ID A0A0A1VFN0_9BURK Unreviewed; 587 AA.
AC A0A0A1VFN0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=AVS7_02143 {ECO:0000313|EMBL:GAD22383.1};
OS Acidovorax sp. MR-S7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1268622 {ECO:0000313|EMBL:GAD22383.1};
RN [1] {ECO:0000313|EMBL:GAD22383.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-S7 {ECO:0000313|EMBL:GAD22383.1};
RX DOI=10.1128/genomeA.00412-13;
RA Miura T., Kusada H., Kamagata Y., Hanada S., Kimura N.;
RT "Genome Sequence of the Multiple-beta-Lactam-Antibiotic-Resistant Bacterium
RT Acidovorax sp. Strain MR-S7.";
RL Genome Announc. 1:e00412-13(2013).
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; DF238918; GAD22383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1VFN0; -.
DR STRING; 1268622.AVS7_02143; -.
DR eggNOG; COG1002; Bacteria.
DR Proteomes; UP000030646; Unassembled WGS sequence.
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; IPR046819; MmeI_hel.
DR InterPro; IPR046816; MmeI_Mtase.
DR InterPro; IPR046817; MmeI_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR33841:SF6; DNA METHYLTRANSFERASE A; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF20465; MmeI_hel; 1.
DR Pfam; PF20473; MmeI_Mtase; 1.
DR Pfam; PF20464; MmeI_N; 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 ECO:0000313|EMBL:GAD22383.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030646};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..159
FT /note="MmeI-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20464"
FT DOMAIN 172..253
FT /note="MmeI-like helicase spacer"
FT /evidence="ECO:0000259|Pfam:PF20465"
FT DOMAIN 329..587
FT /note="MmeI-like DNA-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20473"
SQ SEQUENCE 587 AA; 64948 MW; 15705CC92322633A CRC64;
MNAVEIESAV SDLAAQPFDA AEFPYAFLAA FGNKETTLKR LRTGNNNASD VPGGVLLRNN
IHIAVCDAGA VGESLRTLRD SPATTKAKAK FILATDGQTL EAEELISGET IACDFEDFPN
HFGFLLPLAG ISTIKEIKDN PIDVRATGRL NKLYVELLRE NPDWAKEERR SDMNHFMARL
VFCFFAEDTD IFDGKGLFTQ TVDRMSANDG SNTHQVLSEI FRAMNIKVSE RANSDPRLPN
WANGFPYVNG GLFSGSTEVP RFTRMARTYL LHAGALSWRE INPDIFGSMI QAVADDDERG
ALGMHYTSVP NILKVLNPLF LDDLRAALAD AGDNERKLLN LRKRMARIRV FDPACGSGNF
LVIAYKQMRE IEAEINRRRD EVHLRSEIPL TNFRGIELRD FPAEIARLAL IIAEFQCDVL
YRGQKDALAE FLPLDAQNWI VCGNALRLDW LSICPPSGTG VKVVADDLFL TPLDQKEIDF
ENDGGETYIC GNPPYLGSKW QSDAQKADLA AVFAAHGTGW KTLDYVAGWF MKAADYGAKA
SSATAFVSTN SICQGVQVPI LWPLVFATGH QIVFAHTSFK WANLASN
//
