ID A0A101IHX6_9EURY Unreviewed; 587 AA.
AC A0A101IHX6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=XE07_1739 {ECO:0000313|EMBL:KUK95541.1};
OS Methanothrix harundinacea.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=301375 {ECO:0000313|EMBL:KUK95541.1, ECO:0000313|Proteomes:UP000053961};
RN [1] {ECO:0000313|Proteomes:UP000053961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK95541.1}.
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DR EMBL; LGHB01000032; KUK95541.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101IHX6; -.
DR PATRIC; fig|301375.6.peg.944; -.
DR Proteomes; UP000053961; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025931; TaqI_C.
DR PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF07669; Eco57I; 1.
DR Pfam; PF12950; TaqI_C; 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 Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 36..136
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
FT DOMAIN 244..401
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KUK95541.1"
SQ SEQUENCE 587 AA; 67020 MW; 5CE0638687382FF7 CRC64;
REAQRIAEDR SFFHWQLEFP EVFFAGGAVK ESPGWDAVVG NPPYVRQEGL GEFKGYFAEK
YRVYHGVADL YVYFVEQGVS LVQKDGFFSY ILPNKWMRAN YGSSLRSWMK GRCIDEIVDF
GDLPVFPEAT TYPCILRLCG GPAKPSFKAA EVESLDFGRL TDYVEVNAYS VSLSGLEDSG
WSLVDESVQR LLEKLRRAGT PLGEYVGGKI YRGILTGLNE AFVIDEGTRA RLIREDPKSA
ELIKPFLAGR DIKRYEPPVS DNYLILIPNG WTRAQSSGAE DPWSWFEARY PAVAAHMVQF
SEAAQKRYDK GEYWWELRAC DYYDQFEKPK IMYLVFQVKP AFTFDEAGTY GNNAIWITPG
EDLYLLSILN SRLGWLLISN YCTEIQNGYQ LIFKYLGKIP IRRISFSTPE DERRRLAEEL
KGLCAAGQFE KVLEVVGDCL PKDDASEFVA EGERSDVVHD LLAHLAEEMI RMNKEKQEEI
RGFLAWLEEF AGAKVDDLTN KTKVSAYYEI EFSELLSIMK KNKRKLPCDP NRRAFSEDLR
REFSASMEKL SPLLLRIGET DRLIDAVVYK LYGLSEAEIA IVEGSLS
//
