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Database: UniProt
Entry: L0J6M5_9MYCO
LinkDB: L0J6M5_9MYCO
Original site: L0J6M5_9MYCO 
ID   L0J6M5_9MYCO            Unreviewed;       811 AA.
AC   L0J6M5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
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=Mycsm_06103 {ECO:0000313|EMBL:AGB26262.1};
OS   Mycobacterium sp. JS623.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB26262.1, ECO:0000313|Proteomes:UP000010844};
RN   [1] {ECO:0000313|Proteomes:UP000010844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA   Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL   Submitted (OCT-2011) 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; CP003078; AGB26262.1; -; Genomic_DNA.
DR   RefSeq; WP_015309836.1; NC_019966.1.
DR   AlphaFoldDB; L0J6M5; -.
DR   STRING; 212767.Mycsm_06103; -.
DR   REBASE; 58775; M.Msm623ORF6103P.
DR   KEGG; msa:Mycsm_06103; -.
DR   PATRIC; fig|710686.3.peg.6148; -.
DR   HOGENOM; CLU_013049_6_0_11; -.
DR   OrthoDB; 9784823at2; -.
DR   Proteomes; UP000010844; 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   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1260.30; -; 2.
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; PTHR42933; SLR6095 PROTEIN; 1.
DR   PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 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:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:AGB26262.1};
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:AGB26262.1}.
FT   DOMAIN          10..122
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          135..442
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   811 AA;  89648 MW;  679BFEBCA926839A CRC64;
     MALKKSDLYS SLWKSCDELR GGMDASQYKD YILTLLFVKY VSDKAKADPT SLIEVPTGGS
     FDDLVKLKGK PNIGEEINVA IRKLADANDL QGVINNADFD DPNKLGDGKA MQDRLSKLIG
     IFQALDFSGS RAEGDDLLGD AYEYLMRHFA TESGKSKGQF YTPAEVSRVM AQVIGIKPNT
     PKRTTVYDPT CGSGSLLLKV VDAAPNGLTI YGQEKDNATW ALSKMNMILH GNVTADIRMG
     DSIVDPKFRS GDTLDSFDLL VANPPFSVKS WTNGLENEYG RFDGYARPPE KNGDYAFLLH
     MVKSLKSTGK GAVILPHGVL FRGHTEATIR KELIKRGYIK GIIGLPANLF YGTGIPACII
     VLDKENAQAR TGIFMIDASK GFMKDGNKNR LRPRDMHQIV DSFTKQIEVE RYSRMVPLKE
     IADPNNDYNL NIPRYIDSSE PEDIQDLHAH LHGGIPDRDL DALDDYWKAF STLRSTLFTE
     NRPGYSDLTI DVASVQETVL DSAKFKKFAA RVDADVDEWL GSHRARLAKI TENTKPGELI
     SEISEDLLAR FKSVPLLDEY DVYEQLMTYW NETMHDDVFL IMNEGWVGAA KPRKTIEDKD
     RKLTEVPDLI AGSGRGATKY KMDLIPPAVM VAANFADYQP YIDELTAAAE EAARAVEEYT
     EEHAVEDGLL AAAMDDDKIS KALAAARLKD AKKEGSDPDE IKALQHLIDL YDAETDAKKA
     VKEAQAELDA AVLKEYGHLT EDAVKSLVLD DKWCAAVRGR IGGEVNSLTL DLVARIQELG
     ERYSETVGAL DAELERLEAT IAGHLADMGV N
//
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