NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/BF00425543; PubMed=6429477 [NCBI, ExPASy, EBI, Israel, Japan]
Gryczan T., Israeli-Reches M., del Bue M., Dubnau D.;
"DNA sequence and regulation of ermD, a macrolide-lincosamide-streptogramin B resistance element from Bacillus licheniformis.";
Mol. Gen. Genet. 194:349-356(1984).

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 and oleandomycin.
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

M29832; AAA22599.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I39885; I39885.

3D structure databases

ModBase

Q03986.

Ontologies

GO:0000179;	Molecular function: rRNA (adenine-N6,N6-)-dimethyltransferase activity (inferred from electronic annotation from InterPro).
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).
GO:0000154;	Biological process: rRNA modification (inferred from electronic annotation from InterPro).
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.

ProtoNet

Q03986.

Other

UniRef

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

Keywords

Antibiotic resistance; Methyltransferase; S-adenosyl-L-methionine; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 287`	`287`		`rRNA adenine N-6-methyltransferase.`	`PRO_0000101669`

Sequence information

Length: 287 AA [This is the length of the unprocessed precursor]

Molecular weight: 32798 Da [This is the MW of the unprocessed precursor]

CRC64: D3227F255A729060 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKKNHKYRG KKLNRGESPN FSGQHLMHNK KLIEEIVDRA NISIDDTVLE LGAGKGALTT 

        70         80         90        100        110        120 
VLSQKAGKVL AVENDSKFVD ILTRKTAQHS NTKIIHQDIM KIHLPKEKFV VVSNIPYAIT 

       130        140        150        160        170        180 
TPIMKMLLNN PASGFQKGII VMEKGAAKRF TSKFIKNSYV LAWRMWFDIG IVREISKEHF 

       190        200        210        220        230        240 
SPPPKVDSAM VRITRKKDAP LSHKHYIAFR GLAEYALKEP NIPLCVALRG IFTPRQMKHL 

       250        260        270        280 
RKSLKINNEK TVGTLTENQW AVIFNTMTQY VMHHKWPRAN KRKPGEI

Q03986 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