ID   Y1364_MYCA1             Reviewed;         222 AA.
AC   A0QCH0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Putative O-methyltransferase MAV_1364;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MAV_1364;
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   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-dependent O-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01019}.
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DR   EMBL; CP000479; ABK65048.1; -; Genomic_DNA.
DR   RefSeq; WP_003875521.1; NC_008595.1.
DR   AlphaFoldDB; A0QCH0; -.
DR   SMR; A0QCH0; -.
DR   EnsemblBacteria; ABK65048; ABK65048; MAV_1364.
DR   GeneID; 66693084; -.
DR   KEGG; mav:MAV_1364; -.
DR   HOGENOM; CLU_067676_2_0_11; -.
DR   OMA; RGMRPDG; -.
DR   OrthoDB; 1948290at2; -.
DR   Proteomes; UP000001574; Chromosome.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002935; SAM_O-MeTrfase.
DR   Pfam; PF01596; Methyltransf_3; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51682; SAM_OMT_I; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..222
FT                   /note="Putative O-methyltransferase MAV_1364"
FT                   /id="PRO_0000380091"
FT   BINDING         49
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         71
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         73..74
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         79
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         97
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         98
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
SQ   SEQUENCE   222 AA;  22733 MW;  A77F72B4E0B1D568 CRC64;
     MDGTDAEAPG QTAPSRAESL VAHAEASISE DALLAAARER AVDIGAGAVT PAVGALLSLL
     TKLSGGKAIA EVGTGAGVSG LWLLSGMSDD GVLTTIDIEP EYLRLAKQAF AEAGIGPSRT
     RLIGGRAQEV LTRLADESYD LVFIDADPID QPDYVVEGVR LLRPGGVIVV HRAALGGRAG
     DPAARDAEVV AVREAARLIA EDERLTPALV PLGDGILAAV RD