ID A0A257TE62_9BACT Unreviewed; 520 AA.
AC A0A257TE62;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=B7X04_03265 {ECO:0000313|EMBL:OYV83694.1};
OS Parcubacteria group bacterium 21-54-25.
OC Bacteria.
OX NCBI_TaxID=1970248 {ECO:0000313|EMBL:OYV83694.1, ECO:0000313|Proteomes:UP000216537};
RN [1] {ECO:0000313|EMBL:OYV83694.1, ECO:0000313|Proteomes:UP000216537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=21-54-25 {ECO:0000313|EMBL:OYV83694.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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 -!- 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:OYV83694.1}.
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DR EMBL; NCBJ01000008; OYV83694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257TE62; -.
DR Proteomes; UP000216537; 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 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; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDI METHYLASE SUBUNIT; 1.
DR PANTHER; PTHR42998; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 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:0000313|EMBL:OYV83694.1};
KW Transferase {ECO:0000313|EMBL:OYV83694.1}.
FT DOMAIN 17..134
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 160..479
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT COILED 488..515
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 520 AA; 58357 MW; 36B5F15174F6475D CRC64;
MKMKNDSTEK NGQNARLEGQ LFSAADKLRK NIDAAEYKHI VLGLIFLKYI SDSFEVMHEK
LSSGKADYAG ADPEDPDEYR AENVFWVPQE ARWTHLHSRA KQPSIGKDLD AAMDAIEKHN
PTLKSILPKV FASPNIDKLA LGALIDLISN IALGDEAAKS KDILGRVYEY FLGQFASAEG
KKGGQFYTPR SIVELMVDMI EPHKGRVYDP ACGSGGMFVM SEKFVLSHRG RIDDISVFGQ
ESNHTTYRLA RMNLAIRGID GSQVEWNNEG SFLKDAHPDL KADYILANPP FNQDDWGWDI
VKNDPRWQYG MPPSGNANFG WMQHMIYHLA PKGVMAMVLA NGSLSSNQSG EGEIRQNIVD
ADLVDCIVAL PKQLFYNTGI PACLWFISRK RLGNGDRKRT GEVLFIDASE MGHLVDRTHR
EFTDEDVQKI AQTYHEWRSK DGKYEDVKGF CRSAALPEIQ KHKYVLTPGR YVGAAAVADD
GEPFDEKMKR LTSTLKSQMA EEEQLNAEIA KQLKKVGFDL
//