ID A0A126ZDM1_9BURK Unreviewed; 519 AA.
AC A0A126ZDM1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=AX767_13380 {ECO:0000313|EMBL:AMM25240.1};
OS Variovorax sp. PAMC 28711.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1795631 {ECO:0000313|EMBL:AMM25240.1, ECO:0000313|Proteomes:UP000070169};
RN [1] {ECO:0000313|EMBL:AMM25240.1, ECO:0000313|Proteomes:UP000070169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 28711 {ECO:0000313|EMBL:AMM25240.1,
RC ECO:0000313|Proteomes:UP000070169};
RA Park H.;
RT "Complete genome of Variovorax sp.";
RL Submitted (FEB-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; CP014517; AMM25240.1; -; Genomic_DNA.
DR RefSeq; WP_068631791.1; NZ_CP014517.1.
DR AlphaFoldDB; A0A126ZDM1; -.
DR STRING; 1795631.AX767_13380; -.
DR REBASE; 140824; M.Vsp28711ORF13380P.
DR KEGG; vaa:AX767_13380; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000070169; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDI METHYLASE SUBUNIT; 1.
DR PANTHER; PTHR42998; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 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.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Endonuclease {ECO:0000313|EMBL:AMM25240.1};
KW Hydrolase {ECO:0000313|EMBL:AMM25240.1};
KW Nuclease {ECO:0000313|EMBL:AMM25240.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070169}.
FT DOMAIN 6..148
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 161..479
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 519 AA; 57237 MW; 9B3C895EC3A27FBE CRC64;
MIDTFKKALW ATADKLRANM DAAEYKHLVL GLIFVKYISD TFAARRAELV TRFADPADEY
HFADATADDL AAELEQRDYY RAANVFWVPE AARWESIRAA AKQPDIGKRI DEALTLIEAE
NPSLKGILDK RYARAQLPDG KLGELIDLVS TIGFGVDAAQ ARDVLGQVYE YFLGMFANAE
GKRGGQFYTP RSIVKTLVAV LAPHHGKVYD PCCGSGGMFV QSEEFIEAHG GKRGDVSIYG
QEANPTTWRL AAMNMAIRGL DFDLGKEPAD TFVRDQHKDL RADFVLANPP FNISDWWHGS
LEGDARWVYG DPPQGNANYA WLQHMLHHLK PDTGRAGIVL ANGSMSSSQN GEAQIRAAMV
EADVVEVMVA LPGQLFFNTQ IPACLWFLAK KKAPARKGEV LFIDARKLAT MISRVQCELT
DAVIDRIANT VAAWRGDASA PAYEDVAGFC RSVKLEEIAQ HGHVLTPGRY VGAEAVEDDD
EAFAEKMQKL TETLGEQMAK GAELDALIRK KLGGLGYEF
//
