ID   Y3439_MYCTA             Reviewed;         348 AA.
AC   A5U874;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 3.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MRA_3439;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MRA_3439;
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|UniProtKB:Q9CCZ4}.
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; ABQ75224.1; -; Genomic_DNA.
DR   RefSeq; WP_010886169.1; NC_009525.1.
DR   AlphaFoldDB; A5U874; -.
DR   SMR; A5U874; -.
DR   STRING; 419947.MRA_3439; -.
DR   EnsemblBacteria; ABQ75224; ABQ75224; MRA_3439.
DR   KEGG; mra:MRA_3439; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; PFADDHI; -.
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..348
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MRA_3439"
FT                   /id="PRO_0000361227"
FT   BINDING         171
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CCZ4"
FT   BINDING         200..201
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CCZ4"
SQ   SEQUENCE   348 AA;  38140 MW;  8C06D9F9BEFEBFBD CRC64;
     MARPMGKLPS NTRKCAQCAM AEALLEIAGQ TINQKDLGRS GRMTRTDNDT WDLASSVGAT
     ATMIATARAL ASRAENPLIN DPFAEPLVRA VGIDLFTRLA SGELRLEDIG DHATGGRWMI
     DNIAIRTKFY DDFFGDATTA GIRQVVILAA GLDTRAYRLP WPPGTVVYEI DQPAVIKFKT
     RALANLNAEP NAERHAVAVD LRNDWPTALK NAGFDPARPT AFSAEGLLSY LPPQGQDRLL
     DAITALSAPD SRLATQSPLV LDLAEEDEKK MRMKSAAEAW RERGFDLDLT ELIYFDQRND
     VADYLAGSGW QVTTSTGKEL FAAQGLPPFA DDHITRFADR RYISAVLK