ID A0A1M7IS51_9STAP Unreviewed; 531 AA.
AC A0A1M7IS51;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SAMN02745189_02134 {ECO:0000313|EMBL:SHM43187.1};
OS Salinicoccus alkaliphilus DSM 16010.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Salinicoccus.
OX NCBI_TaxID=1123231 {ECO:0000313|EMBL:SHM43187.1, ECO:0000313|Proteomes:UP000184206};
RN [1] {ECO:0000313|EMBL:SHM43187.1, ECO:0000313|Proteomes:UP000184206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16010 {ECO:0000313|EMBL:SHM43187.1,
RC ECO:0000313|Proteomes:UP000184206};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FRCF01000011; SHM43187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M7IS51; -.
DR STRING; 1123231.SAMN02745189_02134; -.
DR Proteomes; UP000184206; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000184206};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 15..164
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 179..480
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT COILED 484..515
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 531 AA; 60781 MW; 931FDD5C2B967FD5 CRC64;
MMTVTEKQRQ QQAELHKRLW DIANDLRGNM DASEFRNYIL GLIFYRFLSE KTEDVVNDLL
KEDELSYREA WEDEEYREAL QDELTTRIGY IVEPKYLFSR MIEEIEQGEF DIEKLSEAIS
AVEASTLGEA SEDDFTHLFD DMDLTSSRLG NNVSARTKLI SKVMLNLSTL PFVHSDLEID
MLGDAYEYMI GQFAATAGKK AGEFYTPQQV SKILAEIVTT GKKNLRNVYD PTCGSGSLLL
RVGKHANVRH FYGQEYNSTT YNLARMNMLL HDVNYKAFTI ENGDTLEEPA FMDMKFEAVV
ANPPYSAKWS ADPSFNDDER FSGYGKLAPK SKADFAFIQH MVHYLADNGT MAVVLPHGVL
FRGAGEGTIR KYLIEQKNYL DAVIGLPANI FFGTSIPTTI LVLKKSRETD DVLFIDASQS
FEKGKNQNHL TDDDVKKIVE TYRNREEIDK YSHVALREEI EENEYNLNIP RYVDTFEEEE
PVDIKALHEE IKDINKELEE AEASLLEMLD ELEGDEDGLA LIEATKEVFR R
//
