ID E9FJU0_9STRE Unreviewed; 625 AA.
AC E9FJU0;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=HMPREF0851_00546 {ECO:0000313|EMBL:EFX59570.1};
OS Streptococcus sp. M334.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=563038 {ECO:0000313|EMBL:EFX59570.1, ECO:0000313|Proteomes:UP000003840};
RN [1] {ECO:0000313|EMBL:EFX59570.1, ECO:0000313|Proteomes:UP000003840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M334 {ECO:0000313|EMBL:EFX59570.1,
RC ECO:0000313|Proteomes:UP000003840};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C.,
RA Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S., Surette M.G.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptococcus sp. M334.";
RL Submitted (MAR-2010) 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; GL732486; EFX59570.1; -; Genomic_DNA.
DR RefSeq; WP_000150987.1; NZ_GL732486.1.
DR AlphaFoldDB; E9FJU0; -.
DR REBASE; 101686; Ssp334ORF544P.
DR eggNOG; COG0286; Bacteria.
DR eggNOG; COG1002; Bacteria.
DR HOGENOM; CLU_456257_0_0_9; -.
DR OrthoDB; 9813673at2; -.
DR Proteomes; UP000003840; Unassembled WGS sequence.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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 Pfam; PF07669; Eco57I; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000313|EMBL:EFX59570.1};
KW Hydrolase {ECO:0000313|EMBL:EFX59570.1};
KW Nuclease {ECO:0000313|EMBL:EFX59570.1}.
FT DOMAIN 287..385
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
SQ SEQUENCE 625 AA; 72182 MW; EE9A15C84167942A CRC64;
MTIDISEESL AMESADLLKI LLKDRTTKKN IVWATHSYEL LGKGFAPSDR INASKVTGTY
ADLVQPRSEK SKYEQKDRTK IRAEVFTPTW LVEKQNGYVE AELESLDLED YIQLRWLEIT
CGEAPYMVTR YDTVTGEEIP LSERVGFVDR KLQRISREVS DEATFYELVK KAYRASYGYE
YQGDSLLLAR ENLLATFEDY YLANIGNQPT LEQKKEIATI ISYNVFQMDG LEKNSPYSAK
QEQSQQLSLF SDELEVQEVE ESKTQIKDWK KNKMIGFERL SSEESEMKFD VVIGNPPYQE
EAQGTSTKDM PIYHKFISES YKISKKASLI TPARFLSNAG GTPKTWNQQM LNNQHVKVSF
FEQKSGNVFP GTDIKGGVAV TYYDAEREFE PIEVFVPFIE MNSIRKKVIK KNFESIDQFV
TNRGSYRYSD LIYTDFPKLM SRVSDRRVAS NAFEKLPELF FDIKPEDGNE YIKIYGRFNN
ERVYKWFRKD YVTCPSNFEK YKIILPKANG SGAIGEVLST PVIGSPVIGY TETFISVGEF
DSLEEAEACL KYIKSKFLRT MLGILKITQD NTKDKWKYVP LQDFTVNSDI DWTQSVADID
RQLYQKYGLS PEEIAFIETH VREMD
//
