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Database: UniProt
Entry: A0A136NGL0_9BACT
LinkDB: A0A136NGL0_9BACT
Original site: A0A136NGL0_9BACT 
ID   A0A136NGL0_9BACT        Unreviewed;       542 AA.
AC   A0A136NGL0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   Name=hsdM {ECO:0000313|EMBL:KXK45186.1};
GN   ORFNames=UZ10_BCD003002183 {ECO:0000313|EMBL:KXK45186.1};
OS   Bacteroidetes bacterium OLB10.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1617421 {ECO:0000313|EMBL:KXK45186.1, ECO:0000313|Proteomes:UP000070480};
RN   [1] {ECO:0000313|EMBL:KXK45186.1, ECO:0000313|Proteomes:UP000070480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB10 {ECO:0000313|EMBL:KXK45186.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC         COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC         Evidence={ECO:0000256|ARBA:ARBA00001279};
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:KXK45186.1}.
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DR   EMBL; LNBX01000044; KXK45186.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136NGL0; -.
DR   STRING; 1617421.UZ10_BCD003002183; -.
DR   PATRIC; fig|1617421.3.peg.2285; -.
DR   Proteomes; UP000070480; 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:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:KXK45186.1};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KXK45186.1}.
FT   DOMAIN          179..495
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   542 AA;  61956 MW;  DFA272AE3EEE5A3C CRC64;
     MVTQDFTAKT KELIDNLKGV CTSYGLGNDG NEFKIITQVF LYKFMNDKFG YEVKQLEPKL
     AKAESWEKEI AQYSDKQYEM LLLRMNPESA KLKREHYLSN LFNRQDKEEF AKFFDDTLRD
     IAIFNNEIFS VKTGTGAKIT LFDELSNYIT DSSQRDNFCK AIINQLVNFS FEKIFNQKFD
     FFSTIFEYLI KDYNKDGGGK YAEYYTPHAV SKIMASILVD KPVSNVTCYD PSAGSGTLLM
     NLAHAIGEDR CTIYSQDISQ KSSSMLRLNL ILNNLVHSIQ NIIQGNTMLN PYHKVGDKLM
     TFDYIVSNPP FKLDFSDFRN DLDSKQNKER FFAGIPKIKA KDKDKMEIYL LFIQHIMFSL
     SAKGKAAIVV PTGFITAPNG IEKKIREKLV ESKMLRGVIS MPSNIFATTG TNVSVLFIDK
     ANTKGDIVLM DASKLGEEVK DGKNKKTLLS PIEEQLIINT FNNHEAVEDF TVVVSYEQIK
     EKNFSFSAGQ YFEVKINYSE ITPKEFNEKV DSFKASFTKL FADSKLLEVE IKKQLEGLHY
     DL
//
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