ID   Y893_MYCTO              Reviewed;         325 AA.
AC   P9WFI0; L0T579; P64747; Q10552;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MT0917;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MT0917;
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}.
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; AE000516; AAK45163.1; -; Genomic_DNA.
DR   PIR; B70782; B70782.
DR   RefSeq; WP_003404654.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFI0; -.
DR   SMR; P9WFI0; -.
DR   EnsemblBacteria; AAK45163; AAK45163; MT0917.
DR   KEGG; mtc:MT0917; -.
DR   PATRIC; fig|83331.31.peg.985; -.
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..325
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MT0917"
FT                   /id="PRO_0000428535"
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   325 AA;  36073 MW;  6280F61020906EDE CRC64;
     MRTEDDSWDV TTSVGSTGLL VAAARALETQ KADPLAIDPY AEVFCRAAGG EWADVLDGKL
     PDHYLTTGDF GEHFVNFQGA RTRYFDEYFS RATAAGMKQV VILAAGLDSR AFRLQWPIGT
     TIFELDRPQV LDFKNAVLAD YHIRPRAQRR SVAVDLRDEW QIALCNNGFD ANRPSAWIAE
     GLLVYLSAEA QQRLFIGIDT LASPGSHVAV EEATPLDPCE FAAKLERERA ANAQGDPRRF
     FQMVYNERWA RATEWFDERG WRATATPLAE YLRRVGRAVP EADTEAAPMV TAITFVSAVR
     TGLVADPART SPSSTSIGFK RFEAD