ID Q9RZJ0_DEIRA Unreviewed; 609 AA.
AC Q9RZJ0;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=DR_B0137 {ECO:0000313|EMBL:AAF12566.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OG Plasmid megaplasmid MP1 {ECO:0000313|Proteomes:UP000002524}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF12566.1, ECO:0000313|Proteomes:UP000002524};
RN [1] {ECO:0000313|EMBL:AAF12566.1, ECO:0000313|Proteomes:UP000002524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524};
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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};
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DR EMBL; AE001826; AAF12566.1; -; Genomic_DNA.
DR PIR; D75633; D75633.
DR RefSeq; NP_051667.1; NC_000958.1.
DR RefSeq; WP_010883983.1; NZ_JMLF01000035.1.
DR AlphaFoldDB; Q9RZJ0; -.
DR DNASU; 1799868; -.
DR EnsemblBacteria; AAF12566; AAF12566; DR_B0137.
DR GeneID; 69519385; -.
DR KEGG; dra:DR_B0137; -.
DR PATRIC; fig|243230.17.peg.134; -.
DR HOGENOM; CLU_448135_0_0_0; -.
DR InParanoid; Q9RZJ0; -.
DR OrthoDB; 9815272at2; -.
DR Proteomes; UP000002524; Plasmid megaplasmid MP1.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR046816; MmeI_Mtase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF20473; MmeI_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Plasmid {ECO:0000313|EMBL:AAF12566.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002524};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 471..548
FT /note="MmeI-like DNA-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20473"
SQ SEQUENCE 609 AA; 66907 MW; 9C57FED47D15FFEB CRC64;
MTTQLHHVRL HGLGLTDDFL LQLSDRAQTG KVEGATPASY DLPPKTSLEE AIQDAWDDAR
KAWAKYQQHG TDAWAGWVRP LLRALDYNFV GGGAAGGKYA VGHLTETGDV PLHFTRQPDL
DRVTDETGLR VSPHGLMQGY LNATPEHLWG LVTNGETLRL LRDNAQVTRP AYAEFQIGEM
LRTEDARAFR VLWLLLHRTR LRGGKVGPLE AWNEASKVLG QRANDTLRDG VQLAIEHLGT
GFLRHNPELL ERTRSGEVKA EDLYRAALTT VYQMVFLFVT EDRDLLFARD EDGEYLPDAQ
TRARAAHYLT RALRQKAGSV NGNPLHHDAY VAWERLLGYL RGGFAPLGLP ALGSLLFQPT
LLSGLKLGND AFYGAVRALS EISVNGSLRP VNYAGLDSEE LGSIYESLLE LVPRIEPGPR
FSLTVLPGNE RKSTGSYYTP GSLIDLLLDS ALDPVIEDAV RDKLPEDAIA ALKGLKVIDP
ACGSGHFLIA AARRIGARLA ELEEETSLPS PRALRKATRT VIAHCIYGAD INPMAIELAK
VALWLESQDA GRPLAFLDHR LRVGNSLLGA TPELMNAEDE IPEKTVRGVT SRAVRAHTLH
LPDEAFSAI
//
