ID   Y1947_MYCTO             Reviewed;         303 AA.
AC   P9WFH6; L0T871; O07736; Q7D7T8;
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 MT1947;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MT1947;
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; AAK46218.1; -; Genomic_DNA.
DR   PIR; E70517; E70517.
DR   RefSeq; WP_003409526.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFH6; -.
DR   SMR; P9WFH6; -.
DR   EnsemblBacteria; AAK46218; AAK46218; MT1947.
DR   KEGG; mtc:MT1947; -.
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..303
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MT1947"
FT                   /id="PRO_0000428537"
FT   BINDING         129
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         158..159
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   303 AA;  33267 MW;  7480EB8065C70DA8 CRC64;
     MTTPEYGSLR SDDDHWDIVS NVGYTALLVA GWRALHTTGP KPLVQDEYAK HFITASADPY
     LEGLLANPRT SEDGTAFPRL YGVQTRFFDD FFNCADEAGI RQAVIVAAGL DCRAYRLDWQ
     PGTTVFEIDV PKVLEFKARV LSERGAVPKA HRVAVPADLR TDWPTPLTAA GFDPQRPSAW
     SVEGLLPYLT GDAQYALFAR IDELCAPGSR VALGALGSRL DHEQLAALET AHPGVNMSGD
     VNFSALTYDD KTDPVEWLVE HGWAVDPVRS TLELQVGYGL TPPDVDVKID SFMRSQYITA
     VRA