ID A0A1M5YLR8_9CLOT Unreviewed; 338 AA.
AC A0A1M5YLR8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=SAMN02745196_03073 {ECO:0000313|EMBL:SHI12910.1};
OS Clostridium collagenovorans DSM 3089.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121306 {ECO:0000313|EMBL:SHI12910.1, ECO:0000313|Proteomes:UP000184526};
RN [1] {ECO:0000313|EMBL:SHI12910.1, ECO:0000313|Proteomes:UP000184526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3089 {ECO:0000313|EMBL:SHI12910.1,
RC ECO:0000313|Proteomes:UP000184526};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQXP01000019; SHI12910.1; -; Genomic_DNA.
DR RefSeq; WP_072832851.1; NZ_FQXP01000019.1.
DR AlphaFoldDB; A0A1M5YLR8; -.
DR STRING; 1121306.SAMN02745196_03073; -.
DR OrthoDB; 9813719at2; -.
DR Proteomes; UP000184526; 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; 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; 1.
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:UP000184526};
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 80
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 338 AA; 39009 MW; 7BE4DE8C17A8B306 CRC64;
MERIKYKNRH LKTVSLFAGA GGLDLGFLNA GFDIIWANDV DKYAYESYRH NISDHIVLGD
INQLLDDIPS HEVLIGGFPC QPFSMMGQQL GFEDERGTLF FTIEQIVRKH RPKVIVLENV
KNLETHNGGE TFARMQRILR DELLDDNGLG YSVFYQVLNS ADFGIPQTRR RVFVVAFDRG
YFNNINFEFP QPIELQQDLR DILDGNVDKK YFLSEKILPT ILSHGTGNYY SKSEIDLRIA
RPLCATMHKM HRASQDNYVT DIENRRRFED TEEKRISNVR RLTPNECKKL QGFPSEWEIN
VSDTQAYRQF GNAVTVDVAY NVAMQIVRAL NITLEIEG
//
