ID   MYRB_MICGR              Reviewed;         311 AA.
AC   P43433;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Mycinamicin-resistance protein MyrB;
DE            EC=2.1.1.-;
GN   Name=myrB;
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 resistance to macrolide, lincosamide and
CC       streptogramin B antibiotics.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. rRNA adenine N(6)-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01026}.
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DR   EMBL; D14532; BAA03402.1; -; Genomic_DNA.
DR   RefSeq; WP_063844871.1; NG_047846.1.
DR   AlphaFoldDB; P43433; -.
DR   SMR; P43433; -.
DR   KEGG; ag:BAA03402; -.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR001737; KsgA/Erm.
DR   InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR   InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11727; PTHR11727; 1.
DR   Pfam; PF00398; RrnaAD; 1.
DR   SMART; SM00650; rADc; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR   PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Methyltransferase; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..311
FT                   /note="Mycinamicin-resistance protein MyrB"
FT                   /id="PRO_0000101693"
FT   REGION          272..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         27
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         29
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         54
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         75
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         98
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   311 AA;  34149 MW;  5597618B76AC4AF3 CRC64;
     MSSIRRRHAA ASLDTPAVGG RHELGQNFLV DRGVCTRIAE VVSSTTAHPV LELGAGDGAI
     TRALVAANLP VTALELDPRR VRRLQRTFAD GVTVVHGDML RYDFGPYPHH VVSTVPFSIT
     TPLLRRLIGQ RFWHTAVLLV QWEVARKRAG VGGTTMLTAA SWPWYEFTLV ERVPKTSFDP
     VPSVDGGILV IERRSAPLLD DRCVGDYQNL VREVYTGPGR GLAAILRTRL PGREVDAWLR
     RERVDPAALP RDLKAGHWAS LYRLYREVGT RPAPAGRSVR ARPGSVGPDR SLPPRGLRSG
     PPRARRRGGG A