ID A0A2N3IBL5_9BACT Unreviewed; 541 AA.
AC A0A2N3IBL5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-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=Rain11_1940 {ECO:0000313|EMBL:PKQ67665.1};
OS Raineya orbicola.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Raineyaceae; Raineya.
OX NCBI_TaxID=2016530 {ECO:0000313|EMBL:PKQ67665.1, ECO:0000313|Proteomes:UP000233387};
RN [1] {ECO:0000313|EMBL:PKQ67665.1, ECO:0000313|Proteomes:UP000233387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPSPC-11 {ECO:0000313|EMBL:PKQ67665.1,
RC ECO:0000313|Proteomes:UP000233387};
RA Albuquerque L., Polonia A.R.M., Barroso C., Froufe H.J.C., Lage O.,
RA Lobo-Da-Cunha A., Egas C., Da Costa M.S.;
RT "Raineya orbicola gen. nov., sp. nov. a slightly thermophilic bacterium of
RT the phylum Bacteroidetes and the description of Raineyaceae fam. nov.";
RL Submitted (JUN-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 -!- 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:PKQ67665.1}.
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DR EMBL; NKXO01000031; PKQ67665.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3IBL5; -.
DR OrthoDB; 32195at2; -.
DR Proteomes; UP000233387; 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; 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; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR023135; N6_DNA_MeTrfase_TaqI_C.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025931; TaqI_C.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR PANTHER; PTHR33841:SF1; DNA METHYLTRANSFERASE YEEA-RELATED; 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 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:PKQ67665.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000233387};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PKQ67665.1}.
FT DOMAIN 95..347
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT DOMAIN 395..507
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
SQ SEQUENCE 541 AA; 62274 MW; D42E9F28528B21D3 CRC64;
MQTNIFGEVE LKKLTLEQAA RKAKVSTATI RNWIKAGYLA VVGKSLISQD SLEIFLSEVV
GKEKLNARAN KLSKDKNIYT IAKDINFIIQ NKQGESMGKE YENSLSDSYR NKEGIYYTPS
WVVQDMFKGI KIQQNFTFLD PCCGSGNFIV EAIRQGIRPE NVYGFDTDEN AVLITKQRIK
EEFGYEATNI RVADFLQEAH SLSREKISFD LIFTNPPWGK KIEKNKKEIY ASMFECGNSL
DTTSLFLGAS LLLLKPNGCL GFLTQEAFFN IANFEDIRRK VLTKKILRLV DYGKVFKGLL
TKAQAIILEN SPSDNNNLIE CCNEDKNFQR TQKSFTITPK KIFNFWITEQ EAHLIEHLYA
ITHITLKNRA VWALGIVTGN NKKFCTNQPQ EGYIPIYKGS DITKKGLKRP TTYILNDFSK
FQQVAPLELY QAPEKIIYRF ISTDLCFYCD TEQSYILNSA NLFIPKDMPI NARQLTELLN
SEMINWLFKK MFATHKILRG DLELLPIHYE YFSKYSVFSE KSYLDYLQIA KTPNGTYQLK
K
//