ID A0A239RQ85_9BACT Unreviewed; 1216 AA.
AC A0A239RQ85;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=SAMN06298210_13110 {ECO:0000313|EMBL:SNU12537.1};
OS Prevotellaceae bacterium KH2P17.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae.
OX NCBI_TaxID=1945886 {ECO:0000313|EMBL:SNU12537.1, ECO:0000313|Proteomes:UP000214740};
RN [1] {ECO:0000313|EMBL:SNU12537.1, ECO:0000313|Proteomes:UP000214740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH2P17 {ECO:0000313|EMBL:SNU12537.1,
RC ECO:0000313|Proteomes:UP000214740};
RA Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL Submitted (JUL-2017) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FZRE01000031; SNU12537.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239RQ85; -.
DR Proteomes; UP000214740; 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; 3.90.220.10; Adenine-n6-DNA-methyltransferase Taqi, Chain A, domain 2; 1.
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; IPR046816; MmeI_Mtase.
DR InterPro; IPR023135; N6_DNA_MeTrfase_TaqI_C.
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; PF20473; MmeI_Mtase; 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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:SNU12537.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000214740};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 534..687
FT /note="MmeI-like DNA-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20473"
FT DOMAIN 825..926
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
FT DOMAIN 1036..1153
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
SQ SEQUENCE 1216 AA; 141215 MW; 3183AF11DC43B676 CRC64;
MAQLTIKQSL NKIYYKQPVV RKDIEQFATA LSVFYHKITA GQIEGNQETH LRDFLKATFY
KDYAISKPED NNIDWAIHLG NSESTNIGII IEAKRTTNET EMISTADLNR KALHELILYF
LIERVEKKND DVRHLIATNM REFFIFDAQL FEQLFYKNKS FLKEFKKFRE GIKTDKSTSH
FYNEIARSYV ETILEKIDYV YFNLESYAKY LGDDKKLKDI LPLYKVFSNI YLLKLPYVND
SNTLNKGFYT ELLHIIGIEE VTKSNKHVIE RKKKDRNAAS LIENVINKLE TDDSLSNYND
KELQTFGADK EEQTFNIALQ LCITWINRIL FLKLLESQLI NYNDGDQNYR FLNADKITDF
DELNRLFFQV LAVDYDKRSE DVTNDYPNVP YLNSSLFEIT DLERKTIKIS SLSQKEKLPV
FANSVLRKQK KYKNVSALPI IAYLFQFLDS YNYGNDKADE IAENNKTLIS ASVLGLIFEK
INGHKDGAVF TPGYISMYMC RQSIRNTVIQ KFNETFNWNC TSITDIYNKD FDIVKANEVI
DSIKICDPAV GSGHFLVSAL NEIVLIKFEL GILVDADGKR IKQQDYAFTI ENDELLVSDS
DNNLFEYHPQ QAESRRIQET LFNEKKKIIE NCLYGVDINP NSVNICRLRL WIELLKNSYY
TAASGYKHLE TLPNIDINIK CGNSLLMKHT LGDNIKQVLA NSNLTIKKYK EDVKAYKTTS
VKANKKEIEK DIQIIKSKIT TGLSDRNPVF KEWAKENREL LTLENDAFGK DDVKFLKKVE
TKRKAVQRLR AQVDDIKENP LYRDAFEWRY EFPEVLDTDG KFEGFDCIIG NPPYGVSFKG
ELRSKIVAQW GHLPDFEIYY YFVELAQFIL KPHGTLGHII PNSWLFNMNA SSFRVNLLNH
WEIKELLDCS QFNIFESVTV RNTVLNMQLS HNGSETVGFR KTNCADKFSE LIEEDLDYIK
KENLLALNQN WGLAFSRKKE VIELVQKINN SYSCVSNLFP EISQGLIAYD KYKGQSKEII
EKRAYHFKEY KDGLKKWLWG QDVTRYNLKW NGQEYIDYCD GIANPREPKF FLGSRLLVRE
ITNPSIYATI VDEEYYNDPS LLIVLDNKQY SLKVLCAILN SSLATFYHFN HSPKATKGAF
PKILIADLKG FPLPQISEQD KETLEAMVDE IMDEKRKGNQ NIVAQLDEKI DNFVLKLYDI
TDEADMAMIK STTEIS
//