ID A0A395JM77_9GAMM Unreviewed; 484 AA.
AC A0A395JM77;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=DFR28_102180 {ECO:0000313|EMBL:RBP50768.1};
OS Arenicella xantha.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Arenicellales;
OC Arenicellaceae; Arenicella.
OX NCBI_TaxID=644221 {ECO:0000313|EMBL:RBP50768.1, ECO:0000313|Proteomes:UP000253083};
RN [1] {ECO:0000313|EMBL:RBP50768.1, ECO:0000313|Proteomes:UP000253083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24032 {ECO:0000313|EMBL:RBP50768.1,
RC ECO:0000313|Proteomes:UP000253083};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUN-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:RBP50768.1}.
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DR EMBL; QNRT01000002; RBP50768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395JM77; -.
DR InParanoid; A0A395JM77; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000253083; 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:UP000253083};
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..142
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 153..451
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 484 AA; 54806 MW; D8FEDE8E0CCC6E62 CRC64;
MFEQVFKNID DILHKDAGCS SELDYTEQTS WMLFLKYLDD LEREKALAAE LMEQEYSHII
DPEHRWNTWA APKDAEGNFD HNEALTGDDL MEYVDNELFP YLKSFKQRAT SPDTIEYKIG
EIFGEIKNKI QSGYSLRDAL EKIDELRFRS QEEKHELSHL YETKIKNMGN AGRNGGEYYT
PRPLIRAMIA VVNPQIGETV YDGAAGSAGF LCETYDVLRQ REGLSSTDLK ILQESTFYAQ
EKKSLAYVIA IMNMILHGIE APNVIHTNTL GENIADIQDS NRHDIILANP PFGGKERPEI
QQNFTIKTGE TAFLFLQHFI KKLRPGGRAA VVIKNTFLSN TDNAAVALRK ELLENCNLHS
VLDCPGGTFI GAGVKTVVLF FEKGAPTQKV WFYQLDVGRN MGKTNPLNDN DLKGFVALQK
TFADSDQSWS VDVSEIDQST WDLSVKNPNK NDEVIFREPA VIIEEIMALD KESEVILGNI
RELL
//
