ID   MYRA_MICGR              Reviewed;         295 AA.
AC   P37000;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Putative 23S rRNA (guanine-N(1)-)-methyltransferase;
DE            EC=2.1.1.-;
DE   AltName: Full=Mycinamicin-resistance protein MyrA;
GN   Name=myrA;
OS   Micromonospora griseorubida.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Micromonospora.
OX   NCBI_TaxID=28040;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8163173; DOI=10.1016/0378-1119(94)90125-2;
RA   Inouye M., Morohoshi T., Horinouchi S., Beppu T.;
RT   "Cloning and sequences of two macrolide-resistance-encoding genes from
RT   mycinamicin-producing Micromonospora griseorubida.";
RL   Gene 141:39-46(1994).
CC   -!- FUNCTION: Confers strong resistance to mycinamicin (MM) and tylosin
CC       (TY). May function as methyltransferase.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmA family.
CC       {ECO:0000305}.
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DR   EMBL; D16099; BAA03674.1; -; Genomic_DNA.
DR   RefSeq; WP_063854489.1; NG_048010.1.
DR   AlphaFoldDB; P37000; -.
DR   SMR; P37000; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016718; rRNA_m1G-MeTrfase_A_prd.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PIRSF; PIRSF018249; MyrA_prd; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Metal-binding; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase; Zinc.
FT   CHAIN           1..295
FT                   /note="Putative 23S rRNA (guanine-N(1)-)-methyltransferase"
FT                   /id="PRO_0000096672"
FT   BINDING         11
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         31
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         35
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         116..117
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   295 AA;  31348 MW;  AC42F0AF750BCB1A CRC64;
     MHPDLLPHLR CPVCGQPLHQ ADAAPPRALR CPAGHSFDIA RQGYVNLLTG RAPHVGDTAE
     MIAAREEFLA AGHYDPFSAA LATAAARAVP RRVRPGDGVG EPVAYPDLVV DAGAGTGRHL
     AAVLDAVPTA VGLALDVSKP ALRRAARAHP RAGAAVCDTW GRLPLADATV AVLVNVFAPR
     NGPEFRRVLR PDGALLVVTP TAEHLVELVD RLGLLRVDPA KDARVADSLT RHFEPAGQST
     HRHRLQLTRK EVLTLVGMGP SAWHTDPARL TARVAALSEP VTVTAAVRLA RYRPI