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Database: UniProt
Entry: A0A0R0BR30_9GAMM
LinkDB: A0A0R0BR30_9GAMM
Original site: A0A0R0BR30_9GAMM 
ID   A0A0R0BR30_9GAMM        Unreviewed;       542 AA.
AC   A0A0R0BR30;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   ORFNames=ABB25_04575 {ECO:0000313|EMBL:KRG59789.1};
OS   Stenotrophomonas koreensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=266128 {ECO:0000313|EMBL:KRG59789.1, ECO:0000313|Proteomes:UP000051254};
RN   [1] {ECO:0000313|EMBL:KRG59789.1, ECO:0000313|Proteomes:UP000051254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17805 {ECO:0000313|EMBL:KRG59789.1,
RC   ECO:0000313|Proteomes:UP000051254};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL   Submitted (MAY-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:KRG59789.1}.
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DR   EMBL; LDJH01000006; KRG59789.1; -; Genomic_DNA.
DR   RefSeq; WP_057664285.1; NZ_LDJH01000006.1.
DR   AlphaFoldDB; A0A0R0BR30; -.
DR   STRING; 266128.ABB25_04575; -.
DR   PATRIC; fig|266128.3.peg.2566; -.
DR   OrthoDB; 9784823at2; -.
DR   Proteomes; UP000051254; 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   Gene3D; 1.20.1260.30; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR022749; D12N6_MeTrfase_N.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   PANTHER; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDI METHYLASE SUBUNIT; 1.
DR   PANTHER; PTHR42998; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 1.
DR   Pfam; PF12161; HsdM_N; 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:0000313|EMBL:KRG59789.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051254};
KW   Transferase {ECO:0000313|EMBL:KRG59789.1}.
FT   DOMAIN          18..134
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          156..502
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   REGION          444..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   542 AA;  60076 MW;  D30A02726E452134 CRC64;
     MAKAKKTKGD KNDGLGFEAE LFKAADKLRG NMEPSDYKHV ALGLIFLKYI SDAFEAKHQA
     LLEEDAQAAE DKDEYLAENV FWVPKQARWS HLQASAKQPT IGTLIDDAMR AIEKDNESLK
     GVLPKDYARP ALNKVMLGEL IDLISGIALN EEGDRSKDIL GRVYEYFLGQ FAGAEGKRGG
     EFYTPRSVVR VLVEMLKPVP DPARGITGRV YDPCCGSGGM FVQSEKFVAE HGGRIGDIAI
     YGQESNYTTW RLAKMNLAVR GIDSDIRWNN EGSFHKDELR DLKADFILAN PPFNISDWGG
     ERLREDVRWQ FGVPPVGNAN YAWLQHIYHH LAPNGTAGVV LANGSMSSNQ SGEGEIRRAM
     LEADVVDCMV ALPGQLFYST QIPACLWFLT RNKNAGHGLR DRRGQVLFID ARNMGELVDR
     TRRELTDEDV QKIADTYHAW RRAGGPSVAE GRTPGSDRGE TDAGEYADVP GFCKSASMED
     IRKNGHVLTP GRYVGAADVE DDGEPFTEKM TRLSAQWREH SAEAARLDAA IEANLKELGY
     GE
//
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