 {ECO:0000313|EMBL:OAV62807.1};
OS Enteractinococcus helveticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae.
OX NCBI_TaxID=1837282 {ECO:0000313|EMBL:OAV62807.1, ECO:0000313|Proteomes:UP000078292};
RN [1] {ECO:0000313|EMBL:OAV62807.1, ECO:0000313|Proteomes:UP000078292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UASWS1574 {ECO:0000313|EMBL:OAV62807.1,
RC ECO:0000313|Proteomes:UP000078292};
RA Crovadore J., Chablais R., Lefort F.;
RT "First whole genome shotgun sequence of the bacterium Enteractinococcus sp.
RT strain UASWS1574.";
RL Submitted (APR-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:OAV62807.1}.
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DR EMBL; LXEY01000008; OAV62807.1; -; Genomic_DNA.
DR RefSeq; WP_052499957.1; NZ_LXEY01000008.1.
DR AlphaFoldDB; A0A1B7M2H3; -.
DR STRING; 1837282.A6F49_04690; -.
DR REBASE; 164998; M.Ehe1574ORF4690P.
DR OrthoDB; 9813719at2; -.
DR Proteomes; UP000078292; 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}; 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 98
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 382 AA; 41518 MW; E24A30BEBD95AE49 CRC64;
MTLTAVSTAA AFRVPILHDP APLSRPTVIS LFAGAGGTAL GFDHAGFDHV LLSEIDNDAV
ATLAANRPEW TVTHGDVTDI DFTPFYDQVD VVEGGFPCQA FSYAGNRQGL ADTRGTMFFE
FSRAIAQVMP KVFVGENVRG LLSHDKGRTI VTMLDELSAI QDPSTGASYR IGYRIVKSQD
HFVPQNRLRV IIVGVRSDVG DTTFFPKDQQ QLYTLEDAIG DRPQGDGQAY SEAKHAVLDM
VPAGGHWRDL PDNIAKSYLG KAYYGSGGRT SIARRLAWTK ASPTLTCSPA QKQTELCHPD
ETRPLNVREY ARIQTFPDNW HFAGGIGSQY RQIGNAVPVN LGFFLAQAVR AMLGETEPID
SGYVEQATPT DLYTGAPDTV GT
//
