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Database: UniProt
Entry: A0A0J5GR37_9BACI
LinkDB: A0A0J5GR37_9BACI
Original site: A0A0J5GR37_9BACI 
ID   A0A0J5GR37_9BACI        Unreviewed;       331 AA.
AC   A0A0J5GR37;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=AB685_18750 {ECO:0000313|EMBL:KMJ57039.1};
OS   Bacillus sp. LL01.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1665556 {ECO:0000313|EMBL:KMJ57039.1, ECO:0000313|Proteomes:UP000036436};
RN   [1] {ECO:0000313|EMBL:KMJ57039.1, ECO:0000313|Proteomes:UP000036436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LL01 {ECO:0000313|EMBL:KMJ57039.1,
RC   ECO:0000313|Proteomes:UP000036436};
RA   Vilo C., Galetovic A., Araya J., Gomez Silva B., Dong Q.;
RT   "Draft Genome Sequence of a Bacillus Bacterium from the Atacama Desert
RT   Wetlands Metagenome.";
RL   Submitted (JUN-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:KMJ57039.1}.
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DR   EMBL; LFEL01000007; KMJ57039.1; -; Genomic_DNA.
DR   RefSeq; WP_047972136.1; NZ_LFEL01000007.1.
DR   AlphaFoldDB; A0A0J5GR37; -.
DR   PATRIC; fig|1665556.3.peg.5873; -.
DR   OrthoDB; 9788159at2; -.
DR   Proteomes; UP000036436; 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:0006306; P:DNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.150.470; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR016843; S-AdoMet-dep_Ade-MeTrfase_prd.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR048375; YtxK-like_N.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   Pfam; PF21106; YtxK_like; 1.
DR   PIRSF; PIRSF026567; Adenine_mtase_bact_prd; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          7..86
FT                   /note="YtxK-like N-terminal helical"
FT                   /evidence="ECO:0000259|Pfam:PF21106"
FT   DOMAIN          96..303
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   331 AA;  37216 MW;  C69B3465BBBA5212 CRC64;
     MSITKLENTF TLFDTTAQML QEELDCTYLE ALAETAENLF HGSVIQEEVS EVTKRRLEKE
     YSKLKITSLQ KEEIRKGFQL AILKGMKDAV QANHQMTPDA IAMFMGYLVG KYTSHLQQIT
     LLDPAIGTGN LLTAVLNHQP NKKLEAFGVD VDDLLVKLAY NNANLQEQAI SLFNQDGLSN
     LFIEPVDVVV SDLPVGFYPD DANAANFKLK AAEGHSYAHY LFIEQSLRYT KPGGHLLFLV
     PNSMFEEEES KQVNSLIKEE AYIQGMLQLP ETMFQNKNHA KSILVLQKKG IGVAPPKEAL
     LVNLPSFSNM QAMEKIMGQI NHWFSEQKSK K
//
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