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Database: UniProt
Entry: E3C8K3_9LACO
LinkDB: E3C8K3_9LACO
Original site: E3C8K3_9LACO 
ID   E3C8K3_9LACO            Unreviewed;       484 AA.
AC   E3C8K3;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=HMPREF9265_0777 {ECO:0000313|EMBL:EFQ52970.1};
OS   Limosilactobacillus oris PB013-T2-3.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=908339 {ECO:0000313|EMBL:EFQ52970.1, ECO:0000313|Proteomes:UP000003070};
RN   [1] {ECO:0000313|EMBL:EFQ52970.1, ECO:0000313|Proteomes:UP000003070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB013-T2-3 {ECO:0000313|EMBL:EFQ52970.1,
RC   ECO:0000313|Proteomes:UP000003070};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (OCT-2010) 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};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594}.
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:EFQ52970.1}.
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DR   EMBL; AEKL01000057; EFQ52970.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3C8K3; -.
DR   eggNOG; COG0286; Bacteria.
DR   OrthoDB; 9814572at2; -.
DR   Proteomes; UP000003070; 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: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; 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:SF4; TYPE I RESTRICTION ENZYME ECOKI METHYLASE SUBUNIT; 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   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EFQ52970.1};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          125..439
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   484 AA;  55613 MW;  AD4925F3EEDFA4AD CRC64;
     MVMSNQEIVQ QLWKESDVLR DDGVTYQDYV TELTYILFLK MSKEQNEEAE IPEKYRWDSL
     LQYEGLELMN FYRQLLLDLG NPQKTNSPRI NAIYDNASTS IDEPANLEKI IHDIDGLDWF
     SARQEGLGAL YEGLLEKNAN ETKSGAGQYF TPRPLINMMV RMTKPQVGER LNDPAAGTFG
     FMVAANDYLS EQTDEFFDLS QEDRKFEKEE AFSGMELVPN THRLALMNQY LHGMDGRLDQ
     GDSLSAAGKW MKNFDVVLTN PPFGTKKGGE RATRDDLTYE TSNKQLNFLQ IIYNSLKTDG
     HGRAAVVVPD NVLFADGTGE AIRKDLLNKC NLHTILRLPT GIFYAQGVQT NVLFFTRGAS
     DTDNTKEIWI YDMRHQMRTF GKRNPLNEKD FAEFEKLFSA DDLTKRKENW DKDKNPNGRW
     RKFTIDEIMK RPNTSLDISW MNEEEEHDNR SLKEILSEMN DKSTAISEAI AELNKALEGI
     NDED
//
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