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Database: UniProt
Entry: A0A0G0LX43_9BACT
LinkDB: A0A0G0LX43_9BACT
Original site: A0A0G0LX43_9BACT 
ID   A0A0G0LX43_9BACT        Unreviewed;       422 AA.
AC   A0A0G0LX43;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Methyltransferase {ECO:0000256|RuleBase:RU362026};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU362026};
GN   ORFNames=UT22_C0047G0002 {ECO:0000313|EMBL:KKQ95597.1};
OS   Parcubacteria group bacterium GW2011_GWC2_39_11.
OC   Bacteria.
OX   NCBI_TaxID=1618921 {ECO:0000313|EMBL:KKQ95597.1, ECO:0000313|Proteomes:UP000034836};
RN   [1] {ECO:0000313|EMBL:KKQ95597.1, ECO:0000313|Proteomes:UP000034836}
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 = an N(4)-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC         Evidence={ECO:0000256|ARBA:ARBA00001893};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC       subfamily. {ECO:0000256|ARBA:ARBA00010203}.
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:KKQ95597.1}.
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DR   EMBL; LBVZ01000047; KKQ95597.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0LX43; -.
DR   PATRIC; fig|1618921.3.peg.773; -.
DR   Proteomes; UP000034836; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR   InterPro; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR017985; MeTrfase_CN4_CS.
DR   InterPro; IPR001091; RM_Methyltransferase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01555; N6_N4_Mtase; 2.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 3.
DR   PROSITE; PS00093; N4_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:KKQ95597.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          12..94
FT                   /note="DNA methylase N-4/N-6"
FT                   /evidence="ECO:0000259|Pfam:PF01555"
FT   DOMAIN          246..419
FT                   /note="DNA methylase N-4/N-6"
FT                   /evidence="ECO:0000259|Pfam:PF01555"
SQ   SEQUENCE   422 AA;  48680 MW;  4F231E9616EA221B CRC64;
     MSQVATLFSK TKIDYSWSFS DKTRKDTAYI THGYHRYPAK FIPQIVSRLA EKYTKEGDLI
     VDPFGGCGTT LVESKVMGRP SVGVDINPVA VLITKAKITP LDSPKIEKAF TVLKAKLDTY
     TRDTKVKAPE HERIDYWFKP EEKRKLAFIF AEISKLKNQD IRDFFFCGFS NILKNCSIWL
     QKSNKPTRDF NKKPSDPIPT FYKQIKMMMR GNARFYELSK EKNHLKIPSQ VYCTDARTIP
     VKDNSVSLIV TSPPYVTSYE YADLHQLTAL WLEYTKDLSD FRKRFIGTSY HNKKDLVLNS
     KLAEEIRNEL LKKDKKTAEE VSTYFSEMNQ VFVEMKRMLK KGGKTCIVIG NTSLKGIEIL
     NAEVFAEQLK NLELKIADII KREIPSKNLP SIRDEKTGKF ARISDKNKVS AYPTEYILIM
     EK
//
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