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Database: UniProt
Entry: Q4JHH6_STAAU
LinkDB: Q4JHH6_STAAU
Original site: Q4JHH6_STAAU 
ID   Q4JHH6_STAAU            Unreviewed;       244 AA.
AC   Q4JHH6;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   03-MAY-2023, entry version 71.
DE   RecName: Full=rRNA adenine N-6-methyltransferase {ECO:0000256|ARBA:ARBA00016505};
DE            EC=2.1.1.184 {ECO:0000256|ARBA:ARBA00012304};
DE   AltName: Full=Erythromycin resistance protein {ECO:0000256|ARBA:ARBA00030809};
DE   AltName: Full=Macrolide-lincosamide-streptogramin B resistance protein {ECO:0000256|ARBA:ARBA00029941};
OS   Staphylococcus aureus.
OG   Plasmid pWBG738 {ECO:0000313|EMBL:AAY88963.1}.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280 {ECO:0000313|EMBL:AAY88963.1};
RN   [1] {ECO:0000313|EMBL:AAY88963.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CMRSA {ECO:0000313|EMBL:AAY88963.1};
RC   PLASMID=pWBG738 {ECO:0000313|EMBL:AAY88963.1};
RA   O'Brien F.G., Zaini Z., Grubb W.B.;
RT   "The complete sequence of plasmid pWBG738 from the ST1-MRSA-IV lineage of
RT   community methicillin-resistant Staphylococcus aureus.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein produces a dimethylation of the adenine residue
CC       at position 2085 in 23S rRNA, resulting in reduced affinity between
CC       ribosomes and macrolide-lincosamide-streptogramin B antibiotics.
CC       {ECO:0000256|ARBA:ARBA00003100}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(2085) in 23S rRNA + 2 S-adenosyl-L-methionine = 2
CC         H(+) + N(6)-dimethyladenosine(2085) in 23S rRNA + 2 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:42784, Rhea:RHEA-COMP:10237, Rhea:RHEA-
CC         COMP:10238, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74493; EC=2.1.1.184;
CC         Evidence={ECO:0000256|ARBA:ARBA00001449};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. rRNA adenine N(6)-methyltransferase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01026}.
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DR   EMBL; DQ088624; AAY88963.1; -; Genomic_DNA.
DR   RefSeq; WP_011282421.1; NG_047815.1.
DR   RefSeq; YP_271816.1; NC_007209.1.
DR   AlphaFoldDB; Q4JHH6; -.
DR   GO; GO:0052910; F:23S rRNA (adenine(2085)-N(6))-dimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.8.100; Ribosomal RNA adenine dimethylase-like, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; DIMETHYLADENOSINE TRANSFERASE; 1.
DR   PANTHER; PTHR11727:SF7; DIMETHYLADENOSINE TRANSFERASE-RELATED; 1.
DR   Pfam; PF00398; RrnaAD; 1.
DR   SMART; SM00650; rADc; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR   PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01026}; Plasmid {ECO:0000313|EMBL:AAY88963.1};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01026};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01026};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01026}.
FT   DOMAIN          18..180
FT                   /note="Ribosomal RNA adenine methylase transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00650"
FT   BINDING         11
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         13
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         38
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         59
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         84
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         101
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   244 AA;  28908 MW;  FC7CA652481C7AA2 CRC64;
     MNEKNIKHSQ NFITSKHNID KIMTNIRLNE HDNIFEIGSG KGHFTLELVQ RCNFVTAIEI
     DHKLCKTTEN KLVDHDNFQV LNKDILQFKF PKNQSYKIFG NIPYNISTDI IRKIVFDSIA
     DEIYLIVEYG FAKRLLNTKR SLALFLMAEV DISILSMVPR EYFHPKPKVN SSLIRLNRKK
     SRISHKDKQK YNYFVMKWVD KEYKKIFTKN QFNNSLKHAG IDDLNNISFE QFLSLFNSYK
     LFNK
//
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