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Database: UniProt
Entry: A0A2K0X2C6_9BIFI
LinkDB: A0A2K0X2C6_9BIFI
Original site: A0A2K0X2C6_9BIFI 
ID   A0A2K0X2C6_9BIFI        Unreviewed;       697 AA.
AC   A0A2K0X2C6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=BFS08_04860 {ECO:0000313|EMBL:PNP88682.1};
OS   Gardnerella sp. KA00735.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Gardnerella.
OX   NCBI_TaxID=1973156 {ECO:0000313|EMBL:PNP88682.1, ECO:0000313|Proteomes:UP000236541};
RN   [1] {ECO:0000313|Proteomes:UP000236541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA00735 {ECO:0000313|Proteomes:UP000236541};
RA   Bumgarner R.E., Fredricks D.N., Srinivasan S.;
RL   Submitted (NOV-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:PNP88682.1}.
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DR   EMBL; NBMV01000002; PNP88682.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K0X2C6; -.
DR   OrthoDB; 9784823at2; -.
DR   Proteomes; UP000236541; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.1660.10; -; 1.
DR   Gene3D; 3.90.220.20; DNA methylase specificity domains; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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; IPR041657; HTH_17.
DR   InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
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; PF12728; HTH_17; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   Pfam; PF12950; TaqI_C; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF116734; DNA methylase specificity domain; 1.
DR   SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          24..70
FT                   /note="Helix-turn-helix"
FT                   /evidence="ECO:0000259|Pfam:PF12728"
FT   DOMAIN          230..463
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   DOMAIN          519..630
FT                   /note="TaqI-like C-terminal specificity"
FT                   /evidence="ECO:0000259|Pfam:PF12950"
SQ   SEQUENCE   697 AA;  79306 MW;  1E9A36A31E0CA01B CRC64;
     MRGLNTFNSE QNLTLDLLET KKTLDVNETA KKLSVSTATI RNWVKLGRIK KINTSGKKLL
     FEEHEVEKLL SDIITGKSDK LTKRRNKKAI KGLNLYADYI EDDGKNILIG SELVKKDSAL
     YTSIHNTLHT DTYPNQDQYP DPYPEKNIRI LIATLALKLY LQSAKLPYIS LQVFIAQNKN
     DCISKLLREL LHNIDISQLG TYQNVPTPTF IPYQDFLGFI YISVSSISYR KSTGSYFTPI
     NIVNKLLDSV KASTQFNNGN IIDLCCGTGN FLLASLKRGA SIERLYGNDI DEISVSIAKL
     NLCINGINNI NTLNEHIRKV DSLLNRDTRK YDLVIGNPPW GYVYSETEIN KLLNSYKTAS
     KKGSESYDLF MELSLNIINQ NGLIAYVLPE AILNVKAHQK IRCFIKNTSS IKFVSYIGNP
     FTGVACPCIL IVLKKDGEGS TIGCNIETNN LRFTINKNRD LSEEYWNFDL SDEDVDCLEK
     LTNVKNGFTL KNQADFALGI VTGANKKYIS NTKNPQNEMI LKGSNLHKYY FDNSNSYIHF
     VPNTFQQVAP IEMYRAKEKL IYRFICEAPV FSYDANQTLS LNSANILIPH VTGISMKYIL
     AILNSRTITY WCRKKYNSVK LLRSHIEEIP FPTPSSEEQN TIVKLVDNLL SLENHCTLDK
     TTLYNEIEEH VMRLYNLNNS EKEIINSFSS QFDSFLK
//
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