ID Q8DPM0_STRR6 Unreviewed; 625 AA.
AC Q8DPM0;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 111.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=spr1102 {ECO:0000313|EMBL:AAK99905.1};
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101 {ECO:0000313|EMBL:AAK99905.1, ECO:0000313|Proteomes:UP000000586};
RN [1] {ECO:0000313|EMBL:AAK99905.1, ECO:0000313|Proteomes:UP000000586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6 {ECO:0000313|Proteomes:UP000000586};
RX PubMed=11544234; DOI=10.1128/JB.183.19.5709-5717.2001;
RA Hoskins J.A., Alborn W.Jr., Arnold J., Blaszczak L., Burgett S.,
RA DeHoff B.S., Estrem S., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A., LaGace R., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S., McHenney M.,
RA McLeaster K., Mundy C., Nicas T.I., Norris F.H., O'Gara M., Peery R.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C., Baltz R.H., Jaskunas S.Richard.,
RA Rosteck P.R.Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
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};
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DR EMBL; AE007317; AAK99905.1; -; Genomic_DNA.
DR PIR; E98009; E98009.
DR PIR; G95141; G95141.
DR RefSeq; NP_358695.1; NC_003098.1.
DR AlphaFoldDB; Q8DPM0; -.
DR STRING; 171101.spr1102; -.
DR REBASE; 5624; SpnRII.
DR KEGG; spr:spr1102; -.
DR PATRIC; fig|171101.6.peg.1197; -.
DR eggNOG; COG0286; Bacteria.
DR eggNOG; COG1002; Bacteria.
DR HOGENOM; CLU_456257_0_0_9; -.
DR OMA; WATHSYN; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 Pfam; PF07669; Eco57I; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AAK99905.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000586};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 289..385
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
SQ SEQUENCE 625 AA; 71869 MW; 3A36917CFA15A218 CRC64;
MLMTIDISEE SLAKESADLL KILLKDRTTK KSIVWATHSY ELLGKGFAPS DRINPSKVTG
NFANLIQPRS EKSKYEQKDR TKIRAEVFTP TWLVAKQNGY VESKLGSLSL EEYVDLRWLE
VTCGEAPYMV TRYDTVTGEE IPLSERVGFV DRKLQRISRE VSDEVTFYKL VKDAYHASYG
YEYQGDSLLL ARENLLATFE DYYLAKTGNQ PTLEQKKEIA TIISYNVFQM DGLKKSSPYS
AKQKQSQQLS LFADELEVQE VEESKTHIKD WKKNRMIGFE RLSSEESEMK FDVVIGNPPY
QETGEARDEP IYHYFIDEAY KIADKSILIT PARFLFKAGQ TPKNWMEKML EDKHLKVQFY
ELKSGKVFTG TDIKGGVAIT YRDVDKDLGP IGVFTIFETL NGIVKKIEKH PEFETFSDLV
YPQGIYRFSN KLFSDYPNAE KLQGKGTKNK IVSKSLTQLD FVFKNNEEKD HVALLGRIGS
ERVYRYINKK YLDLPETFEN YNVFVPEANG SGALGEVLST PLIGEPLIGH TDTFLSIGNF
KTKFEADACI KFIKTKFARV LLGVLKVTQH NSRKTWYYVP LQDFTVNSDI DWTQSVTDID
RQLDQKYDLS PEEIAFIENH VREMD
//