ID A5GCE0_GEOUR Unreviewed; 541 AA.
AC A5GCE0;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=Gura_0548 {ECO:0000313|EMBL:ABQ24762.1};
OS Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=351605 {ECO:0000313|EMBL:ABQ24762.1, ECO:0000313|Proteomes:UP000006695};
RN [1] {ECO:0000313|EMBL:ABQ24762.1, ECO:0000313|Proteomes:UP000006695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rf4 {ECO:0000313|EMBL:ABQ24762.1,
RC ECO:0000313|Proteomes:UP000006695};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M.,
RA Lovley D., Richardson P.;
RT "Complete sequence of Geobacter uraniireducens Rf4.";
RL Submitted (MAY-2007) 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};
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DR EMBL; CP000698; ABQ24762.1; -; Genomic_DNA.
DR RefSeq; WP_011937487.1; NC_009483.1.
DR AlphaFoldDB; A5GCE0; -.
DR STRING; 351605.Gura_0548; -.
DR REBASE; 15257; M.GurRORF548P.
DR KEGG; gur:Gura_0548; -.
DR HOGENOM; CLU_037306_0_0_7; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000006695; Chromosome.
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; 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; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 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:ABQ24762.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006695};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 179..495
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 541 AA; 61623 MW; 986DF2A60B0E53FD CRC64;
MVARDFTAKT KELIDNLKGV CASYGLGNDG NEFKIITQVF LYKFMNDKFG YEVKEMEPKL
KKAAIWEQEI AKYSDKDYEM LLLKMSPDSA RLKREHFLPR LHNRQNEGEF AKLFDDTLRD
IAIFNNDIFS VKTGTGAKVT LFDELSNFIT DSSRRDDFCR AIITQLIPFS FEKIFHQKLD
FFSTIFEYLI KDYNKDGGGK YAEYYTPHAV SKIMAAILVD KPVKNVTCYD PSAGSGTLLM
NLAHAIGEDR CTIYSQDISQ KSTSMLRLNL ILNNLVHSIQ NIIQGNTMLT PYHKSGDKLM
TFDYVVSNPP FKLDFSDFRN DLETKQNRDR FFAGIPKIPN KDKDKMAIYL LFIQHIMFSL
SAKGKAAIVV PTGFITAQSG IEKKIREKLV VAKMLRGVVS MPSNIFATTG TNVSVLFLDK
TNTKGDIVLM DASKLGTTVK EGKNQKTVLS VAEEELIIKT FNDHKAVEDF TVVVSYEQIK
EKNYSLSAGQ YFDVKIEYTD ITPKEFTAKM AGYWKNLDQL FGESQKLEKE IKKQLVGLKY
E
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