[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PLASMID=pE194; DOI=10.1093/nar/8.24.6081; PubMed=6162157 [NCBI, ExPASy, EBI, Israel, Japan] Gryczan T.J., Grandi G., Hahn J., Grandi R., Dubnau D.; "Conformational alteration of mRNA structure and the posttranscriptional regulation of erythromycin-induced drug resistance."; Nucleic Acids Res. 8:6081-6097(1980).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PLASMID=pE194; PubMed=6938954 [NCBI, ExPASy, EBI, Israel, Japan] Horinouchi S., Weisblum B.; "Posttranscriptional modification of mRNA conformation: mechanism that regulates erythromycin-induced resistance."; Proc. Natl. Acad. Sci. U.S.A. 77:7079-7083(1980).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48. PLASMID=pT48; PubMed=3141573 [NCBI, ExPASy, EBI, Israel, Japan] Catchpole I., Thomas C., Davies A., Dyke K.G.H.; "The nucleotide sequence of Staphylococcus aureus plasmid pT48 conferring inducible macrolide-lincosamide-streptogramin B resistance and comparison with similar plasmids expressing constitutive resistance."; J. Gen. Microbiol. 134:697-709(1988).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40. PLASMID=pA22; DOI=10.1016/0378-1097(90)90410-R; PubMed=2116351 [NCBI, ExPASy, EBI, Israel, Japan] Catchpole I., Dyke K.G.H.; "A Staphylococcus aureus plasmid that specifies constitutive macrolide-lincosamide-streptogramin B resistance contains a novel deletion in the ermC attenuator."; FEMS Microbiol. Lett. 57:43-47(1990).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11. PLASMID=pE194; DOI=10.1016/0022-2836(85)90061-0; PubMed=2414456 [NCBI, ExPASy, EBI, Israel, Japan] Mayford M., Weisblum B.; "Messenger RNA from Staphylococcus aureus that specifies macrolide-lincosamide-streptogramin resistance. Demonstration of its conformations and of the leader peptide it encodes."; J. Mol. Biol. 185:769-780(1985).

Comments

FUNCTION: This protein produces a dimethylation of the adenine residue at position 2058 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics.
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing N⁶-methyladenine.
INDUCTION: By erythromycin.
SIMILARITY: Belongs to the rRNA adenine N(6)-methyltransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

V01278; CAA24591.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M37841; AAA98226.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X54338; CAA38227.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A93717; YESA9E.

RefSeq

YP_025321.1; -.

3D structure databases

HSSP

P13956; 1QAN. [HSSP ENTRY / PDB]

SMR

P02979; 9-244.

ModBase

P02979.

Ontologies

GO:0003723;	Molecular function: RNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008988;	Molecular function: rRNA (adenine-N6-)-methyltransferase activity (inferred from electronic annotation from EC).
GO:0046677;	Biological process: response to antibiotic (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001737; RRNA_meth_trans.
Graphical view of domain structure.

PANTHER

PTHR11727; RRNA_meth_trans; 1.

Pfam

PF00398; RrnaAD; 1.
Pfam graphical view of domain structure.

SMART

SM00650; rADc; 1.
SMART graphical view of domain structure.

PROSITE

PS01131; RRNA_A_DIMETH; 1.

Genome annotation databases

GeneID

3284064; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Antibiotic resistance; Methyltransferase; Plasmid; RNA-binding; S-adenosyl-L-methionine; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 244`	`244`	`rRNA adenine N-6-methyltransferase.`	`PRO_0000101682`
`BINDING`	`11 11`		`S-adenosyl-L-methionine; via carbonyl oxygen (By similarity).`
`BINDING`	`13 13`		`S-adenosyl-L-methionine; via amide nitrogen (By similarity).`
`BINDING`	`38 38`		`S-adenosyl-L-methionine; via carbonyl oxygen (By similarity).`
`BINDING`	`59 59`		`S-adenosyl-L-methionine (By similarity).`
`BINDING`	`84 84`		`S-adenosyl-L-methionine (By similarity).`
`BINDING`	`101 101`		`S-adenosyl-L-methionine (By similarity).`

Sequence information

Length: 244 AA [This is the length of the unprocessed precursor]

Molecular weight: 28861 Da [This is the MW of the unprocessed precursor]

CRC64: 3CA9A267C4FE3C30 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNEKNIKHSQ NFITSKHNID KIMTNIRLNE HDNIFEIGSG KGHFTLELVK RCNFVTAIEI 

        70         80         90        100        110        120 
DHKLCKTTEN KLVDHDNFQV LNKDILQFKF PKNQSYKIYG NIPYNISTDI IRKIVFDSIA 

       130        140        150        160        170        180 
NEIYLIVEYG FAKRLLNTKR SLALLLMAEV DISILSMVPR EYFHPKPKVN SSLIRLSRKK 

       190        200        210        220        230        240 
SRISHKDKQK YNYFVMKWVN KEYKKIFTKN QFNNSLKHAG IDDLNNISFE QFLSLFNSYK 


LFNK

P02979 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools