ID A0A385NTG8_9BACI Unreviewed; 327 AA.
AC A0A385NTG8;
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=DOE78_18600 {ECO:0000313|EMBL:AYA77294.1};
OS Bacillus sp. Y1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=352858 {ECO:0000313|EMBL:AYA77294.1, ECO:0000313|Proteomes:UP000265711};
RN [1] {ECO:0000313|EMBL:AYA77294.1, ECO:0000313|Proteomes:UP000265711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y1 {ECO:0000313|EMBL:AYA77294.1};
RA Rathod J., Jean J.-S.;
RT "Arsenic resistant and redox active subsurface bacterial isolate Bacillus
RT sp. Y1 from Yichu borehole sediment.";
RL Submitted (JUN-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};
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DR EMBL; CP030028; AYA77294.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A385NTG8; -.
DR KEGG; bacq:DOE78_18600; -.
DR OrthoDB; 9788159at2; -.
DR Proteomes; UP000265711; Chromosome.
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 ECO:0000313|EMBL:AYA77294.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000265711};
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:AYA77294.1}.
FT DOMAIN 7..86
FT /note="YtxK-like N-terminal helical"
FT /evidence="ECO:0000259|Pfam:PF21106"
FT DOMAIN 97..320
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 327 AA; 36964 MW; E041E8FBC99263F9 CRC64;
MSPSTLEDLF TLFNETASIL QEELNCTYLE ALAETGENLF QQSVLQEELS ELTLKRLKKS
YEAFRPDKYS AEELRKAYQL AILKGMKESV QPNHQMTPDA VGMLVGYLVD KFVQSTNFRL
LDPAVGTGNL LTTVMNHQVN KKVTAIGVDI DDLLIHLSFV NANLQEHQIE LFNQDSLEPL
FIDPVDAVVA DLPVGYYPND VRAQDYQLKS SEGHSYAHHL FIEQSVKHTK AGGYLFFIIP
NGLFESEEAP KLHAFLKEQA HIQGILQLPM TMFKNKQAAK SILILQKLGG EIKPPKQVLL
VNIPTLSKGQ DVERMLRNID IWIKENK
//
