ID   Y3087_BACCN             Reviewed;         212 AA.
AC   A7GT53;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Uncharacterized methyltransferase Bcer98_3087 {ECO:0000255|HAMAP-Rule:MF_02100};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_02100};
GN   OrderedLocusNames=Bcer98_3087;
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
CC   -!- FUNCTION: Could be a S-adenosyl-L-methionine-dependent
CC       methyltransferase. {ECO:0000255|HAMAP-Rule:MF_02100}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. YrrT family.
CC       {ECO:0000255|HAMAP-Rule:MF_02100}.
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DR   EMBL; CP000764; ABS23311.1; -; Genomic_DNA.
DR   RefSeq; WP_012095548.1; NC_009674.1.
DR   AlphaFoldDB; A7GT53; -.
DR   SMR; A7GT53; -.
DR   STRING; 315749.Bcer98_3087; -.
DR   EnsemblBacteria; ABS23311; ABS23311; Bcer98_3087.
DR   GeneID; 56418633; -.
DR   KEGG; bcy:Bcer98_3087; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_111961_0_0_9; -.
DR   OMA; FEDWAAT; -.
DR   OrthoDB; 1739932at2; -.
DR   Proteomes; UP000002300; Chromosome.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_02100; Methyltr_YrrT; 1.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR023553; Uncharacterised_MeTfrase_YrrT.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..212
FT                   /note="Uncharacterized methyltransferase Bcer98_3087"
FT                   /id="PRO_0000373845"
FT   BINDING         53
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02100"
FT   BINDING         74
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02100"
FT   BINDING         97
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02100"
SQ   SEQUENCE   212 AA;  24373 MW;  52FC20A2FEF01CC3 CRC64;
     MGTEFNGLFD EWAHTYDSFV QGEDIQYKEV FAHYEEILED VVNKSFGNVL EFGVGTGNLT
     NKLLLAGRTV YGIEPSREMR AIAKEKLPEG FTITEGDFLK FDVPNTIDTI VSTYAFHHLT
     DEEKDRAIAK YSQLLNKGGK IVFADTIFVD QEAYDKTVET AKQRGFHQLA NDLQTEYYTR
     IPIMQSIFEK NGFHVTFTRL NHFVWVMEAT KQ