ID A0A369T809_9PROT Unreviewed; 495 AA.
AC A0A369T809;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=DRB17_17125 {ECO:0000313|EMBL:RDD60594.1};
OS Ferruginivarius sediminum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Ferruginivarius.
OX NCBI_TaxID=2661937 {ECO:0000313|EMBL:RDD60594.1, ECO:0000313|Proteomes:UP000253941};
RN [1] {ECO:0000313|EMBL:RDD60594.1, ECO:0000313|Proteomes:UP000253941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WD2A32 {ECO:0000313|EMBL:RDD60594.1,
RC ECO:0000313|Proteomes:UP000253941};
RA Wang S.;
RT "Venubactetium sediminum gen. nov., sp. nov., isolated from a marine solar
RT saltern.";
RL Submitted (JUL-2018) 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:RDD60594.1}.
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DR EMBL; QPMH01000023; RDD60594.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369T809; -.
DR Proteomes; UP000253941; 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 GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
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; 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.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:RDD60594.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253941};
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:RDD60594.1}.
FT DOMAIN 7..113
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 124..429
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 495 AA; 55819 MW; 0783EE2BED21D435 CRC64;
MKDARELAQK VWSYANVLYD DGVGVADYVE QITCLLFLKM DEERAENMNE PSLVPEGYRW
GDLKGKSGPE LEQQYRHTLE ALATQPGLLG TIYRKAQNKI QDPAKLRRLV SLIDAETWIG
LPVDVKGNIY EDLLERTASE SKTGAGQYFT PRPLIDAIVE VMQPGIGESV HDPACGTGGF
LIAAYEHMRK GEKDRTRLRR LRRETFTGRD ITDGVVRLCA MNLYLHGIGG EEEAPVAQGD
SLIDDDGRRY DKVLTNPPFG KKSSYTFVGA DGAAGREAMT YERQDFIATT SNKQLNFLQH
ITTILAENGS AAVVLPDNVL FEGGAGERIR RKLLERFDFH TLLRLPTGIF YKPGVKANVL
FFDKKPAAET PWTKHLWIYD LRTNQHFTLK ERPLERHHLD DFVACFKPGR RAEREESERF
RCFSYDELVA RDKANLDIFW LKDESLEDAD SLPAPEVLAA EIVENLEAAL EQFRSVAEEL
SGGGEKETPE KDAAE
//
