ID A0A1B2LVY8_9GAMM Unreviewed; 516 AA.
AC A0A1B2LVY8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=BFG52_01110 {ECO:0000313|EMBL:AOA57084.1};
OS Acinetobacter larvae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1789224 {ECO:0000313|EMBL:AOA57084.1, ECO:0000313|Proteomes:UP000093391};
RN [1] {ECO:0000313|EMBL:AOA57084.1, ECO:0000313|Proteomes:UP000093391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRTC-1 {ECO:0000313|EMBL:AOA57084.1,
RC ECO:0000313|Proteomes:UP000093391};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) 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; CP016895; AOA57084.1; -; Genomic_DNA.
DR RefSeq; WP_067551441.1; NZ_CP016895.1.
DR AlphaFoldDB; A0A1B2LVY8; -.
DR STRING; 1789224.BFG52_01110; -.
DR REBASE; 153666; M.AspBRTC1II.
DR KEGG; ala:BFG52_01110; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000093391; Chromosome.
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:AOA57084.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000093391};
KW Transferase {ECO:0000313|EMBL:AOA57084.1}.
FT DOMAIN 16..145
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 157..478
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 516 AA; 57767 MW; 43FA95CB00A0EF93 CRC64;
MARAPKKETK QESLEVVLWK AADKLRKNID AAEYKHVVLG LIFLKYISDS FDVHYQQLVK
GEGEFVGADP EDRDEYIAYN VFFVPEQARW NYLLSQAKQT TIGQLVDAAM EAIEGENPQL
KGVLPKVYAR QNLDATILGE LIDMIGNIAL GDAKERSADV LGHVFEYFLG EFALAEGKQG
GQFYTPKSIV SLLVNMLEPY KGRVFDPCCG SGGMFVQSEQ FVEAHQGRID DISIYGQESN
QTTWRLAKMN LAIRGINAEH VKWNSEGSFL NDAHKDLKAD YIIANPPFNV SDWSGEQLAG
DARWQYGTPP TGNANFAWMQ HFLFHLSPKG QAGVVLAKGA LTSKTSGEGE IRKALVAEAN
VIDCIVNLPA KLFLNTQIPA ALWFMRRDRA NSSSYRDRSG EILFIDARNL GHLINRRSKV
LSEEDIQLIT DTYHNWRNPE GAYEDVAGFC ASVSRDKVAE LDYVLTPGRY VGLADDEDEF
DFKERFTALK AEFEAQLVEE AQLNQAIVEN LAKVMV
//
