ID   Y301_MYCA1              Reviewed;         314 AA.
AC   A0Q9K2;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MAV_0301;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MAV_0301;
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; ABK65850.1; -; Genomic_DNA.
DR   RefSeq; WP_011723470.1; NC_008595.1.
DR   AlphaFoldDB; A0Q9K2; -.
DR   SMR; A0Q9K2; -.
DR   EnsemblBacteria; ABK65850; ABK65850; MAV_0301.
DR   KEGG; mav:MAV_0301; -.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; DSMPPTL; -.
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..314
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MAV_0301"
FT                   /id="PRO_0000361105"
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   314 AA;  34846 MW;  32DDE70C697502D3 CRC64;
     MPRTDNDSWD ITQSVGATAL GVAAARAAET ESENPLISDP FARIFVDAAG KGMWSIYADP
     ALLTKADDLE PDLRGRLQLM IDFMATRTAF FDEFFLAAAD AGVRQVVILA AGLDARSWRL
     PWPDGTVVYE LDQPKVLDFK STTLREHGAQ PKAELVNVPI DLRQDWPKAL QEAGFDASRP
     AVWSAEGLVR YLPAQAQDLL FERIDALSVP GSRLASNVPD SGFTDPDRLA RQREDMRRMR
     AAAAKLVDAE ITDFDDLWYP EERTPVDSWL RERGWDVSTA TFAELMARYG RSIPQGAQDS
     MPPTLYVSAQ RRAG