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Database: UniProt
Entry: A0A1I1LJZ7_9BACT
LinkDB: A0A1I1LJZ7_9BACT
Original site: A0A1I1LJZ7_9BACT 
ID   A0A1I1LJZ7_9BACT        Unreviewed;       356 AA.
AC   A0A1I1LJZ7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE            EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN   ORFNames=SAMN05421780_1095 {ECO:0000313|EMBL:SFC73361.1};
OS   Flexibacter flexilis DSM 6793.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flexibacteraceae;
OC   Flexibacter.
OX   NCBI_TaxID=927664 {ECO:0000313|EMBL:SFC73361.1, ECO:0000313|Proteomes:UP000199514};
RN   [1] {ECO:0000313|EMBL:SFC73361.1, ECO:0000313|Proteomes:UP000199514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6793 {ECO:0000313|EMBL:SFC73361.1,
RC   ECO:0000313|Proteomes:UP000199514};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FOLE01000009; SFC73361.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1LJZ7; -.
DR   STRING; 927664.SAMN05421780_1095; -.
DR   Proteomes; UP000199514; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199514};
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        85
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   356 AA;  40481 MW;  6F9D4E444C6A724B CRC64;
     MMTNMLNNTV VIDLFCGIGG LSHGFVKEDF KVVAGIDIDK SCKYPFEANN NSVFILKSVS
     DISKKDIAPL FEKAECKILV GCAPCQPFSS YTFKDEEKKD NEKWSLLYDF ARIVRETQPD
     IVSMENVSQL INFKKAPVFE DFLNSLKELG YFVHYEVVNC PDYGIPQKRK RLVLLASRLG
     KIQLIPKTHT KKTYVTVKDA IGQLPAIQDG EAYKNDKLHY ARKLTPLNKE RIEKTPYGGS
     WKDWPNDLKL ECHKKDSGKS YPSVYGRMKW EEPAPTMTTH CIGYGNGRFG HPEQHRAISL
     REASLLQTFP IDYKFFDEKQ QNFSSVAIAR QIGNAVPVKL GEVIAKSIKE HLKNIA
//
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