ID   Y2363_BACP2             Reviewed;         213 AA.
AC   A8FFL2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Uncharacterized methyltransferase BPUM_2363 {ECO:0000255|HAMAP-Rule:MF_02100};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_02100};
GN   Name=yrrT; OrderedLocusNames=BPUM_2363;
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032;
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(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}.
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DR   EMBL; CP000813; ABV63029.1; -; Genomic_DNA.
DR   RefSeq; WP_012010703.1; NZ_VEIC01000028.1.
DR   AlphaFoldDB; A8FFL2; -.
DR   SMR; A8FFL2; -.
DR   STRING; 315750.BPUM_2363; -.
DR   EnsemblBacteria; ABV63029; ABV63029; BPUM_2363.
DR   KEGG; bpu:BPUM_2363; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_111961_0_0_9; -.
DR   OMA; FEDWAAT; -.
DR   OrthoDB; 1739932at2; -.
DR   Proteomes; UP000001355; 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; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR023553; Uncharacterised_MeTfrase_YrrT.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..213
FT                   /note="Uncharacterized methyltransferase BPUM_2363"
FT                   /id="PRO_0000373847"
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         96
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02100"
SQ   SEQUENCE   213 AA;  24127 MW;  4D38219471F58F04 CRC64;
     MGREFLSLFD HWADSYDDTV SGHDEQYEEV FRRYSVILKE IVHRAGQHVL EFGSGTGNLT
     AALLAADKNV FGVEPSDAMK KAALQKGIPD VFHDGDFLSF PAPPFEPDTI VSSYAFHHLT
     DEEKKQAIHT YSNILHSDGK IVFADTMFQN QSAHQAEIDK AKAAGFDQLA EDLETEYYPS
     IDVLKQIFEE EGFSTSFHQM NDFVWIVEAK KRE