ID A0A0F9ZHQ8_9BACT Unreviewed; 795 AA.
AC A0A0F9ZHQ8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, 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};
GN ORFNames=UR28_C0017G0024 {ECO:0000313|EMBL:KKP38376.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWF2_33_10.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619065 {ECO:0000313|EMBL:KKP38376.1, ECO:0000313|Proteomes:UP000034183};
RN [1] {ECO:0000313|EMBL:KKP38376.1, ECO:0000313|Proteomes:UP000034183}
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:KKP38376.1}.
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DR EMBL; LBOP01000017; KKP38376.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9ZHQ8; -.
DR PATRIC; fig|1619065.3.peg.787; -.
DR Proteomes; UP000034183; 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 GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
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 Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 46..111
FT /note="Type I restriction enzyme R protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13588"
FT DOMAIN 339..629
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 795 AA; 94005 MW; C5BDD554D1B671C2 CRC64;
MNYKIVKDYL DKQRIKVVEI YDFENKTVKY SEKIKGWKID KFRGDEEVVR AFVIAKLVNE
LGYKPENIEL EKEYSIGHPN LKKARIDIIV KDNNSNAFLF IELKSPQDFE NEKNKIIEEQ
LFKLASQEKG QGKNVKYLVL YTFELNESEI KDKCILIDYE KFTSFDGWRE IRDFADELPE
RYGKAQKEPF VKSGKKDLEI SFTHEQLDGL RKNLHNVLWG GGGTDDNDVF SSLVNIILAK
IQDESEKKKG EKYDFQICAY ADKKDEEKTN FESNEELFER INELYRRALK QRLNIVDEAK
LKKSFVIDEN KFSLNKLKYT VAELERFSFV DGKNSFNGKD ILGDFFEGII REGFKQTKGQ
FFTHINIVKF LLWGLQIDKL AIERVNKDLE IPYLIDPSAG SGTFLIEYMK FVTENLKRRF
RDKIDDSRDM EEKFDKWFYP DHRENKWAEE YIWGTEINFN LGTATKVNMI LHGDGSSNIF
VKDGLVPFRQ YQRNFGRNWL SQAKEDKSYF NKDVNEVFDV IITNPPFSVD LDNDTKKNVK
NEFIFGDKKN SENLFVERWY QLLKPNGRFG VVLPESVFDT TENKYIRLFI YKYFKVKAVV
SLPQLTFEPF TSTKTSLLFA QKKTKAEIEE WNKLWSKYSN EWNNLKTRCE NLSAVYLDGK
DRKKLPSIKD LIEKEEKEIL ARMLKNYIEE NDKKLSSKEL VEKYKDELKE LCKYDNDTKD
IFGFVNTWWV FGEVAKELNY KIFMAEVENI GYKRTKRGEK PMPNELYRVN DKSEVLVDDG
VKETALDYLR NVLWD
//
