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Database: UniProt
Entry: A0A0M4MCZ8_9ACTN
LinkDB: A0A0M4MCZ8_9ACTN
Original site: A0A0M4MCZ8_9ACTN 
ID   A0A0M4MCZ8_9ACTN        Unreviewed;        93 AA.
AC   A0A0M4MCZ8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=AL705_07585 {ECO:0000313|EMBL:ALE19412.1};
OS   Lawsonella clevelandensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Lawsonellaceae;
OC   Lawsonella.
OX   NCBI_TaxID=1528099 {ECO:0000313|EMBL:ALE19412.1, ECO:0000313|Proteomes:UP000068137};
RN   [1] {ECO:0000313|EMBL:ALE19412.1, ECO:0000313|Proteomes:UP000068137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X1698 {ECO:0000313|EMBL:ALE19412.1,
RC   ECO:0000313|Proteomes:UP000068137};
RX   PubMed=26659691;
RA   Nicholson A.C., Bell M., Humrighouse B.W., McQuiston J.R.;
RT   "Complete Genome Sequences for Two Strains of a Novel Fastidious, Partially
RT   Acid-Fast, Gram-Positive Corynebacterineae Bacterium, Derived from Human
RT   Clinical Samples.";
RL   Genome Announc. 3:e01462-15(2015).
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; CP012390; ALE19412.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M4MCZ8; -.
DR   STRING; 1528099.AL705_07585; -.
DR   KEGG; cbq:AL705_07585; -.
DR   PATRIC; fig|1562462.4.peg.1547; -.
DR   OrthoDB; 9784823at2; -.
DR   Proteomes; UP000068137; 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   Reference proteome {ECO:0000313|Proteomes:UP000068137};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..74
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   93 AA;  10401 MW;  2F278D37ADDD084B CRC64;
     MLIESVAAVE ADGGDSRTLS LYGQEKNLTT QSIARMNMYI HNLPDHNIMR GDTLREPKFT
     DGDALKQFDV VIAKRWLGQM IRDNGVCEYA LAA
//
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