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Database: UniProt
Entry: F7R0F2_9LACO
LinkDB: F7R0F2_9LACO
Original site: F7R0F2_9LACO 
ID   F7R0F2_9LACO            Unreviewed;       335 AA.
AC   F7R0F2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=LRU_01281 {ECO:0000313|EMBL:EGM51767.1};
OS   Ligilactobacillus ruminis SPM0211.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1040964 {ECO:0000313|EMBL:EGM51767.1, ECO:0000313|Proteomes:UP000002971};
RN   [1] {ECO:0000313|EMBL:EGM51767.1, ECO:0000313|Proteomes:UP000002971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPM0211 {ECO:0000313|EMBL:EGM51767.1,
RC   ECO:0000313|Proteomes:UP000002971};
RX   PubMed=21742873; DOI=10.1128/JB.05601-11;
RA   Lee S., Cho Y.J., Lee A.H., Chun J., Ha N.J., Ko G.;
RT   "Genome Sequence of Lactobacillus ruminis SPM0211, Isolated from a Fecal
RT   Sample from a Healthy Korean.";
RL   J. Bacteriol. 193:5034-5034(2011).
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGM51767.1}.
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DR   EMBL; AFOJ01000005; EGM51767.1; -; Genomic_DNA.
DR   RefSeq; WP_003695480.1; NZ_AFOJ01000005.1.
DR   AlphaFoldDB; F7R0F2; -.
DR   Proteomes; UP000002971; Unassembled WGS sequence.
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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.150.470; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR016843; S-AdoMet-dep_Ade-MeTrfase_prd.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR048375; YtxK-like_N.
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   Pfam; PF21106; YtxK_like; 1.
DR   PIRSF; PIRSF026567; Adenine_mtase_bact_prd; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EGM51767.1};
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:EGM51767.1}.
FT   DOMAIN          8..86
FT                   /note="YtxK-like N-terminal helical"
FT                   /evidence="ECO:0000259|Pfam:PF21106"
FT   DOMAIN          98..307
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   335 AA;  37697 MW;  2F5F40277E112055 CRC64;
     MALADIEKKY DLMNEACELL QEKLQDDCLD ALIENFDNLL NDGKVHVEDG IPDEKTASKL
     AEIYRAVRLD EISTEDRRLL LQLSLLTVYR KEKIQANHQM TPDSIGFLTA YLLQQVYEKK
     DETNFLDLCV GTGNLAAVVI NALKNNGFKN IHGFGIDNDD TLLTIASIES QLCDLDLNLY
     HQDALDKSLI PQADVIVSDL PVGWYPLDER AEGYETHAKE GHSFVHFLLI EQALDNLKEG
     GIGMFLIPSS MFESEESLPL LKFIQKNGYL QSLINLPGAM FASKKSEKAI LILQKKGAKS
     KQANPVLLGE FPLVKDTKNF EKFMAEVAVW KEKNF
//
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