ID   Y3874_MYCTO             Reviewed;         314 AA.
AC   P9WFH4; L0TDR0; O86359; Q7D4W6;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MT3874;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MT3874;
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; AAK48238.1; -; Genomic_DNA.
DR   PIR; H70801; H70801.
DR   RefSeq; WP_003420557.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFH4; -.
DR   SMR; P9WFH4; -.
DR   EnsemblBacteria; AAK48238; AAK48238; MT3874.
DR   KEGG; mtc:MT3874; -.
DR   PATRIC; fig|83331.31.peg.4169; -.
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..314
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MT3874"
FT                   /id="PRO_0000428538"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         161..162
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   314 AA;  34755 MW;  BACD884305460F6E CRC64;
     MPRTDNDSWA ITESVGATAL GVAAARAAET ESDNPLINDP FARIFVDAAG DGIWSMYTNR
     TLLAGATDLD PDLRAPIQQM IDFMAARTAF FDEYFLATAD AGVRQVVILA SGLDSRAWRL
     PWPDGTVVYE LDQPKVLEFK SATLRQHGAQ PASQLVNVPI DLRQDWPKAL QKAGFDPSKP
     CAWLAEGLVR YLPARAQDLL FERIDALSRP GSWLASNVPG AGFLDPERMR RQRADMRRMR
     AAAAKLVETE ISDVDDLWYA EQRTAVAEWL RERGWDVSTA TLPELLARYG RSIPHSGEDS
     IPPNLFVSAQ RATS