ID   Y4457_BACC1             Reviewed;         212 AA.
AC   Q730F9;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Uncharacterized methyltransferase BCE_4457 {ECO:0000255|HAMAP-Rule:MF_02100};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_02100};
GN   OrderedLocusNames=BCE_4457;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017194; AAS43358.1; -; Genomic_DNA.
DR   RefSeq; WP_000536318.1; NC_003909.8.
DR   AlphaFoldDB; Q730F9; -.
DR   SMR; Q730F9; -.
DR   DNASU; 2750845; -.
DR   EnsemblBacteria; AAS43358; AAS43358; BCE_4457.
DR   GeneID; 59155056; -.
DR   KEGG; bca:BCE_4457; -.
DR   HOGENOM; CLU_111961_0_0_9; -.
DR   OMA; FEDWAAT; -.
DR   Proteomes; UP000002527; 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 BCE_4457"
FT                   /id="PRO_0000373842"
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;  24292 MW;  6ABDA7AD9EDF1CC4 CRC64;
     MGTEFNGLFD EWAHTYDSFV QGEDIQYKEV FAHYEDILED VVNKSFGNVL EFGVGTGNLT
     NKLLLAGRTV YGIEPSREMR MIAKEKLPKE FSITEGDFLS FEVPNSIDTI VSTYAFHHLT
     DDEKNVAIAK YSQLLNKGGK IVFADTIFAD QDAYDKTVEA AKQRGFHELA NDLQTEYYTR
     IPIMQTIFEN NGFHVTFTRL NHFVWVMEAT KQ