ID   Y3827_MYCTA             Reviewed;         308 AA.
AC   A5U9B6;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MRA_3827;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MRA_3827;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
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; CP000611; ABQ75616.1; -; Genomic_DNA.
DR   RefSeq; WP_003420620.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U9B6; -.
DR   SMR; A5U9B6; -.
DR   STRING; 419947.MRA_3827; -.
DR   EnsemblBacteria; ABQ75616; ABQ75616; MRA_3827.
DR   KEGG; mra:MRA_3827; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; RMAMETF; -.
DR   OrthoDB; 847145at2; -.
DR   Proteomes; UP000001988; 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 MRA_3827"
FT                   /id="PRO_0000361229"
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