ID A0A0G0N0I8_9BACT Unreviewed; 561 AA.
AC A0A0G0N0I8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=UT36_C0003G0058 {ECO:0000313|EMBL:KKR08938.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWF2_39_17.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619067 {ECO:0000313|EMBL:KKR08938.1, ECO:0000313|Proteomes:UP000034818};
RN [1] {ECO:0000313|EMBL:KKR08938.1, ECO:0000313|Proteomes:UP000034818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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 -!- 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:KKR08938.1}.
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DR EMBL; LBWM01000003; KKR08938.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0N0I8; -.
DR STRING; 1619067.UT36_C0003G0058; -.
DR PATRIC; fig|1619067.4.peg.371; -.
DR Proteomes; UP000034818; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd04761; HTH_MerR-SF; 1.
DR Gene3D; 1.10.1660.10; -; 1.
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; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR000551; MerR-type_HTH_dom.
DR InterPro; IPR004546; Restrct_endonuc_T1M.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR NCBIfam; TIGR00497; hsdM; 1.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR Pfam; PF12161; HsdM_N; 1.
DR Pfam; PF13411; MerR_1; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SMART; SM00422; HTH_MERR; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50937; HTH_MERR_2; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KKR08938.1};
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:KKR08938.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 423..447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..62
FT /note="HTH merR-type"
FT /evidence="ECO:0000259|PROSITE:PS50937"
SQ SEQUENCE 561 AA; 65518 MW; 0CFB4946F126C37B CRC64;
MKREIEKKLK EMPDLLSISE VSEIFGIHQD TLRNWEKKGL LVPLRIGDRQ DRRYRPADIE
TITAKMGSRL TLQQLEQFLW KSADILRGKI DSSDYKKYIF GLLFYKRISD VWDEEYQKVM
DEFNDKNLAK ADYNHRFQVP EDCKWIVIEQ QADNIGQKLN ENFAKLTNAN SPKLDRIFDD
LDFANKHKFP NDTLQRLINH FSQYNFGSNY INSDLLGDAY EYLIKQFAAD AGKKGGEFYT
PREIERVIIN ILKPHEKNHI YDPTVGSGGF LLESYLHLRE KTDEKIANTL YLYGQEINLG
TFAIAKINMF LHGLDAADIR RGDTLQDPQF LDDFGALKQF DIVVANPPYS IKDWPYEFFK
TNRYGRLTGY DMPPNKNADY VFILHIIKSM KENGRAGVVL PHGVLFRGGS EGRIREQILK
NDLIEAIIAM PSKLFYGVGI PVCILIFNRN KPENKKNKLI FIDAEKDYAE GKNQNSLRKK
DIDKIVSAYD DYKDIEKFAR IVDLKEIEKN EFNLNVRRYI ENGEEEEEIN VSEVWGELKE
LEKERSQIDK EVEGYLKELK Y
//
