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Database: UniProt
Entry: A0A0C1CU75_9FLAO
LinkDB: A0A0C1CU75_9FLAO
Original site: A0A0C1CU75_9FLAO 
ID   A0A0C1CU75_9FLAO        Unreviewed;       422 AA.
AC   A0A0C1CU75;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, 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=OA85_13805 {ECO:0000313|EMBL:KIA84780.1};
OS   Flavobacterium sp. AED.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1423323 {ECO:0000313|EMBL:KIA84780.1, ECO:0000313|Proteomes:UP000031403};
RN   [1] {ECO:0000313|EMBL:KIA84780.1, ECO:0000313|Proteomes:UP000031403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AED {ECO:0000313|EMBL:KIA84780.1,
RC   ECO:0000313|Proteomes:UP000031403};
RA   Gale A.N., Newman J.D.;
RT   "Flavobacterium sp. AED Genome.";
RL   Submitted (OCT-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:KIA84780.1}.
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DR   EMBL; JSYM01000004; KIA84780.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1CU75; -.
DR   STRING; 1423323.OA85_13805; -.
DR   OrthoDB; 32195at2; -.
DR   Proteomes; UP000031403; 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; 3.90.120.30; -; 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        167
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   422 AA;  48485 MW;  9F844EC37E3491CB CRC64;
     MIMKENISIE EFDNKKFKMR FVEQEDNKKA VLTHYLHNYD NGVKKHFEKE AKEYLKEIIE
     YKNDEEKLNL VSDVALQQLL FEVREVPFPT PENYTFKFID LFAGIGGFRM AMQNLGGKCV
     FTSEWDENAK KTYRANYGET PFGDITKERT KNYIPDDFDV LCAGFPCQAF SIAGKRGGFE
     DTRGTLFFDV AEIIKNRKPK AIFLENVKGL RNHNGGKTLA TILNVLRNDL GYFVPEPQIV
     NAKNFGVPQN RERIYIVGFR NDLNIDSFSY PEPLEEKVFF RKVKEENVVP TKYYLSTQYL
     RTLISHKERH ASKGNGFGYE IIKDDEVSNA IVVGGMGRER NLVIDNRITD YTPTTHIKGE
     VNREGIRKMT PREWARLQGF PDNFLIPVAD ASAYKQFGNS VAVPAIQATA EKIIDLIKAK
     LC
//
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