Y3960_BACAH
ID Y3960_BACAH Reviewed; 212 AA.
AC A0RIY8;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Uncharacterized methyltransferase BALH_3960 {ECO:0000255|HAMAP-Rule:MF_02100};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_02100};
GN OrderedLocusNames=BALH_3960;
OS Bacillus thuringiensis (strain Al Hakam).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=412694;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Al Hakam;
RX PubMed=17337577; DOI=10.1128/jb.00241-07;
RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL J. Bacteriol. 189:3680-3681(2007).
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 -!- SEQUENCE CAUTION:
CC Sequence=ABK87181.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000485; ABK87181.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000536311.1; NC_008600.1.
DR AlphaFoldDB; A0RIY8; -.
DR SMR; A0RIY8; -.
DR EnsemblBacteria; ABK87181; ABK87181; BALH_3960.
DR KEGG; btl:BALH_3960; -.
DR HOGENOM; CLU_111961_0_0_9; -.
DR Proteomes; UP000000761; 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 BALH_3960"
FT /id="PRO_0000373849"
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; 24300 MW; 14C3A04A12F36C0B CRC64;
MGTEFNGLFD EWAHTYDSFV QGEDIQYKEV FAHYEDILED VVNKSFGHVL EFGVGTGNLT
NKLLLAGRTV YGIEPSREMR MIAKEKLPKE FSITEGDFLS FEVPNSIDTI VSTYAFHHLT
DDEKNVAIAK YSQLLNKGGK IVFADTIFAD QDAYDKTVEA AKQRGFHQLA NDLQTEYYTR
IPVMQTIFEN NGFHVTFTRL NHFVWVMEAT KQ