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Database: UniProt
Entry: K2DN95_9BACT
LinkDB: K2DN95_9BACT
Original site: K2DN95_9BACT 
ID   K2DN95_9BACT            Unreviewed;       421 AA.
AC   K2DN95;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   13-SEP-2023, entry version 39.
DE   RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE            EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN   ORFNames=ACD_22C00238G0003 {ECO:0000313|EMBL:EKD99512.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD99512.1};
RN   [1] {ECO:0000313|EMBL:EKD99512.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
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:EKD99512.1}.
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DR   EMBL; AMFJ01008492; EKD99512.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2DN95; -.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00315; Cyt_C5_DNA_methylase; 1.
DR   CDD; cd04761; HTH_MerR-SF; 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; IPR031303; C5_meth_CS.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR000551; MerR-type_HTH_dom.
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; PF00376; MerR; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SMART; SM00422; HTH_MERR; 1.
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; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS50937; HTH_MERR_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   DOMAIN          5..52
FT                   /note="HTH merR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50937"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   421 AA;  47626 MW;  2172571BC7494A01 CRC64;
     MQDKLLTVIE TAERIGVSAD TIRRWEKMGL LKSIRSEHNY RLFNIDEVER IKKRQDGSHS
     PTKFEVLKSP QKTNYTTIEL FTGAGGTALG LENSGLINTL MVEYDKNAVT TLRTNRPDWN
     VIHDDIKNVS FVGKTADIVE GGFPCQAFSY AGKKLGFEDA TRGTLFFEFA RCVKETMPKI
     AVGENVKGLL KHDNGKTLTT MVEALQEIGY KVAYKVVRAQ YLDVPQKRER LLIIGVRNDL
     DLPILFPKEK DYVVALRDAL KDVPASEGQK YPEKKKKVLD MVPAGGYWKD LPLEMQKEYM
     GASFYMGGGK TGMARRLSWE EPSLTLTCAP AQKQTERCHP KETRPLTYRE YARIQAFPDE
     WTFAGSLASQ YKQIGNAVPV NLGYHLGRCL IAMLENKPDF ETMVKVEPIV YQESLVKGLF
     D
//
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