ID A0A0M1JBC5_9GAMM Unreviewed; 516 AA.
AC A0A0M1JBC5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=TI03_00720 {ECO:0000313|EMBL:KOR30010.1};
OS Achromatium sp. WMS1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Achromatium.
OX NCBI_TaxID=1604834 {ECO:0000313|EMBL:KOR30010.1, ECO:0000313|Proteomes:UP000036736};
RN [1] {ECO:0000313|EMBL:KOR30010.1, ECO:0000313|Proteomes:UP000036736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMS1 {ECO:0000313|EMBL:KOR30010.1};
RX PubMed=26322031; DOI=10.3389/fmicb.2015.00822;
RA Mansor M., Hamilton T.L., Fantle M.S., Macalady J.L.;
RT "Metabolic diversity and ecological niches of Achromatium populations
RT revealed with single-cell genomic sequencing.";
RL Front. Microbiol. 6:822-822(2015).
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:KOR30010.1}.
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; JXSM01000015; KOR30010.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M1JBC5; -.
DR PATRIC; fig|1604834.3.peg.211; -.
DR Proteomes; UP000036736; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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 Endonuclease {ECO:0000313|EMBL:KOR30010.1};
KW Hydrolase {ECO:0000313|EMBL:KOR30010.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nuclease {ECO:0000313|EMBL:KOR30010.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036736};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..158
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 172..482
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 516 AA; 57453 MW; 53489C9764177441 CRC64;
MTSTQQRSEL QRQIWQIAND VRGSVDGWDF KQYVLGTLFY RFISEHFTSS YMESDDADID
YAQLTDTDID ADIIDDAVKT KGYFIYPSQL FINIAKNANK NDNLNTDLAN IFKAIENSAN
GYPSEADIKG LFADFDTTSN RLGNTVKDKN TRLAAVLKGV AGLSFVDFQN NHIDLFGDAY
EFLISNYAAN AGKSGGEFFT PQYVSKLIVQ LAMHKQTSVN KIYDPAAGSG SLLLQAKKHF
DSHKITEGFF GQEINHTTYN LARMNMFLHN IGYDKFNIML GNTLTNPCFS DAKPFDAIVS
NPPYSVKWIG SGDPTLINDE RFAPAGVLAP KSKADFAFVL HALNYLSSKG RAAIVCFPGI
FYRGGAEKKI RQYLIDNNYI ETVISLAPNL FFGTSIAVNI LVLSKHKSNT NTQFIDASGV
DFFKKETNNN VLTDEHIQRI MDVFDSKDDV AHIAKSVSLE AIAANDYNLS VSSYVQAKDT
REVIDIIKLG TELRTTVAKI DQLRRDIDII VAKIDG
//
