ID A0A1M4TMQ4_9BACT Unreviewed; 492 AA.
AC A0A1M4TMQ4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-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=SAMN05444008_101442 {ECO:0000313|EMBL:SHE45557.1};
OS Cnuella takakiae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Cnuella.
OX NCBI_TaxID=1302690 {ECO:0000313|EMBL:SHE45557.1, ECO:0000313|Proteomes:UP000184368};
RN [1] {ECO:0000313|EMBL:SHE45557.1, ECO:0000313|Proteomes:UP000184368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26897 {ECO:0000313|EMBL:SHE45557.1,
RC ECO:0000313|Proteomes:UP000184368};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
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DR EMBL; FQUO01000001; SHE45557.1; -; Genomic_DNA.
DR RefSeq; WP_073039428.1; NZ_MTFE01000010.1.
DR AlphaFoldDB; A0A1M4TMQ4; -.
DR STRING; 1302690.BUE76_01755; -.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000184368; 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 Reference proteome {ECO:0000313|Proteomes:UP000184368};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..113
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 123..411
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 492 AA; 56104 MW; 7FE33EEEF7047345 CRC64;
MSTNQIISKV WSFCNTLRDD GVSYGDYLEQ LTYLLFLKMA HEYTKPPYNR TLPIPPEYGW
QSLTVLKGAE LEGHYTTMLR ELGKGKGILG QIFTKSQNKI QDPAKLYKLV QLIDAENWTL
MDADVKGDIY EGLLEKNAED TKSGAGQYFT PRPLISAMVA CVRPEPLKTI ADPACGTGGF
FLSAYDFITH NHSLDKEAKR FLKFNTFWGN EIVAGTRRLA LMNLFLHNIG DIDSDNSISP
ADALIAPPAQ RYDYVLANPP FGKKSSQTFT NEAGEQEKED LTYNRQDFWA TTSNKQLNFV
QHIRAMLKPT GQAAVVLPDN VLFEGGAGET VRKRLLETTD VHTILRLPTG IFYANGVKAN
VVFFDNKPSS KEHQTREIWF YDYRTNVHHT LKKNPLRLEH LQDFVTCYNP ANRHQRTETW
HPTNNPEGRW RKYPYEEIIT RDKTSLDITW LKDKSLADLD NLPDPDELAE EIVENLESAL
EGFRAIIAQL KK
//
