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Database: UniProt
Entry: A0A1Y1RD91_9BACT
LinkDB: A0A1Y1RD91_9BACT
Original site: A0A1Y1RD91_9BACT 
ID   A0A1Y1RD91_9BACT        Unreviewed;       345 AA.
AC   A0A1Y1RD91;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE            EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN   ORFNames=B6244_14885 {ECO:0000313|EMBL:OQY25577.1};
OS   Candidatus Cloacimonetes bacterium 4572_55.
OC   Bacteria; Candidatus Cloacimonadota.
OX   NCBI_TaxID=1971726 {ECO:0000313|EMBL:OQY25577.1, ECO:0000313|Proteomes:UP000192623};
RN   [1] {ECO:0000313|Proteomes:UP000192623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Seitz K., Teske A., Baker B.;
RT   "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT   hydrothermal sediment communities.";
RL   Submitted (MAR-2017) 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:OQY25577.1}.
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DR   EMBL; NBMB01000107; OQY25577.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1RD91; -.
DR   STRING; 1971726.B6244_14885; -.
DR   Proteomes; UP000192623; 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; 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        78
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   345 AA;  39271 MW;  4DADA4F13626B497 CRC64;
     MSIKYIDLFC GIGGFRLGAT QVFEKYNIPS KCVFSSDIDL YAREAYHANF GEYPAGDITK
     IDADEIPDHD LLFAGFPCQP FSIIGNGKGF EDTRGTLFFD IARILDAKKP KAFVLENVKR
     LVGHNKGRTL RKISDVLTEL GYYFDYRVLN ALDYGLPQKR ERVFIVGFHK PIQFQWPAQL
     STYTSLNDIL EDNVADKHYA SERIKQKRLE SHTPMHTPSV WHENKAGNIS SYPYSCALRA
     GASYNYLLVN GERRLTPREM LRLQGFPDSY KIVVSDAQTR KQAGNAVPVN LVRAVVESFV
     PILTDASIKK TTRNSNGYHR HQQTIFLKEH RYALQKENAA FANSR
//
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