ID   Y3895_MYCTO             Reviewed;         308 AA.
AC   P9WFH2; L0TGK0; P72053; Q7D4V4;
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 MT3895;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MT3895;
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; AAK48260.1; -; Genomic_DNA.
DR   PIR; G70696; G70696.
DR   RefSeq; WP_003420620.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFH2; -.
DR   SMR; P9WFH2; -.
DR   EnsemblBacteria; AAK48260; AAK48260; MT3895.
DR   KEGG; mtc:MT3895; -.
DR   PATRIC; fig|83331.31.peg.4190; -.
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..308
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MT3895"
FT                   /id="PRO_0000428539"
FT   BINDING         131
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         160..161
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   308 AA;  33390 MW;  5865CF059D44E304 CRC64;
     MARTDDDSWD LATGVGATAT LVAAGRARAA RAAQPLIDDP FAEPLVRAVG VEFLTRWATG
     ELDAADVDDP DAAWGLQRMT TELVVRTRYF DQFFLDAAAA GVRQAVILAS GLDARGYRLP
     WPADTTVFEV DQPRVLEFKA QTLAGLGAQP TADLRMVPAD LRHDWPDALR RGGFDAAEPA
     AWIAEGLFGY LPPDAQNRLL DHVTDLSAPG SRLALEAFLG SADRDSARVE EMIRTATRGW
     REHGFHLDIW ALNYAGPRHE VSGYLDNHGW RSVGTTTAQL LAAHDLPAAP ALPAGLADRP
     NYWTCVLG