ID W4M2C8_9BACT Unreviewed; 584 AA.
AC W4M2C8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=ETSY2_28420 {ECO:0000313|EMBL:ETX04504.1};
OS Candidatus Entotheonella gemina.
OC Bacteria; Nitrospinae/Tectomicrobia group; Candidatus Tectomicrobia;
OC Candidatus Entotheonella.
OX NCBI_TaxID=1429439 {ECO:0000313|EMBL:ETX04504.1, ECO:0000313|Proteomes:UP000019140};
RN [1] {ECO:0000313|EMBL:ETX04504.1, ECO:0000313|Proteomes:UP000019140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSY2 {ECO:0000313|Proteomes:UP000019140};
RX PubMed=24476823; DOI=10.1038/nature12959;
RA Wilson M.C., Mori T., Ruckert C., Uria A.R., Helf M.J., Takada K.,
RA Gernert C., Steffens U.A., Heycke N., Schmitt S., Rinke C., Helfrich E.J.,
RA Brachmann A.O., Gurgui C., Wakimoto T., Kracht M., Crusemann M.,
RA Hentschel U., Abe I., Matsunaga S., Kalinowski J., Takeyama H., Piel J.;
RT "An environmental bacterial taxon with a large and distinct metabolic
RT repertoire.";
RL Nature 506:58-62(2014).
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:ETX04504.1}.
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DR EMBL; AZHX01001204; ETX04504.1; -; Genomic_DNA.
DR AlphaFoldDB; W4M2C8; -.
DR HOGENOM; CLU_466674_0_0_7; -.
DR Proteomes; UP000019140; 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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR PANTHER; PTHR33841:SF1; DNA METHYLTRANSFERASE YEEA-RELATED; 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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000019140};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..236
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 584 AA; 65219 MW; 85ECDD9C1592E7B9 CRC64;
MKNSLKAQGF VRTPPSIAAL LARWALRAPT DHVLDAGFGE GVFLLESAKR LLELGTALPD
LQGQLHGVDS HPDAVASLQR AFRSFGLPSE LPGVFVGDLF ESEFPRIDGL IGNPPYVRRW
WQKDVDALQL LAEQVPEVGQ FSRLTDLACY FIIYAARFLK PRGRLALIVS DSWLDMRYGT
AFKAYLLRSF QIRAMIGFQS QVFPDVLVRP VVILAEKRPA PRAPGRKQVA FVSLNGRLPK
AIPLDPCRLL THDEMAVSGT VARMQDLQPQ AKWTSLLYAP KAYADLLTHP LMTPLASLAQ
ARIGLQSFAK MFYIVPRETQ QRWGLEQRWL LPMALSPKDF DEPLLAPDTA VRHYVVACHR
EKAQLKGTQI LNYIEHWERQ VLNPRGLARP VIGVQNLPRV RKTRRDPWYN LVDDLTRRGT
APVLLPRRIY QRYRVVRNQA GWVAGENFIE VLPQPHVPLE PLLAVLNAGV SEMALRVSAH
VYGGGVYNLS PGSVGDVPVV DVGQLSDAQQ ERLTAAYRAF LLSKGKDRSA LDDAVLEVLD
LPPAFAASLE SALDRMQHLS DAVLEPIAVD PNEGNTWPEE LRLL
//