ID A0A1H8Y742_9PROT Unreviewed; 608 AA.
AC A0A1H8Y742;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=SAMN02990966_06932 {ECO:0000313|EMBL:SEP47912.1};
OS Rhodospirillales bacterium URHD0017.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales.
OX NCBI_TaxID=1380357 {ECO:0000313|EMBL:SEP47912.1, ECO:0000313|Proteomes:UP000198826};
RN [1] {ECO:0000313|EMBL:SEP47912.1, ECO:0000313|Proteomes:UP000198826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URHD0017 {ECO:0000313|EMBL:SEP47912.1,
RC ECO:0000313|Proteomes:UP000198826};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FODP01000024; SEP47912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8Y742; -.
DR STRING; 1380357.SAMN02990966_06932; -.
DR OrthoDB; 9806213at2; -.
DR Proteomes; UP000198826; 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 CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.20.1260.30; -; 1.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR022749; D12N6_MeTrfase_N.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
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; PF13560; HTH_31; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..54
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000259|PROSITE:PS50943"
SQ SEQUENCE 608 AA; 67768 MW; FE0DABAD467A43F4 CRC64;
MTKMQPVAAT LRTIRANLNL SQERLAERLG VSFATVNRWE GGANVPQKAA LAAIEALAAE
AGIDPDGPNT DVAEAAAKVT RRRLAVKSAT TSTKTMEQML WDAACSIRGE KDAAKFKDYL
LPLLFLKRLS DVFDDEINRL AEEYGDRNTA LEIAEDDHAL LRFYLPPETR WAVISGREPY
DWPNDEQDRS TRPRDIGEHL TKAVRAVMRQ NPSLSGVIDV VDFAAERNGE RDINPAKLRE
VVETFSDPRY RLGLADVQPD FLGRAYEYLL RKFAEGSGQS AGEFFTPTEV GFLMAHIMRP
KPGEECHDYA CGSAGLLVKL QLIARELDPT SKVPLKLYGQ ELTAESYAVA QMNAIIHDMS
VEMARGDTMI NPKFKTADSK IRTYDIVVAN PMWNQPFNPD IFTDDPLDRF RAAGGTTTGK
GDWAWLQHTL ACLNDRGRAA VVLDTGAITR GSGSKNEDKE RNIRKWFVDR DLIDGVILLP
DNLFYNTTAA GVIVVLNKRK PAARKDKIVL LNVTRRVQKG RPKNFIPEDD IRPLAAAFLK
GEPVEGEIAI ITRQQAEEAD YNLSPSRWVA QSDTADHRPL KDIVAELLRL DEQAQVIDAS
LAKMLVRL
//
