ID A0A3N4Q7B6_9BACT Unreviewed; 522 AA.
AC A0A3N4Q7B6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=EGT74_08000 {ECO:0000313|EMBL:RPE13451.1};
OS Chitinophaga lutea.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=2488634 {ECO:0000313|EMBL:RPE13451.1, ECO:0000313|Proteomes:UP000278351};
RN [1] {ECO:0000313|EMBL:RPE13451.1, ECO:0000313|Proteomes:UP000278351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZY74 {ECO:0000313|EMBL:RPE13451.1,
RC ECO:0000313|Proteomes:UP000278351};
RA Zong Y.;
RT "Chitinophaga lutea sp.nov., isolate from arsenic contaminated soil.";
RL Submitted (NOV-2018) 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:RPE13451.1}.
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; RPDH01000001; RPE13451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4Q7B6; -.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000278351; 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:RPE13451.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000278351};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RPE13451.1}.
FT DOMAIN 8..143
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 157..486
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 522 AA; 59815 MW; F59741F0DF66150C CRC64;
MLPDEIKYKV KELWDKFWSG GISNPLNAIE QITYLLFLKQ LDEKDQQREK TAEFLNEKYK
SIFDGKFTIP SENEKRKAVP KTSLRWSSFT KLPSDEMFDT VQTKVFPFIK QLNGQNSHFT
KHMQSASFLI PSPRLLAEAV KKIDEIFIEL EKEKRFIDAQ GDFYEELLRE LNTSGKNGQF
RTPTHIIELI IELVQPKLGS KIADPACGTA GFLIGAYKYI ITSQTSAQYC QPDENGFLRG
SIADKLVSKQ ARKELEEDTF FGFDIDPTMI RIGLMNLMMH GISVPKIDYN DTLSKNYNED
ECYDMVLANP PFTGNIDKGD LNPTFSINTT KSELLFLERI YKMLRPGGTA AVIVPQGVLF
GSGSAFRKIR QLLLDNCKLS AIISLPSGVF KPYAGVATAI LVFTKGGESE NVWFYDMISD
GRTLDDKRSE LFKGNGDRDY GDLHEIITQY RSKDKSTNRR LRHFIVPTSE IVANEYDFSF
KRYREEFFEE LETEDPQKIL LQLSELEKEI QDGLNELKSI FQ
//
