ID A0A0W1A354_9GAMM Unreviewed; 676 AA.
AC A0A0W1A354;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=Lwal_2595 {ECO:0000313|EMBL:KTD75657.1};
OS Legionella waltersii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=66969 {ECO:0000313|EMBL:KTD75657.1, ECO:0000313|Proteomes:UP000054729};
RN [1] {ECO:0000313|EMBL:KTD75657.1, ECO:0000313|Proteomes:UP000054729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51914 {ECO:0000313|EMBL:KTD75657.1,
RC ECO:0000313|Proteomes:UP000054729};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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:KTD75657.1}.
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DR EMBL; LNZB01000056; KTD75657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W1A354; -.
DR STRING; 66969.Lwal_2595; -.
DR PATRIC; fig|66969.6.peg.2806; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000054729; 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; 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 PANTHER; PTHR42933:SF3; 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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054729};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 15..150
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 165..479
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 676 AA; 77799 MW; B9D2105F38B185D4 CRC64;
MKNENNKKIE NLSTFSWSIA EILRGDFKQS EYGKVILPFV VLRRLDCILE PSKDAVVSAN
EKLPEGIDDH TKDMMLFSAV GGGLKVYNYN TLTFSKIRNQ DPGDVHKNLL DYITSFNSSV
RDIFLEKFLF TDQLKRLKDG GILWQVFDLF CQIDLHPDNI SNIEMGYLFE DLIRRFSEIS
NETAGEHFTP REVIRLIVDL LLINDAEALA GSGIIRTVYD PACGTGGMLA LMEEAMKEYN
SKIRVELYGQ ELNPESFGIC TSDMLVTGHN PEQIAFGNTL TEDAHKDKKF HYMLSNPPYG
VDWKKYQDPI KQEAQEKGMD GRFGAGLPRI SDGQLLFLQH MISKMRDDEV GSRIGIVMNG
SPLFTGGAGS GESEIRRWML ENDWVEAIIA LPTDLFYNTG IQTYVWMLTN KKDKNRWGKV
QLINASSERF WQSMRKSLGS KRREIPDHAR SEIVKIYYEM LNGGGDWSEF SKIFDREEFG
YREIRIERPL RLNFEGSNER LELLQHEKTF LNLSKIEQQE LIVALNHNTL KQQFKNRDAF
EEALKTSLKN LSFKLTTPLK KAILSTLSEK DETADICYDA KGNPEPDADL RDHELVPLTE
DWREYVEREV KPFVADAWVD DSYKDITDGK VGRIGYEINF NRYFYKYVPP RSVTEIDEEL
KQLEADIANL LKEVVE
//