ID A0A379ND59_9BACT Unreviewed; 736 AA.
AC A0A379ND59;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=NCTC11190_02440 {ECO:0000313|EMBL:SUE45230.1};
OS Rikenella microfusus.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Rikenella.
OX NCBI_TaxID=28139 {ECO:0000313|EMBL:SUE45230.1, ECO:0000313|Proteomes:UP000255233};
RN [1] {ECO:0000313|EMBL:SUE45230.1, ECO:0000313|Proteomes:UP000255233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC11190 {ECO:0000313|EMBL:SUE45230.1,
RC ECO:0000313|Proteomes:UP000255233};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; UGVL01000003; SUE45230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A379ND59; -.
DR REBASE; 415824; Rmi11190ORF2440P.
DR Proteomes; UP000255233; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; 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 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; 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; PF02384; N6_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 Hydrolase {ECO:0000313|EMBL:SUE45230.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000255233};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 22..168
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT DOMAIN 300..411
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
FT DOMAIN 516..671
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
SQ SEQUENCE 736 AA; 85369 MW; 8AE2EB164AC8E32B CRC64;
MQRYNFTIEE STPQEQQVAL DPELLGKVFE NLLGVYNPET QETARNQSGS FYTPREIVEY
MVDESLIAYL GDTPELRTLF SEDFDPTKIP DSNRKEWAAK LKTVKILDPA CGSGAFPMGL
LNRIVDLLHK LDLDEDTYRL KLELIENCIY GVDIQSIATQ ISKLRFFISL ICDCEKDPTK
PNYGIPTLPN LETKFVCADS LIGKKKKEQQ LNLFDNEDID QIKNELLQIR HDHFRADSAA
KKKRLRTQDE RLREQLADRL SNHSFDREDA RQIAEWNPYD QNSVSPFFDP EWMFGLSDGF
DIVIGNPPYI PLQNNSGLLA KRYEHCAYMT FARTGDIYCL FYERGLQMLK NNGILCCITS
NKWMRAGYGE KIRSFFARQS NPKLLIDFAG IKVFESATVD TNILLCSKEE NAKATLCAIM
NKTGHKNLSL FVQQQGVRCA FSSSDSWVIL SPIEQSIKRK IEAVGTPLKD WDIQINYGIK
TGFNDAFIIS TEKRDEILAN CRTEEERERT AELIRPILRG RDIKRYGYEW AKKYLIATFP
SRHYDIEQYP ALKQYLLSFG KERLEQTGKT YTIHGEKIKA RKKTNNKWFE TQDSISYWED
FMRPKVMWKI IGCNINFCYD EKQYICNNAV DIMVGDKSRL IQFVGLMNSK LFDWYLKLTT
EAEVQGGGIQ LYVTTLEKTL MKLDFSDSLT NTIYQRISGL IDDKVVDDKI FDAYLLTQEE
RMFILNDKRV TRNRET
//
