ID D4L9V0_RUMC1 Unreviewed; 369 AA.
AC D4L9V0;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN OrderedLocusNames=RUM_01270 {ECO:0000313|EMBL:CBL16395.1};
OS Ruminococcus champanellensis (strain DSM 18848 / JCM 17042 / KCTC 15320 /
OS 18P13).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=213810 {ECO:0000313|EMBL:CBL16395.1, ECO:0000313|Proteomes:UP000007054};
RN [1] {ECO:0000313|Proteomes:UP000007054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18848 / JCM 17042 / 18P13
RC {ECO:0000313|Proteomes:UP000007054};
RA Pajon A., Turner K., Parkhill J., Bernalier A.;
RT "The genome sequence of Ruminococcus sp. 18P13.";
RL Submitted (MAR-2010) 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; FP929052; CBL16395.1; -; Genomic_DNA.
DR RefSeq; WP_015557303.1; NZ_BBEP01000013.1.
DR AlphaFoldDB; D4L9V0; -.
DR STRING; 213810.RUM_01270; -.
DR REBASE; 32035; M.Rsp18ORF1270P.
DR GeneID; 83154984; -.
DR KEGG; rch:RUM_01270; -.
DR PATRIC; fig|213810.4.peg.2129; -.
DR HOGENOM; CLU_006958_0_3_9; -.
DR OrthoDB; 9813719at2; -.
DR BioCyc; RCHA213810:RUM_RS00620-MONOMER; -.
DR Proteomes; UP000007054; 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 Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 2.
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; PTHR46098; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR46098:SF1; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR Pfam; PF00145; DNA_methylase; 2.
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:UP000007054};
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 76
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 369 AA; 40915 MW; EF205C225328F6AD CRC64;
MAIPFIDLCS GIGGFHSGLV NTGHYRCVGH AEIDKNAEKA YNAIYGEEGG LNYGDLRTIN
PRELPHFDLL CGGFPCQSFS VAGRRLGFRD TRGTVFFEIA RILAEKRPPF LLLENVLGLL
SHDSGRTLNT IFSALVDMGY NLEWMVLNSK YFGVPQQRRR LYIVGYLDPR CAGKVFPLSG
GNAKNLKQLI PGPQGQRVYE TDGIACTQCA GSGGWGGKTG LYFIDMNADP VITDVARCIT
ARQDSGVSNH RGEHSAVLIE DAPRAILTPD RETVRQQGRR MKEPNEAMFT ITAQDKHGVY
HKGRIRKLMP IECWRLQGFT DEQFYKAQAT GLKDGHLYKM AGNAVSVPVI SAIGQRLYEI
NHEFGIVKE
//
