ID A0A1T1AQ31_RHOFE Unreviewed; 527 AA.
AC A0A1T1AQ31;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=RF819_05245 {ECO:0000313|EMBL:OOV06209.1};
OS Rhodoferax fermentans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=28066 {ECO:0000313|EMBL:OOV06209.1, ECO:0000313|Proteomes:UP000190750};
RN [1] {ECO:0000313|EMBL:OOV06209.1, ECO:0000313|Proteomes:UP000190750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 7819 {ECO:0000313|EMBL:OOV06209.1,
RC ECO:0000313|Proteomes:UP000190750};
RA Kim Y.J., Farh M.E.-A., Yang D.-C.;
RT "Genome sequencing of Rhodoferax fermentans JCM 7819.";
RL Submitted (JAN-2017) 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:OOV06209.1}.
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DR EMBL; MTJN01000002; OOV06209.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T1AQ31; -.
DR STRING; 28066.RF819_05245; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000190750; 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; 1.20.1260.30; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR022749; D12N6_MeTrfase_N.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF4; TYPE I RESTRICTION ENZYME ECOKI METHYLASE SUBUNIT; 1.
DR Pfam; PF12161; HsdM_N; 1.
DR Pfam; PF02384; N6_Mtase; 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 ECO:0000313|EMBL:OOV06209.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000190750};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OOV06209.1}.
FT DOMAIN 12..125
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 137..401
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 527 AA; 59000 MW; 513BCBEAB264A617 CRC64;
MNQINPAASD IVAKLWNLCN LLRDDGVTYH QYVSELTYLL FLRMMQETGQ EDGLVIYKAP
KRGEPQVKMD GTRWADLMAA SAPERLDLYK ELLLDYGLHG RGSVQQIYAN ASTFITKPAT
LSKLVLEIDK LDWYSVQRDD LGDLYEGLLE RNANEKKSGA GQYFTPRDLI DSIVTVLQPT
MVDVIQDPAA GTGGFLIAAN NHLRAKFKPE DRSETQQRKY RHSTFFGMEL VQDTHRLALM
NMLLHGIEGG IQFGDTLGEE GTRLPTATLI LSNPPFGTKK GGGLPTRTDF TYPTTNKQFC
FLQHIYRNLK PGGRAAVVLP DNVLFESNVG ADIRRDLMDK CNLHTILRLP TGIFYAQGVK
TNVLFFTRGQ TDTGNTKQVW VYDMRANMPQ FGKRTPFTRD YFRTASAAAP DVPRDKFEDV
FGPDPYGGPA ALAQRVDTGE AGRWRCFSRE YIQARGDNLD ISWLKDDSAE SAQAQRDEPA
LVARLLMHEL SGAMADLRSL LEELGEDPDA ALEDLLIDDE EAVRAPT
//
