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Database: UniProt
Entry: A0A0U4FGL4_9BACI
LinkDB: A0A0U4FGL4_9BACI
Original site: A0A0U4FGL4_9BACI 
ID   A0A0U4FGL4_9BACI        Unreviewed;       515 AA.
AC   A0A0U4FGL4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-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=AOX59_03720 {ECO:0000313|EMBL:ALX47790.1};
OS   Lentibacillus amyloliquefaciens.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX   NCBI_TaxID=1472767 {ECO:0000313|EMBL:ALX47790.1, ECO:0000313|Proteomes:UP000050331};
RN   [1] {ECO:0000313|EMBL:ALX47790.1, ECO:0000313|Proteomes:UP000050331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LAM0015 {ECO:0000313|EMBL:ALX47790.1,
RC   ECO:0000313|Proteomes:UP000050331};
RA   Wang J.-L., He M.-X.;
RT   "Complete genome sequence of strain Lentibacillus amyloliquefaciens
RT   LAM0015T isolated from saline sediment.";
RL   Submitted (JAN-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; CP013862; ALX47790.1; -; Genomic_DNA.
DR   RefSeq; WP_068442020.1; NZ_CP013862.1.
DR   AlphaFoldDB; A0A0U4FGL4; -.
DR   STRING; 1472767.AOX59_03720; -.
DR   REBASE; 137069; M.Lam15ORF3720P.
DR   KEGG; lao:AOX59_03720; -.
DR   OrthoDB; 9814572at2; -.
DR   Proteomes; UP000050331; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
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; IPR004546; Restrct_endonuc_T1M.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   NCBIfam; TIGR00497; hsdM; 1.
DR   PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Endonuclease {ECO:0000313|EMBL:ALX47790.1};
KW   Hydrolase {ECO:0000313|EMBL:ALX47790.1};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nuclease {ECO:0000313|EMBL:ALX47790.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050331};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          14..163
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          178..480
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   COILED          484..511
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   515 AA;  59145 MW;  B7D1FC5DC3283B43 CRC64;
     MTTTEKQRQQ QADLQKKLWD IANDLRGNMD ASEFRNYILG LIFYRFLSEN TEQQVEQLLA
     EDNITYEEAW QNDEYQDVLK QELIARIGYV IEPQDLFSHL VKKIENQTFE IEDLHRAINH
     IEASTRGEDS EDEFERLFED MDLNSSRLGN TNAERTKLIS KVMMNLAALP FVQGDMEIDM
     LGDAYEYLIG QFAATAGKKA GEFYTPQQVS KILAKIVTTG KKDLKNVYDP TCGSGSLLLR
     VGREANVRHY YGQEYNNTTF NLARMNMLLH DVNYHNFSLA NGDTLEHPAV VDGQFEAVVA
     NPPYSAKWSA DPSFLDDERF SNYGKLAPKS KADFAFVQHM IYHLDDNGKM AVVLPHGVLF
     RGAAEETIRK YLIEEKNYLD AVIGLPSNLF FGTGIPTCIL VFKKCREQDE DVLFIDASQS
     FEKGRNQNHL ADEDVNKIVE TFRNRETLDK FSYVSTLDEI RKNDYNLNIP RYVDTFEEEE
     PVDLDKVQQD IQDIDQKIVG LEEEINGYLK ELGVL
//
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