ID A0A0G1L435_9BACT Unreviewed; 364 AA.
AC A0A0G1L435;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 34.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=UW93_C0024G0004 {ECO:0000313|EMBL:KKT90706.1};
OS Parcubacteria group bacterium GW2011_GWC1_45_13.
OC Bacteria.
OX NCBI_TaxID=1618914 {ECO:0000313|EMBL:KKT90706.1, ECO:0000313|Proteomes:UP000034639};
RN [1] {ECO:0000313|EMBL:KKT90706.1, ECO:0000313|Proteomes:UP000034639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKT90706.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCKG01000024; KKT90706.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1L435; -.
DR PATRIC; fig|1618914.3.peg.829; -.
DR Proteomes; UP000034639; 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}; 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 79
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 364 AA; 41579 MW; 997E88F03D055C60 CRC64;
MSLLRLATAF SGIGAIEHAL KRMRVKHELV FACDNDPHVK QSYFANYDMD GSRWFDLVQN
IDGKKFKGKV DLLVGGTPCQ SFSLVGKRRG FKDARGTLFY EFARLVDEIK PKAFIFENVK
GLLSHDSGKT WEVIQNTFKE LGYNYYSQVL NAKEYGIPQN RERLFVVGFR KNKDYKFPNP
VELKIAMQDL LDDSIDSKYY LPEKGIQFVT SQKNLDKKYT QINGRVALCQ KANQQFNWHG
DFVFEPAGKV PEKYFLSDKV AKYVMATGTK NFYSKPETDL AVARPLLATM AKMHRAGVDN
YVTRSGRIRK LSPRECLRLM GFDDTFKIVV SDTQIYRQTG NSIVVNVLMG VLRNMGISAT
KIDL
//
