ERMA_AERER
ID ERMA_AERER Reviewed; 340 AA.
AC P09891;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=rRNA adenine N-6-methyltransferase;
DE EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01026};
DE AltName: Full=Erythromycin resistance protein;
DE AltName: Full=Macrolide-lincosamide-streptogramin B resistance protein;
GN Name=ermA;
OS Aeromicrobium erythreum (strain ATCC 51598 / DSM 8599 / JCM 8359 / NBRC
OS 15406 / NRRL B-3381).
OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC Aeromicrobium.
OX NCBI_TaxID=31956;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=4043733; DOI=10.1016/0378-1119(85)90004-6;
RA Roberts A.N., Hudson G.S., Brenner S.;
RT "An erythromycin-resistance gene from an erythromycin-producing strain of
RT Arthrobacter sp.";
RL Gene 35:259-270(1985).
CC -!- FUNCTION: Involved in erythromycin resistance.
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; M11276; AAA22075.1; -; Genomic_DNA.
DR AlphaFoldDB; P09891; -.
DR SMR; P09891; -.
DR KEGG; ag:AAA22075; -.
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; 1.10.8.100; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001737; KsgA/Erm.
DR InterPro; IPR023165; rRNA_Ade_diMease-like_C.
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..340
FT /note="rRNA adenine N-6-methyltransferase"
FT /id="PRO_0000101666"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 40
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 127
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 340 AA; 37453 MW; E99A714C391952B5 CRC64;
MAGPQDRPRG RGPSSGRPQR PVGGRSQRDR DRRVLGQNFL RDPATIRRIA DAADVDPDGL
VVEAGPGEGL LTRELARRAG RVRTYELDQR LARRLSTDLA QETSIEVVHA DFLTAPHPEE
PFQFVGAIPY GITSAIVDWC LTAPTLTSAT LVTQQEFARK RTGDYGRWTA LTVTTWPTFE
WQYVAKVDRT LFTPVPRVHS AIMRLRRRPQ PLLRDAAARS RFADMVEIGF VGKGGSLYRS
LTREWPRSKV DSAFARADVH HDEIVAFVHP DQWITLFQLL DGSRGGAARG PGDQRGRRGR
PGGGPRPDGR AGGGPRRDAG GRRTGDGRGG RPRPPRGGQA