ID   Y839_MYCTA              Reviewed;         301 AA.
AC   A5U0L8;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MRA_0839;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MRA_0839;
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}.
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; CP000611; ABQ72568.1; -; Genomic_DNA.
DR   RefSeq; WP_003404349.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U0L8; -.
DR   SMR; A5U0L8; -.
DR   EnsemblBacteria; ABQ72568; ABQ72568; MRA_0839.
DR   GeneID; 45424793; -.
DR   KEGG; mra:MRA_0839; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; TRFYDQF; -.
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..301
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MRA_0839"
FT                   /id="PRO_0000361233"
FT   BINDING         127
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         156..157
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   301 AA;  33416 MW;  5F6C68208D1E6199 CRC64;
     MVRADRDRWD LATSVGATAT MVAAQRALAA DPRYALIDDP YAAPLVRAVG MDVYTRLVDW
     QIPVEGDSEF DPQRMATGMA CRTRFFDQFF LDATHSGIGQ FVILASGLDA RAYRLAWPVG
     SIVYEVDMPE VIEFKTATLS DLGAEPATER RTVAVDLRDD WATALQTAGF DPKVPAAWSA
     EGLLVYLPVE AQDALFDNIT ALSAPGSRLA FEFVPDTAIF ADERWRNYHN RMSELGFDID
     LNELVYHGQR GHVLDYLTRD GWQTSALTVT QLYEANGFAY PDDELATAFA DLTYSSATLM
     R