ID A0A1U7M541_TISCR Unreviewed; 817 AA.
AC A0A1U7M541;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=TICRE_15790 {ECO:0000313|EMBL:OLS02427.1};
OS Tissierella creatinophila DSM 6911.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Tissierellaceae;
OC Tissierella.
OX NCBI_TaxID=1123403 {ECO:0000313|EMBL:OLS02427.1, ECO:0000313|Proteomes:UP000186112};
RN [1] {ECO:0000313|EMBL:OLS02427.1, ECO:0000313|Proteomes:UP000186112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6911 {ECO:0000313|EMBL:OLS02427.1,
RC ECO:0000313|Proteomes:UP000186112};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Tissierella creatinophila DSM 6911.";
RL Submitted (FEB-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 -!- 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:OLS02427.1}.
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DR EMBL; LTDM01000028; OLS02427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U7M541; -.
DR REBASE; 193717; M.Tcr6911ORF15790P.
DR Proteomes; UP000186112; 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029464; HSDR_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR Pfam; PF13588; HSDR_N_2; 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 ECO:0000313|EMBL:OLS02427.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186112};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OLS02427.1}.
FT DOMAIN 52..117
FT /note="Type I restriction enzyme R protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13588"
FT DOMAIN 343..681
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 817 AA; 95650 MW; 0AE92532D9D36B3D CRC64;
MEITKKQKEI INAYIEQSKI KAVESIDFVN KKVKYSNEIL NARNIDVLSG DEEIVRAYII
TKLANELGYP LNKIVIEYEY TAGRPHTITS RIDLIVKDKN DDAFLFIELK PPKQYETLDK
DSTIEEQLFK VAGMEKNEGH NVKYLVLYTI NFDNLNNIKD TCMIIDNEKY PNFAQWESVR
NYTDTLPDRY SKVIKKPYIK NSDNDLEKSF THEMLHRLQI DLHNVLWGGG GTDDNEIFSS
LTNLILAKIQ DEDEKMNGDA YDFQALSFVN DEDEFESNDV LFERINELYK RALSNKLNIV
DKNELKKSYV IDTKKFSLSK LKYTVQQLEK YSFVDGKNSL SGKDILGDFF EGIIRNGFKQ
DKGQFFTHIN IVKFMLWGIQ ADRLAIDRIN KDKEIPYMID PSAGSGTFLI EYMKFITENI
KYKYRSQINS SREVTDKMES EWFYPNHREN KWAREYIYGT ELNFNLGTAT KVNMILHGDG
STNIFVKDGL LPFNEYVKEN APNALNKAFK DNLYKYETNS QFDLILTNPP FSVDLDKDTA
KRVKKNFIFG NKKNSENLFI ERYYQLLREN GRMAIILPES IFDTNENRYI RLFLYKYFNI
KAIVSLPQST FAPFTNTKTS IIFAQKKTSE QIELWDSKWN IYTNEWSKLK NRVLNIIDVH
HSVKSKEKLP SIKSLSQLEE IHILAQMLKN NLTIEDSNDI FSFCEDSAES DVLEFKESLI
KKYEEDLISL CKVDNDTKAE FGFVNTWWVF SNVANELSYN IFMAEADEIG YKRTIRGERK
SLNNLFRSDS NDKLIIDDGN KETILDYMRD IEWDEER
//