ID   Y213_MYCA9              Reviewed;         303 AA.
AC   B1MEP9;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MAB_0213c;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MAB_0213c;
OS   Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM
OS   13569 / NCTC 13031 / TMC 1543) (Mycobacterium abscessus).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacteroides; Mycobacteroides abscessus.
OX   NCBI_TaxID=561007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC
RC   1543;
RX   PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA   Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA   Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA   Gaillard J.L.;
RT   "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT   Mycobacterium abscessus.";
RL   PLoS ONE 4:E5660-E5660(2009).
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; CU458896; CAM60313.1; -; Genomic_DNA.
DR   RefSeq; WP_005112905.1; NZ_MLCG01000005.1.
DR   AlphaFoldDB; B1MEP9; -.
DR   SMR; B1MEP9; -.
DR   EnsemblBacteria; CAM60313; CAM60313; MAB_0213c.
DR   GeneID; 66970598; -.
DR   KEGG; mab:MAB_0213c; -.
DR   Proteomes; UP000007137; 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..303
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MAB_0213c"
FT                   /id="PRO_0000361120"
FT   BINDING         126
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         155..156
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   303 AA;  33266 MW;  12252F00E31C4CC8 CRC64;
     MRTDTDTWDI QTSVGSTALA VAAGRALARH PANGAPIDPY AELFCRAAGG QWSDLVQGKQ
     SDHALSSEDF GRSFANFQAA RTAFFDNFFT TTSDTGVRQV VLLASGLDCR AYRLQWPAET
     EVYELDQPLV QQFKQETLDA HGAAPSAVRH PISVDLRQDW STILQESGFD PSRPSAWLVE
     GLLFFLKSSA QDLLLETIDS LAAPGSHIAV EQRDTYPDIE FEMRRAAAAD SAEPGGSPLA
     DFLALIYNES RSEAATWLRG RGWAAERIAL LDYMNTSGFE LPAYSSVGWD TLRYTNMVTA
     AKR