ID A0A1G8HHK7_9PSED Unreviewed; 611 AA.
AC A0A1G8HHK7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=SAMN05216603_12022 {ECO:0000313|EMBL:SDI06075.1};
OS Pseudomonas benzenivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=556533 {ECO:0000313|EMBL:SDI06075.1, ECO:0000313|Proteomes:UP000199168};
RN [1] {ECO:0000313|Proteomes:UP000199168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8628 {ECO:0000313|Proteomes:UP000199168};
RA Varghese N., Submissions S.;
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; FNCT01000020; SDI06075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8HHK7; -.
DR STRING; 556533.SAMN05216603_12022; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000199168; 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:SF3; TYPE I RESTRICTION ENZYME MJAVIII 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 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 6..138
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 152..447
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT REGION 513..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 611 AA; 68466 MW; 0821E66D6652B783 CRC64;
MNQQALSAFI WSVADLLRGD YKQSEYGKVI LPFTVLRRLD CVLEKTKAAV LAEQAEKLKL
VANPEPFLLR KAGQSFYNIC AMDMVRLMGD PDHIRDNLYS YIQGFSLPVR DIFERFDFYT
QIDRLHKCGL LYQVAERFAQ IDLHPEAVDN MQMGLVFEEL IRKFAEISNE TAGEHFTPRE
VIRLMVNLIF IEDDQVLANP GVVRNLYDPT AGTGGMLSIA EEYLVEHNPQ ARLNLHGQEL
NDESYAICKA DMLIKGQDVA NIKAGNTLSD DGHAGKRFDY MLSNPPFGVE WKRVEKAIRQ
EHEQQGFNGR FGPGLPRVSD GSLLFLMHLI AKMRPANEGG SRFAIVLNGS PLFTGGAGSG
ESEIRRYVLE NDLVEAIIGL PTDMFYNTGI STYVWVLTNR KPAQRKGLVQ LIDASSFWQK
MRKSLGSKRK EMPDSAIEEI TQLFGQCVEA RLATLLDADG KEVARQILRD GEAEPSAPAG
GKVKVAPLSR LLSNQAFGYQ NITVERPLRD EHGTIVIGQK GKQKGKPQPD SSLRDSENVP
LGEDVQAYFK REVLPHAPDA WIDHDKTKVG YEIPFNRHFY VFEPPRPLAE IDAELKGVTD
RILAMIGGLS A
//
