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Database: UniProt
Entry: A0A398AZW4_9BACI
LinkDB: A0A398AZW4_9BACI
Original site: A0A398AZW4_9BACI 
ID   A0A398AZW4_9BACI        Unreviewed;       329 AA.
AC   A0A398AZW4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
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=D1970_16585 {ECO:0000313|EMBL:RID83137.1};
OS   Mesobacillus zeae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX   NCBI_TaxID=1917180 {ECO:0000313|EMBL:RID83137.1, ECO:0000313|Proteomes:UP000265816};
RN   [1] {ECO:0000313|EMBL:RID83137.1, ECO:0000313|Proteomes:UP000265816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JJ-247 {ECO:0000313|EMBL:RID83137.1,
RC   ECO:0000313|Proteomes:UP000265816};
RA   Seuylemezian A., Vaishampayan P.;
RT   "Bacillus jemisoniae sp. nov., Bacillus chryseoplanitiae sp. nov., Bacillus
RT   resnikiae sp. nov., and Bacillus frankliniae sp. nov., isolated from Viking
RT   spacecraft and associated surfaces.";
RL   Submitted (AUG-2018) 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:RID83137.1}.
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DR   EMBL; QWVT01000029; RID83137.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A398AZW4; -.
DR   OrthoDB; 9788159at2; -.
DR   Proteomes; UP000265816; 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   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:RID83137.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265816};
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:RID83137.1}.
FT   DOMAIN          7..86
FT                   /note="YtxK-like N-terminal helical"
FT                   /evidence="ECO:0000259|Pfam:PF21106"
FT   DOMAIN          97..290
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   329 AA;  36576 MW;  01BC05B3E01CB97D CRC64;
     MSVSQVEKLF TAFNVTADIL KEELDCTYLE ALAETGENLF HGSVLQEGLN EFAIKRLEKS
     YQEIHLEDFA KEEIRRGFQL AILKGMQENI QPNHQMTPDS IGMFIGYLLD KFITAEEYSL
     LDPAAGTGNL LATVMNQQQG RKIAAAGSEI DEVLIRLAYI NANLLGHDVE LFNQDSLEPL
     FIDPVDAVIC DLPVGFYPAD NKAADFEVSV DSGHTYSHHL FIEQSTRHAK EGACLLFVIP
     NGLFESEQAN KLHDYIKNNL IIQGVIQLPD SMFKHKHAGK SILILQKKGE GVKAPKQALL
     AELPPMSDSR AMGSMLARID GWFAENKKA
//
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