ID A0A0Q6YRA6_9BRAD Unreviewed; 547 AA.
AC A0A0Q6YRA6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=ASC80_22145 {ECO:0000313|EMBL:KQW18214.1};
OS Afipia sp. Root123D2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW18214.1, ECO:0000313|Proteomes:UP000051348};
RN [1] {ECO:0000313|EMBL:KQW18214.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW18214.1,
RC ECO:0000313|Proteomes:UP000051348};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW18214.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW18214.1,
RC ECO:0000313|Proteomes:UP000051348};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQW18214.1}.
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DR EMBL; LMDP01000005; KQW18214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q6YRA6; -.
DR STRING; 1736436.ASC80_22145; -.
DR OrthoDB; 9806213at2; -.
DR Proteomes; UP000051348; 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:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 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:KQW18214.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051348};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 21..225
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 547 AA; 61262 MW; AB57E05B2CDCD9E5 CRC64;
MEGEFDVQLE GERPWQADLC QFFTRESVAE LCLRHVAFPE NILTMKLLEP AAGQGAFFLP
LLPRLVEACY AQGKKFDILG PVIRAYEIDP EVAASLRAKC AGKLEDLGIS RAKAKEIAQS
WIKHEDFLEA RPSKRFTHIV SNPPYIRWDA IPARLRDVYK ARFKSFKQRA DLYVAFIEHA
LGLLEPHGQL AFLCPGTWTR NVYGNSIREA LTSQGQLKSI IDFSDVDSFE TSADAYPHFF
VFQRDISGPT KISSVKEFDK IERSGDEIVR AFLPSASPLL LTRDSAAENA VNAARQRFPK
LEDVGCTIRV GSATGCNDVF LGQAKEIAIE RSRLLPFVNA RSIHDGKVRW AGTHIVNVFD
RNGKVVELSK FPRMAAYLRK NKKALQSRAK ASQSKIWWRT IDSLHPDWHA SPKLLIVDVS
AAPVIGIDLH GYCAGSGVYQ IKSDHWPLAD LLTFLSAGVL GLFVASLSAG SKAGFHRFQK
SQIAAVHMPQ WADLSPDWRV KFKDARKAKD GRAVLNLVAE LYECDASLLE NHVARDWDAF
CSKRPRQ
//
