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Database: UniProt
Entry: L7ZVZ0_9BACI
LinkDB: L7ZVZ0_9BACI
Original site: L7ZVZ0_9BACI 
ID   L7ZVZ0_9BACI            Unreviewed;       515 AA.
AC   L7ZVZ0;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=GHH_c13080 {ECO:0000313|EMBL:AGE21845.1};
OS   Geobacillus sp. GHH01.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1233873 {ECO:0000313|EMBL:AGE21845.1, ECO:0000313|Proteomes:UP000011251};
RN   [1] {ECO:0000313|EMBL:AGE21845.1, ECO:0000313|Proteomes:UP000011251}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GHH01 {ECO:0000313|EMBL:AGE21845.1};
RX   PubMed=23618712;
RA   Wiegand S., Rabausch U., Chow J., Daniel R., Streit W.R., Liesegang H.;
RT   "Complete Genome Sequence of Geobacillus sp. Strain GHH01, a Thermophilic
RT   Lipase-Secreting Bacterium.";
RL   Genome Announc. 1:E0009213-E0009213(2013).
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; CP004008; AGE21845.1; -; Genomic_DNA.
DR   RefSeq; WP_015374511.1; NC_020210.1.
DR   AlphaFoldDB; L7ZVZ0; -.
DR   REBASE; 60338; M.GspGHH01ORF13080P.
DR   KEGG; ggh:GHH_c13080; -.
DR   PATRIC; fig|1233873.3.peg.1383; -.
DR   HOGENOM; CLU_013049_4_1_9; -.
DR   Proteomes; UP000011251; 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   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; 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:AGE21845.1};
KW   Transferase {ECO:0000313|EMBL:AGE21845.1}.
FT   DOMAIN          10..150
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          164..477
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   515 AA;  58684 MW;  61BA735F08B29EE1 CRC64;
     MTVKADIDFQ KDLFEAANKM RGSVAPADYK HYVLPLIFLR YLSNKYEQRR KELEQIVKDP
     SSDWYTEDDE MRQVIITDPD QYKAENVFVV PEEASWSYIM KNAKQPNIKE ILDNAMKRLE
     EENPELEGIL PRIYQGSNLP PENVAGLIEI FSRDVFSANT DDSVDILGRT YEYFISSFAA
     SEGNRGGEFF TPSSIVKLLV AMLEPKSGIV FDPACGSGGM FIQSEEYAPN KHALSFYGQE
     NVVTTVRLGK MNVLLHGINA EIRLGDSLLN DQFPDLKADY VIANPPFNQK DWGADRLSKN
     DPRLIGPVTN SNANYMWMQH FLYHLNDTGT AGFVMANGAM TTNVKEEKEV RQKLVDEGYI
     DCIVQLPEKL FFTTGIPCCL FFLSKNRDGK NGYRARKNEI LFIDARKMGT LVSRKQKALS
     KEEIDKIAAV YHAYKYEEAE QYEDVAGFCK VATIDEVRAN DYKLTPGIYV GTEVSNEDDV
     PFEEKMAELT QRLLEQFEES NRLQEKIKKD LEGLM
//
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