ID   Y293_MYCTO              Reviewed;         302 AA.
AC   P9WFI8; L0T365; O53686; Q7DA39;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MT0293;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MT0293;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Exhibits S-adenosyl-L-methionine-dependent methyltransferase
CC       activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UPF0677 family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK44517.1; -; Genomic_DNA.
DR   PIR; G70835; G70835.
DR   RefSeq; WP_003401448.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFI8; -.
DR   SMR; P9WFI8; -.
DR   EnsemblBacteria; AAK44517; AAK44517; MT0293.
DR   KEGG; mtc:MT0293; -.
DR   PATRIC; fig|83331.31.peg.317; -.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR011610; CHP00027_methylltransferase.
DR   InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF04072; LCM; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00027; mthyl_TIGR00027; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..302
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MT0293"
FT                   /id="PRO_0000428531"
FT   BINDING         126
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         155..156
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   302 AA;  32998 MW;  E61B7CC197AE2782 CRC64;
     MRTEGDSWDI TTSVGSTALF VATARALEAQ KSDPLVVDPY AEAFCRAVGG SWADVLDGKL
     PDHKLKSTDF GEHFVNFQGA RTKYFDEYFR RAAAAGARQV VILAAGLDSR AYRLPWPDGT
     TVFELDRPQV LDFKREVLAS HGAQPRALRR EIAVDLRDDW PQALRDSGFD AAAPSAWIAE
     GLLIYLPATA QERLFTGIDA LAGRRSHVAV EDGAPMGPDE YAAKVEEERA AIAEGAEEHP
     FFQLVYNERC APAAEWFGER GWTAVATLLN DYLEAVGRPV PGPESEAGPM FARNTLVSAA
     RV