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Database: UniProt
Entry: O52273_LACLL
LinkDB: O52273_LACLL
Original site: O52273_LACLL 
ID   O52273_LACLL            Unreviewed;       531 AA.
AC   O52273;
DT   01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 89.
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=HsdM {ECO:0000313|EMBL:AAB91416.1};
OS   Lactococcus lactis subsp. lactis bv. diacetylactis.
OG   Plasmid pND861 {ECO:0000313|EMBL:AAB91416.1}.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=44688 {ECO:0000313|EMBL:AAB91416.1};
RN   [1] {ECO:0000313|EMBL:AAB91416.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UK19161 {ECO:0000313|EMBL:AAB91416.1};
RC   PLASMID=pND861 {ECO:0000313|EMBL:AAB91416.1};
RX   PubMed=11092734;
RA   Deng Y.M., Liu C.Q., Dunn N.W.;
RT   "LldI, a plasmid-encoded type I restriction and modification system in
RT   Lactococcus lactis.";
RL   DNA Seq. 11:239-245(2000).
RN   [2] {ECO:0000313|EMBL:AAB91416.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UK19161 {ECO:0000313|EMBL:AAB91416.1};
RC   PLASMID=pND861 {ECO:0000313|EMBL:AAB91416.1};
RA   Deng Y.-M., Dunn N.W.;
RL   Submitted (JUL-2000) 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; AF034786; AAB91416.1; -; Genomic_DNA.
DR   PIR; T09460; T09460.
DR   AlphaFoldDB; O52273; -.
DR   REBASE; 3606; M.LldI.
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; -; 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; IPR004546; Restrct_endonuc_T1M.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   NCBIfam; TIGR00497; hsdM; 1.
DR   PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 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   Plasmid {ECO:0000313|EMBL:AAB91416.1};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..157
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          169..476
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   531 AA;  60725 MW;  773B79ACFAE84429 CRC64;
     MATGLNQQLW ASADILRGKM DASEYKNYLL GLIFYKYLSD AQLREVYEQE NGKTDTFPER
     STQYAGFMEW YEEDKDDLIE NIQPKQGYFI QPDQLFYHYR IKADNYEFNL TDLQAGFNEL
     ERQGEEFSGL FADIDLNSTK LGSNAQQRNV TITEVLRALD EIDLFEHNGD VIGDAYEYLI
     GMFAEGAGKK AGEFYTPQAV SRIMSEITSI GQESRAPFHI YDPAMGSGSL MLNIRRYLLN
     PNQVHYHGQE LNTTTFNLAR MNLILHGVDK ERMNLNNGDT LDADWPSEEP YQFDSVVMNP
     PYSAKWSAAD KFLSDPRFER FGKLAPKSKA DFAFLLHGFY HLKESGTMGI VLPHGVLFRG
     AAEGTIRQAL LEMGAIDAVI GLPANIFFGT SIPTTVIILK KNRSRRDVLF IDASQDFEKQ
     KNQNVLLDEH IDKIVSTYKK REDIERYAHV ASFDEIQEND FNLNIPRYVD TFEEEEPVDL
     VAVNTNLLKI NEELVQQDQT LLSLINDFSE SEENQAMIES MRLLLRGGHD E
//
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