ID A0A095XWF8_9BACT Unreviewed; 451 AA.
AC A0A095XWF8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=HMPREF1640_13325 {ECO:0000313|EMBL:KGF14111.1};
OS Prevotella sp. S7-1-8.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1284775 {ECO:0000313|EMBL:KGF14111.1, ECO:0000313|Proteomes:UP000029597};
RN [1] {ECO:0000313|EMBL:KGF14111.1, ECO:0000313|Proteomes:UP000029597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S7-1-8 {ECO:0000313|EMBL:KGF14111.1,
RC ECO:0000313|Proteomes:UP000029597};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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:KGF14111.1}.
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DR EMBL; JRNC01000110; KGF14111.1; -; Genomic_DNA.
DR RefSeq; WP_036895197.1; NZ_JRNC01000110.1.
DR AlphaFoldDB; A0A095XWF8; -.
DR eggNOG; COG0270; Bacteria.
DR OrthoDB; 32195at2; -.
DR Proteomes; UP000029597; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000029597};
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 82
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 451 AA; 51211 MW; DB1B03F2F0515A07 CRC64;
MHNYTIKFID LFAGLGGIRI GFEEAAAELG INTKCVFTSE IKDSALKAYQ FNFNEDIPKR
DITKVDAGEI PEFNILLGGF PCQAFSFAGS QKGFADTRGT LFFEIERILR HHLKNVDGFL
LENVEGLIEH QKEFKSDPYG RTLKVILTVL REKLKFNTEF ILLNASDFGV AQARKRVYIV
GCKKKYGSIK FAFSNIPQKT VGECIDYGMA CPQTDFTKLL LEHYNVKELE GKFLKDKRGG
ASNIHSWDFE YKGKVSAKQK ELLNLLFKQR RRHSWAEAIG IEWMDGMPLT TKQISTFFND
ENLQSMLDDL VCKNYLVLEY PKKKIYHNEN GSSYTERVPD ETLPKGYNIV TGKLSFPISH
ILPSKGIAPT IVAMDMNTLG VIDNSGIRHL TLKEGLRLFG YPSWYSLEEF NKSPRTIKLG
YDLLGNSVCV PVIKAVAKVL LSNLKKKYEK N
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