ID   Y2576_MYCA1             Reviewed;         313 AA.
AC   A0QFS9;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MAV_2576;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MAV_2576;
OS   Mycobacterium avium (strain 104).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=243243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000479; ABK68901.1; -; Genomic_DNA.
DR   RefSeq; WP_011724893.1; NC_008595.1.
DR   AlphaFoldDB; A0QFS9; -.
DR   SMR; A0QFS9; -.
DR   EnsemblBacteria; ABK68901; ABK68901; MAV_2576.
DR   KEGG; mav:MAV_2576; -.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; WDINESV; -.
DR   OrthoDB; 847145at2; -.
DR   Proteomes; UP000001574; 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..313
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MAV_2576"
FT                   /id="PRO_0000361102"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         161..162
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   313 AA;  34004 MW;  4EF451BDA14CBA6D CRC64;
     MARTDNDTWD INESVGATAL GVAGGRAAET RSADPLISDP YAKLFLEAAG DGIWRVYLDD
     ELPAELVGAD PQFEDRMQAM LGYTACRTKF FDDYFLAAAG EGIRQIVILA AGLDSRAWRL
     AWPAGCVVYE IDQPKVLEFK IGTLKSHAVD PIASHVSVGI DLRLDWPKAL AQAGFDASAP
     TAWSAEGLLP YLTADAQGLL FDRIQSLSAP GSRVAVEAFT NEFFSPESFA RREEQTERYR
     QAAIRLGGKD ITESGNLLYE EERTEVVDWL QAHGWTVTAA TSAEDLMAAS NRAVPAGLDA
     AVPESVFVEG RLR