ID A8YW15_LACH4 Unreviewed; 484 AA.
AC A8YW15;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=lhv_1480 {ECO:0000313|EMBL:ABX27442.1};
OS Lactobacillus helveticus (strain DPC 4571).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=405566 {ECO:0000313|EMBL:ABX27442.1, ECO:0000313|Proteomes:UP000000790};
RN [1] {ECO:0000313|EMBL:ABX27442.1, ECO:0000313|Proteomes:UP000000790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPC 4571 {ECO:0000313|EMBL:ABX27442.1,
RC ECO:0000313|Proteomes:UP000000790};
RX PubMed=17993529; DOI=10.1128/JB.01295-07;
RA Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA Beresford T., Ross R.P.;
RT "Genome sequence of Lactobacillus helveticus: an organism distinguished by
RT selective gene loss and IS element expansion.";
RL J. Bacteriol. 190:727-735(2008).
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}.
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DR EMBL; CP000517; ABX27442.1; -; Genomic_DNA.
DR RefSeq; WP_012212064.1; NC_010080.1.
DR AlphaFoldDB; A8YW15; -.
DR REBASE; 16732; M.LheDORF1480P.
DR KEGG; lhe:lhv_1480; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_018284_2_0_9; -.
DR Proteomes; UP000000790; 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; -; 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; 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; 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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..112
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 123..439
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT COILED 454..484
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 484 AA; 56010 MW; E74C62C23784943C CRC64;
MTNQEIVQKL WNECNVLRDD GVSYQDYITE LTYILFLKMS KEQDEEKDIP EKYRWDNLVN
KEGLELKNFY RQLLLDLGNP EVVKSERINA IYANASTAID EPANLEKIIK DINDLDWWSA
REEGLGDLYE GLMEKNANEV KSGAGQYFTP RVLINMMVKM TKPKIGDRCN DPAAGTFGFM
VAADQYLKDK TDDYSELSEE KYDFQVKEAF SGMELVPNTH RLAIMNEYLH GMDGRLEQGD
SLSANGKWMK NFDVVLTNPP FGTKKGGERV TRDDLTYETS NKQLNFLQII YNSLKRDGKA
RAAVVVPDNV LFADGVGEEI RKDLLNKCNL HTILRLPTGI FYAQGVQTNV LFFTRGEEDK
DNTKETWIYD MRHQMRSFGK RNPLNDKDFV EFEKLFCVDD RSKRKETWDK EKNPNGRWRK
FTIDEIKKRP NTSLDISWMS DEEEHETKSL KEILSDMNEK SKAISEAIAE LNKALEGIDD
SEDE
//
