Y4623_BACAA
ID Y4623_BACAA Reviewed; 212 AA.
AC C3P965;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Uncharacterized methyltransferase BAA_4623 {ECO:0000255|HAMAP-Rule:MF_02100};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_02100};
GN OrderedLocusNames=BAA_4623;
OS Bacillus anthracis (strain A0248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=592021;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A0248;
RA Dodson R.J., Munk A.C., Bruce D., Detter C., Tapia R., Sutton G., Sims D.,
RA Brettin T.;
RT "Genome sequence of Bacillus anthracis A0248.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001598; ACQ48279.1; -; Genomic_DNA.
DR RefSeq; WP_000536319.1; NC_012659.1.
DR AlphaFoldDB; C3P965; -.
DR SMR; C3P965; -.
DR GeneID; 64199718; -.
DR KEGG; bai:BAA_4623; -.
DR HOGENOM; CLU_111961_0_0_9; -.
DR OMA; FEDWAAT; -.
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 BAA_4623"
FT /id="PRO_1000189546"
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; 24277 MW; 6ABDA7AD8E90A82F CRC64;
MGTEFNGLFD EWAHTYDSFV QGEDIQYKEV FAHYEDILED VVNKSFGNVL EFGVGTGNLT
NKLLLAGRTV YGIEPSREMR MIAKEKLPKE FSITEGDFLS FEVPNSIDTI VSTYAFHHLT
DDEKNVAIAK YSQLLNKGGK IVFADTIFAD QDAYDKTVEA AKQRGFHQLA NDLQTEYYTR
IPVMQTIFEN NGFHVTFTRL NHFVWVMEAT KQ