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Database: UniProt
Entry: A0A1I2GNF6_9BACT
LinkDB: A0A1I2GNF6_9BACT
Original site: A0A1I2GNF6_9BACT 
ID   A0A1I2GNF6_9BACT        Unreviewed;      1254 AA.
AC   A0A1I2GNF6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=SAMN04488541_101985 {ECO:0000313|EMBL:SFF19494.1};
OS   Thermoflexibacter ruber.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Thermoflexibacteraceae;
OC   Thermoflexibacter.
OX   NCBI_TaxID=1003 {ECO:0000313|EMBL:SFF19494.1, ECO:0000313|Proteomes:UP000199513};
RN   [1] {ECO:0000313|EMBL:SFF19494.1, ECO:0000313|Proteomes:UP000199513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GEY, DSM 9560 {ECO:0000313|Proteomes:UP000199513};
RA   de Groot N.N.;
RL   Submitted (OCT-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   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594}.
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DR   EMBL; FONY01000019; SFF19494.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2GNF6; -.
DR   STRING; 1003.SAMN04488541_101985; -.
DR   OrthoDB; 32195at2; -.
DR   Proteomes; UP000199513; 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   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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:SFF19494.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199513};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          864..971
FT                   /note="Type II methyltransferase M.TaqI-like"
FT                   /evidence="ECO:0000259|Pfam:PF07669"
FT   DOMAIN          1078..1195
FT                   /note="TaqI-like C-terminal specificity"
FT                   /evidence="ECO:0000259|Pfam:PF12950"
FT   COILED          807..838
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1254 AA;  145423 MW;  20B9EC9F238ADCF7 CRC64;
     MILKELTPRK ALNKAFLKLK PSRTEIDNFK TNLITLLERV NDTESEEFHK NLLIDFLKKT
     YYDPHHFLNT KGRNDLVIHN GSTAKSPVGV IIEAKKPSNK VEMLTRDNIN KKAFQELILY
     YLRERVTHKN LEIKHLAATN IYEWFIFDAM LLDRLFAQNK NLVKLFNDFE AGRLADTKTD
     FFYKQVAEPF IGEISAEIEF TYFSFPRVNS GAIDDNDLIP LFKILSPEHL LKLPFANDSN
     SLDKRFYSEL LHIIGLTEIK EGNKKLIERN KAGERHTGTI LENAVIQLDS LDKMSRLEKP
     SQFGKTEQER LFNVALELSI TWVNRILFLK LLEAQLITYH KGDASYSFLH SDKIKSYDDL
     NSLFFQVLAR QHDERNEEVK KIFEKVPYLN SSLFEPTDTE QQTIFISNLK DNINIPIFSQ
     TVLKDPQGKK RTGKLNTLQY FLEFLDAYNF GAEGSEEIQE DNKTLINASV LGLIFEKING
     YKDGSFFTPG FITMYMCRET IRRAVVQKFK EAGYQLSESL ELSRSLTEIY NQIKDIKEAN
     KIVNTLKICD PAAGSGHFLV SALNEIIAIK NDLGILCDFE GRPLKNYWVE VVNDELFITE
     KETGEEFCYI APMPRTEKAI KHTFGGDTSN YKASQLPERQ VVQQSLFKEK QAIIENCLFG
     VDINPNSVKI CRLRLWIELL KNAYYSPESN FTELETFPNI DINIKCGNSL VSRFAIDADL
     SKSLRSLKWD IKTYRQLVQS YLHATDKEAK RGFEKLINDI KKDFSIQISN SDPKKTRLSK
     LAYELYNRFT GMMLFEPEVP YGDNKSDKNL EAKRKEEQGK IEEEMEKLRR EIDEIENNKI
     FENAFEWRFE FPEVLNDDGD FVGFDVVIGN PPYGVSIKEK TEREYLVSNL SKVPDYEIYY
     WFINKGHHIL KQNGIISYII PNTILFNVFA QSYRLSLFDN WTINEILDCT NFNIFEDATV
     RNIIFQFIKS DSKKNTLGYK NTANIENFEN LISCKTLTIS KEIAVSNIQN WGLVFKLDRE
     TLNVVEKIRS EKKPLIELFP ETSQGLIAYD KYQGQNAEII KNRAYHHFSN PNNKFKRWLY
     GGDITRYSVK WNGKEFIDYC DGIANPREPK YFKGKRLLIR EITNPRIFSA ITTEELYNDP
     AIIIVKENPK SYPIECLLGI FNSKLATFYH FNSSPKATKG AFPKILVYDV NNFPLPKTID
     KVTQEKIENL VNQILTKKAE DNSNDTADLE NQIDQLVYEL YGLTEAEIKM IEQS
//
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