ID   W0B7G0_9GAMM            Unreviewed;       346 AA.
AC   W0B7G0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   Name=hsdM2 {ECO:0000313|EMBL:AHE65770.1};
GN   ORFNames=Loa_00180 {ECO:0000313|EMBL:AHE65770.1};
OS   Legionella oakridgensis ATCC 33761 = DSM 21215.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=1268635 {ECO:0000313|EMBL:AHE65770.1, ECO:0000313|Proteomes:UP000018838};
RN   [1] {ECO:0000313|EMBL:AHE65770.1, ECO:0000313|Proteomes:UP000018838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OR-10, ATCC 33761 {ECO:0000313|Proteomes:UP000018838};
RX   PubMed=23932911; DOI=10.1016/j.ijmm.2013.07.003;
RA   Brzuszkiewicz E., Schulz T., Rydzewski K., Daniel R., Gillmaier N.,
RA   Dittmann C., Holland G., Schunder E., Lautner M., Eisenreich W., Luck C.,
RA   Heuner K.;
RT   "Legionella oakridgensis ATCC 33761 genome sequence and phenotypic
RT   characterization reveals its replication capacity in amoebae.";
RL   Int. J. Med. Microbiol. 303:514-528(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; CP004006; AHE65770.1; -; Genomic_DNA.
DR   RefSeq; WP_025384749.1; NZ_CP004006.1.
DR   AlphaFoldDB; W0B7G0; -.
DR   STRING; 1268635.Loa_00180; -.
DR   KEGG; lok:Loa_00180; -.
DR   PATRIC; fig|1268635.3.peg.186; -.
DR   eggNOG; COG0286; Bacteria.
DR   HOGENOM; CLU_801202_0_0_6; -.
DR   Proteomes; UP000018838; 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   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
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   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:AHE65770.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018838};
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:AHE65770.1}.
FT   DOMAIN          46..309
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   346 AA;  38995 MW;  FA822FA95487ECC5 CRC64;
     MQFTSADALE KLVSYINNVT DFNKFADELT NAFQKSASKE FELSITDQVI VEIIKGIIGD
     TSQLTIYDGA AGICSLTSQM TSKKLLLEDI NSKFVAIGRC ILFLKDMDAE YTLANSLTSN
     KKSVSADLVV TQAPWGVRFT PNDIEKIKES KYIQLKNKIE IPTSANDSLW IQHSIYHLNK
     NGRAILLMPQ GWLFRGGYDA ELRNYLIGSD LIEAIIGLPS GLLKNTMIPT VLLIINRNKF
     IKNIIHYIDA SKFGRKQKRH LELSKDEINL IAKLASGLLS ESPYYRAVSL CEISENSNDL
     NISRYFSAEV KFKKHDLDHE IELLKIARLK FDSANEHLIG LLTQKI
//