ID W2DXM8_9PSED Unreviewed; 489 AA.
AC W2DXM8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=H096_07242 {ECO:0000313|EMBL:ETK24094.1};
OS Pseudomonas sp. FH1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1284392 {ECO:0000313|EMBL:ETK24094.1, ECO:0000313|Proteomes:UP000018863};
RN [1] {ECO:0000313|EMBL:ETK24094.1, ECO:0000313|Proteomes:UP000018863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FH1 {ECO:0000313|EMBL:ETK24094.1,
RC ECO:0000313|Proteomes:UP000018863};
RX PubMed=24286439; DOI=10.1111/1462-2920.12345;
RA Rhodes G., Bosma H., Studholme D., Arnold D.L., Jackson R.W., Pickup R.W.;
RT "The rulB gene of plasmid pWW0 is a hotspot for the site-specific insertion
RT of integron-like elements found in the chromosomes of environmental
RT Pseudomonas fluorescens group bacteria.";
RL Environ. Microbiol. 16:2374-2388(2014).
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:ETK24094.1}.
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DR EMBL; AOHM01000019; ETK24094.1; -; Genomic_DNA.
DR RefSeq; WP_033897472.1; NZ_AOHM01000019.1.
DR AlphaFoldDB; W2DXM8; -.
DR PATRIC; fig|1284392.3.peg.1428; -.
DR Proteomes; UP000018863; 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 Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..129
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 140..454
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 489 AA; 55856 MW; 0921B510D3838EEA CRC64;
MSISSTIKSI QDIMRKDVGV DGDAQRIGQL VWLLFLKIFD DRELEWELMD DNYRSPIPDS
CRWRTWAADP EGMTGDALKD FIDNNLFPQL QNLDEYSNTP SAFVVRSVFE DAYNYMKSGQ
LLRQVINKVQ EGVDFNKAQE RHEFGNLYEQ LLRDLQNAGN AGEFYTPRPV TEFMVRMVDP
KLEEKVMDPA CGTGGFLTCA IEHKRSRYVK TAEDERTLQA SIFGVEKKPL PHLLATTNMI
LHGIEVPSQI KHDNTLSKPL ISWGPSERVH CIVANPPFGG MEEDGIETNF PAAFRTRETA
DLFLVLIVHL LKDGGRAAVV LPDGFLFGDG IKSRIKEKLL TECNLHTIVR LPKGVFNPYT
GIKTNLLFFT KGTPTKQVWF YEHQYPAGVK NYSKTRPMRI EEFVLEQDWW GNEDDGFTAR
VEGEFAWKVS VEELKARNWN LDCKNPHIGE QISHDPDKLL RNYATLQGEI SELRDQLKAV
LAEALEHQV
//
