ID A0A399FU95_9ACTN Unreviewed; 544 AA.
AC A0A399FU95;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=NI17_010265 {ECO:0000313|EMBL:UOE21453.1}, NI17_22590
GN {ECO:0000313|EMBL:RIH99643.1};
OS Thermobifida halotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=483545 {ECO:0000313|EMBL:RIH99643.1};
RN [1] {ECO:0000313|EMBL:RIH99643.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44931 {ECO:0000313|EMBL:RIH99643.1};
RA Toth A., Tancsics T.A., Farkas T., Papp P., Olasz F., Balint B.,
RA Herczeg R., Nagy I., Baka E., Kukolya J.;
RT "De novo genome project of the cellulose decomposer Thermobifida
RT halotolerans type strain.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:UOE21453.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44931 {ECO:0000313|EMBL:UOE21453.1};
RA Nagy I., Horvath B., Kukolya J., Nagy I., Orsini M.;
RT "De novo genome project of the cellulose decomposer Thermobifida
RT halotolerans type strain.";
RL Submitted (OCT-2020) 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};
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DR EMBL; JRUV01000309; RIH99643.1; -; Genomic_DNA.
DR EMBL; CP063196; UOE21453.1; -; Genomic_DNA.
DR RefSeq; WP_068693697.1; NZ_LIZN01000028.1.
DR AlphaFoldDB; A0A399FU95; -.
DR STRING; 483545.GCA_001660385_02746; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000265719; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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; 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDI METHYLASE SUBUNIT; 1.
DR PANTHER; PTHR42998; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 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.
PE 4: Predicted;
KW Endonuclease {ECO:0000313|EMBL:RIH99643.1};
KW Hydrolase {ECO:0000313|EMBL:RIH99643.1};
KW Methyltransferase {ECO:0000313|EMBL:UOE21453.1};
KW Nuclease {ECO:0000313|EMBL:RIH99643.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000265719};
KW Transferase {ECO:0000313|EMBL:UOE21453.1}.
FT DOMAIN 24..162
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 176..503
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 544 AA; 60844 MW; 66B1577275E021D4 CRC64;
MPPRKRATAG QGELPGISST KEIQDILWKA ADKLRGSMDA AQYKEFVLGL VFLKYVSDAF
AERRTQLAAD PELAEIPEHR RTAFLEDKDE YTEQNVFWVP PTARWDYIAA NAASAEGGVG
KLLDDAMDEV MKANKVLTGV LPKIFNRDNV DQNRLKDLVD LISDARFTGH GDRPAQDVLG
EVYEYFLERF ARAEGKRAGE FYTPASVVKL LVEVLEPYEG RVYDPCCGSG GMFVQSGKFV
ERRRGRDHTH DIAIYGQEAN ERTWRLAKMN LAIHGMDPKG IGDRWADTFA DDKLPDLRAD
FVMANPPFNM SVWERKTDDP RWKFGVPPQS NANYAWLQHI VSKLGDRGSA GVVLSNGSMS
SKQSGEGEIR AALVEADLVA CMVALPGNLF RTTAIPACLW FLTKDKTPQG ANALTDRRGE
VLFIDARTMG TMVDRTERVF TDEDLAKISD TYHAWRGTKS ARDKKLSYED VPGFCYSATL
QEIAKHDHVL TPGRYVGAAE PEEDPNAEPV EERIARLTKE LFAHFDESAR LEAVVREQLG
RIDG
//
