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Database: UniProt
Entry: F0RE64_CELLC
LinkDB: F0RE64_CELLC
Original site: F0RE64_CELLC 
ID   F0RE64_CELLC            Unreviewed;       414 AA.
AC   F0RE64;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE            EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN   OrderedLocusNames=Celly_0997 {ECO:0000313|EMBL:ADY28826.1};
OS   Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 /
OS   NCIMB 1423 / VKM B-1433 / Cy l20).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Cellulophaga.
OX   NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY28826.1, ECO:0000313|Proteomes:UP000007487};
RN   [1] {ECO:0000313|EMBL:ADY28826.1, ECO:0000313|Proteomes:UP000007487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 /
RC   VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487};
RX   PubMed=21677859; DOI=10.4056/sigs.1774329;
RA   Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Mavromatis K., Ovchinikova G., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA   Brambilla E.M., Kannan K.P., Rohde M., Spring S., Goker M., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Ivanova N.;
RT   "Complete genome sequence of Cellulophaga lytica type strain (LIM- 21).";
RL   Stand. Genomic Sci. 4:221-232(2011).
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; CP002534; ADY28826.1; -; Genomic_DNA.
DR   RefSeq; WP_013620574.1; NC_015167.1.
DR   AlphaFoldDB; F0RE64; -.
DR   STRING; 867900.Celly_0997; -.
DR   REBASE; 33118; M.Cly7489ORF997P.
DR   KEGG; cly:Celly_0997; -.
DR   eggNOG; COG0270; Bacteria.
DR   eggNOG; COG0789; Bacteria.
DR   HOGENOM; CLU_006958_2_0_10; -.
DR   OrthoDB; 32195at2; -.
DR   Proteomes; UP000007487; Chromosome.
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   CDD; cd04762; HTH_MerR-trunc; 1.
DR   Gene3D; 1.10.1660.10; -; 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; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR041657; HTH_17.
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   Pfam; PF12728; HTH_17; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF46955; Putative DNA-binding domain; 1.
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:UP000007487};
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   DOMAIN          6..56
FT                   /note="Helix-turn-helix"
FT                   /evidence="ECO:0000259|Pfam:PF12728"
FT   ACT_SITE        147
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   414 AA;  47253 MW;  FE27E894AB5DC8C7 CRC64;
     MVTKDYYSLN EVSEILGKSK ETLRRWDRDG KFSAVREPIS QYRIYKKEQV NSLLEQLSID
     YEDTIDNSVT PIKEFKVLEL FAGAGGLAVG LEKAGIKCVA LNEIDKWACQ TLRENRPHWN
     VLEGDIKSFN FSEYNNQVDI VTGGFPCQAF SYAGKKLGLQ DARGTLFYEF ARAVKEVNPL
     ICIGENVKGL LSHEKGKTIE GMISILDEIG YNVVPVKVLK AINYKVPQKR ERVILVGVRK
     DIDIKYEYPK PHNKIYNLID ALKKGELYNC NVPKSEGSKY PEHKKAVLDL IPQKGYWRNL
     PLDIQKEYMG KSFYLGGGKT GIARRIGWDE PSLTLTCSPA QKQTERCHPE ETRPFTVREY
     ARIQTFPDEW KFMGSVSQQY KQIGNAVPCN LGQEIGYSVI KFLNEYYLSL SKPK
//
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