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Database: UniProt
Entry: A0A1B6Y7L1_9BACT
LinkDB: A0A1B6Y7L1_9BACT
Original site: A0A1B6Y7L1_9BACT 
ID   A0A1B6Y7L1_9BACT        Unreviewed;       527 AA.
AC   A0A1B6Y7L1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, 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};
GN   ORFNames=A8B79_05975 {ECO:0000313|EMBL:OAN61021.1};
OS   Balneola sp. EhC07.
OC   Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Balneola.
OX   NCBI_TaxID=1849360 {ECO:0000313|EMBL:OAN61021.1, ECO:0000313|Proteomes:UP000078514};
RN   [1] {ECO:0000313|EMBL:OAN61021.1, ECO:0000313|Proteomes:UP000078514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EhC08 {ECO:0000313|EMBL:OAN61021.1,
RC   ECO:0000313|Proteomes:UP000078514};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) 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};
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:OAN61021.1}.
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DR   EMBL; LXYG01000017; OAN61021.1; -; Genomic_DNA.
DR   RefSeq; WP_066221392.1; NZ_LXYG01000017.1.
DR   AlphaFoldDB; A0A1B6Y7L1; -.
DR   STRING; 1849360.A8B79_05975; -.
DR   REBASE; 159505; M.BspC07ORF5975P.
DR   InParanoid; A0A1B6Y7L1; -.
DR   OrthoDB; 9814572at2; -.
DR   Proteomes; UP000078514; 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; 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; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
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; 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   ECO:0000313|EMBL:OAN61021.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078514};
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:OAN61021.1}.
FT   DOMAIN          6..114
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          158..492
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   527 AA;  61172 MW;  725F9DE9EDC66CB9 CRC64;
     MLSKELKSKI DNLWDKFWSR GMANPLQAIE HISYLLFMRR LEQMDAEESK RSSYKSIFEG
     TWDTGKKDSE GDSITVEKRM LRWTVFKDFE TEERLTHVSQ YVFPFLKDLK EENSPYARHM
     QSANFFMPSA LLLEDAMRAI DEIFDYIEND KKAGQAFQDT QGDVYEYLLS ELKNAGKNGQ
     FRTPRHLIRF LVEILDPDIG DKICDPAAGT GGFLVAAYQY ILAKKSSEKK KIKDDDGFYN
     GLGNKIKDEK HWNQLKKETF YGYDIDSGMV RIGLMNLMLH GISYPHIENQ DTLSKKYDDD
     HKEGEFSMVL ANPPFTGKIS KNDKSDEFRI SSNSTELLFL ERIIKMLQPG GKGGVIIPEG
     VLFGSSKANR QLREIMAKDC QLEAVISLPS GVFKPYTGVK TAILVFTKAQ QDSNEFHTEK
     VWFYELKSDG YSLDDNRRRL KDSPLPQAVT DWEEREEKSS ENERKGQHFF VRLEEIQKND
     YDLSFNRYKE FVYEEQDYDS PKEILESLMA LENQILKEME ELRNLVG
//
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