ID   Y2020_MYCLE             Reviewed;         303 AA.
AC   Q9CBG0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase ML2020;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=ML2020;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Exhibits S-adenosyl-L-methionine-dependent methyltransferase
CC       activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UPF0677 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC30975.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL583924; CAC30975.1; ALT_INIT; Genomic_DNA.
DR   PIR; G87161; G87161.
DR   RefSeq; WP_041323116.1; NC_002677.1.
DR   AlphaFoldDB; Q9CBG0; -.
DR   SMR; Q9CBG0; -.
DR   EnsemblBacteria; CAC30975; CAC30975; CAC30975.
DR   KEGG; mle:ML2020; -.
DR   Leproma; ML2020; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; GSAASMW; -.
DR   Proteomes; UP000000806; 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; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..303
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase ML2020"
FT                   /id="PRO_0000361159"
FT   BINDING         130
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         159..160
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   303 AA;  33027 MW;  50B45FF06288A465 CRC64;
     MAATPEFGSL RSDDDHWDIV SSVGYTALLV AGWRALHAVG PQPLVRDEYA KYFITASRDP
     YLMNLLANPG TSLNETAFPR LYGVQTRFFD DFFSSAGDTG IRQAVIVAAG LDSRAYRLKW
     PNGATVFEID LPKVLEFKAR VLAEQGAIPN AGRSEVAADL RADWPRALKA AGFDPQRSSA
     WSVEGLLPYL TNDAQSALFT RIGELCAPGS RIAVGALGSR LDRKQLAALE ATHPGVNISG
     DVDFSALTYE PKTDSAQWLA AHGWAVEPVR NTLELQTSYG MTPPDVDVQM DSFMHSQYIT
     ATR