ID H5SLT8_9ZZZZ Unreviewed; 282 AA.
AC H5SLT8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
DE Flags: Fragment;
GN ORFNames=HGMM_F47C12C01 {ECO:0000313|EMBL:BAL57124.1};
OS uncultured prokaryote.
OC unclassified sequences; environmental samples.
OX NCBI_TaxID=198431 {ECO:0000313|EMBL:BAL57124.1};
RN [1] {ECO:0000313|EMBL:BAL57124.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT "Genetic and functional properties of uncultivated thermophilic
RT crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT genome fragments.";
RL Environ. Microbiol. 7:1967-1984(2005).
RN [2] {ECO:0000313|EMBL:BAL57124.1}
RP NUCLEOTIDE SEQUENCE.
RA Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S.,
RA Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.;
RT "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA
RT Pathway Dominates a Subsurface Ecosystem.";
RL PLoS ONE 7:e30559-e30559(2012).
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; AP011767; BAL57124.1; -; Genomic_DNA.
DR AlphaFoldDB; H5SLT8; -.
DR REBASE; 46706; M.UbaGMORFIP.
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; IPR029063; SAM-dependent_MTases_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; 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:0000313|EMBL:BAL57124.1};
KW Transferase {ECO:0000313|EMBL:BAL57124.1}.
FT DOMAIN 1..238
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAL57124.1"
SQ SEQUENCE 282 AA; 32192 MW; BF1F940AD836167F CRC64;
RLAKMNLAIR GIDGRIEQGD TFHNDRFPDL KADYILANPP FNMKEWGGER LREDKRWKFG
VPPVRNANFA WVQHIIHHLA PTGYAGFVLA NGSMSSNQSG EGEIRKNIIE ADLVDCMVAL
PDKLFYSTQI PACLWFLARD KSGRPPAGQK KPLRDRRGEV LFIDARRMGR MVDRVHRELT
DEEIQRIGRT YHAWRGEPDA GEYRDVPGFC KSATLAEIRQ HGYVLTPGRY VGAEVQDEDD
EPFEEKMQRL VAELRKQQAE AAKLDEAIWK NLEELGYGNS AS
//
