ID A0A2S4HJY4_9GAMM Unreviewed; 549 AA.
AC A0A2S4HJY4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=C0068_03055 {ECO:0000313|EMBL:POP54259.1};
OS Marortus luteolus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; Marortus.
OX NCBI_TaxID=2067667 {ECO:0000313|EMBL:POP54259.1, ECO:0000313|Proteomes:UP000237222};
RN [1] {ECO:0000313|EMBL:POP54259.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZX-21 {ECO:0000313|EMBL:POP54259.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-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:POP54259.1}.
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DR EMBL; PQGG01000007; POP54259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4HJY4; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000237222; 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 M PROTEIN; 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:0000313|EMBL:POP54259.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000313|EMBL:POP54259.1}.
FT DOMAIN 7..122
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 132..421
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 549 AA; 60923 MW; 28CCE1E6C0377248 CRC64;
MTNNDIVQKL WNLCDVLRDD GINYSDYVTE LVMLLFMKMV HENTESDLLK THILPEGCRW
TDLSSKSGLN LLDDYKRILL ALSSGKDANG KQVHNDLLIS AVYADAQTRL REPRHLEQLV
KALDQIDWYS AQQDGLGDLY EGLLEKNASE TKSGAGQYFT PRALINSMVR CIQPQAGETV
QDPAAGTAGF LIAADAYIKQ HTDDLFDLPA KDQKFQRNNA FLGVELVPST RRMALMNCLL
HGMEGDDEGV VHLGNALGMV GANLAKADII LANPPFGTSK GGDASITRDD LTYKTSNKQL
AFLQHIYRNL KPGGRAAVVL PDNVLFEAGV GNEVRRDLMN KCNLHTILRL PTGIFYAQGV
KTNVLFFTKG HPKDKLQDEN CTANVWVYDL RTNMPSFGKR TPFTEEHLKP FEDCYFAKNK
KATAKDGGSV ENAGAIFDRM EGDYSFNAKE ADTTEEAGSN DDLAKSRWRV FSRDWIRDSK
GDSLDISWLK DKDSVDAANL PEPEVLAAEA MSELTEALRE MDGLMQALGA GDEAAVQRML
VHEILCESK
//