ID A0A0P0E9D1_9MICO Unreviewed; 559 AA.
AC A0A0P0E9D1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-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=AOA12_18175 {ECO:0000313|EMBL:ALJ21713.1};
OS Microbacterium sp. No. 7.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1714373 {ECO:0000313|EMBL:ALJ21713.1, ECO:0000313|Proteomes:UP000059097};
RN [1] {ECO:0000313|EMBL:ALJ21713.1, ECO:0000313|Proteomes:UP000059097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 7 {ECO:0000313|EMBL:ALJ21713.1,
RC ECO:0000313|Proteomes:UP000059097};
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete genome sequence of a polypropylene glycol-degrading strain
RT Microbacterium sp. No. 7.";
RL Submitted (SEP-2015) 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; CP012697; ALJ21713.1; -; Genomic_DNA.
DR RefSeq; WP_054685928.1; NZ_CP012697.1.
DR AlphaFoldDB; A0A0P0E9D1; -.
DR STRING; 1714373.AOA12_18175; -.
DR REBASE; 129743; M.Msp7ORF18175P.
DR KEGG; mio:AOA12_18175; -.
DR PATRIC; fig|1714373.3.peg.3745; -.
DR OrthoDB; 32195at2; -.
DR Proteomes; UP000059097; 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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 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:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ALJ21713.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059097};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ALJ21713.1}.
FT DOMAIN 22..225
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 559 AA; 59769 MW; 067D8ED89FD0F71A CRC64;
MPAEPATAPV APIALVGDTP ALRKSRGAFF TPDPLASFVV DWAIRDAGDT VLEPSCGEAA
FLTRAVERLR MLGRPAPRVD GVEIHAPSAA AARRLVREAG GEPRIAAQDF FLTPPSGSYA
AVVGNPPYIR YQDFSGAARA RSREAALRAG VNLSGLASSW AAFTVHAALM LRRGGRLGLV
VPAELLSVNY AAEVRRFLLS RFARVDLVLF TERVFAEAQE EVILLLADGF DEGGATHMSV
YQAQNAAALG STLDATTWMP NDPADKWTPS LLSAPARAAY ATLAGDGFTV LHEWGETTLG
MVTGNNRYFT MSPREAADRG IPRSELLPLS PPGSAHLRGL ELSRRAWRTL GDGGAATLLF
RPGDRPSAAA WEYIRAGETA RVHQAYKCRV RRTWWQVPLV EPADLLLTYM NADTPRITTN
AAGARHLNSV HGVYLSDAHR DLGRDLLPVA ALTSMTLVGA ETVGRAYGGG MLKIEPREAD
RLPVPSPAVV AAAGATLTAA RPRVAALLRA GRLLDAAALV DGILLVGELG MPRSDVAALR
DQYLHLAARR TARGRRVEV
//
