ID A0A0Q7SDC3_9BURK Unreviewed; 402 AA.
AC A0A0Q7SDC3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=ASD35_20240 {ECO:0000313|EMBL:KQY85967.1};
OS Pelomonas sp. Root1444.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1736464 {ECO:0000313|EMBL:KQY85967.1, ECO:0000313|Proteomes:UP000051648};
RN [1] {ECO:0000313|Proteomes:UP000051648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1444 {ECO:0000313|Proteomes:UP000051648};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY85967.1, ECO:0000313|Proteomes:UP000051648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1444 {ECO:0000313|EMBL:KQY85967.1,
RC ECO:0000313|Proteomes:UP000051648};
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 -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
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:KQY85967.1}.
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DR EMBL; LMFP01000011; KQY85967.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q7SDC3; -.
DR STRING; 1736464.ASD35_20240; -.
DR Proteomes; UP000051648; Unassembled WGS sequence.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
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; PF07669; Eco57I; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000051648};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 61..173
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
SQ SEQUENCE 402 AA; 44886 MW; 2C053D6D69867AF2 CRC64;
MERFPRVLDL GAGDARFSRA VDAYDSYTGI EFDPAKAHSV TLPEKAKLIE ADAMAWVDQG
FSLCIGNPPY IRYHGLEVKW REKALQTLED ATGVQLKRSA NAFVMFLLRA LQLTADDGLV
VQLIPFEWVT RPSAKELRDH IKTNGWATTV YRFDCEIFPR VLTTASITII DKRRKDPVWK
FGIIGKGGQV RSIAEPSGSS EAVLAYAKRA EDIYGLRGLS PGGQDIFVLT EEERLQFALR
KTRDVTPCVT TLRHLGQDLA VLDAEAFNRL YVAAGKRCWL IRSDKDVLSE PLQAYLKAVG
NRWRAYSTCT ERSVWWRYKP HPAPEMLFSS GFVGSGTKVL VNKVRAIAAG SVYGVISTGA
RSVDKIADEL RGYDFAKRVV SHSNNLKKVE VRQLNAVLAE IA
//
