[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TRANSPOSON=Tn1545; DOI=10.1093/nar/18.12.3660; PubMed=2163525 [NCBI, ExPASy, EBI, Israel, Japan] Trieu-Cuot P., Poyart-Salmeron C., Carlier C., Courvalin P.; "Nucleotide sequence of the erythromycin resistance gene of the conjugative transposon Tn1545."; Nucleic Acids Res. 18:3660-3660(1990).
[2]	STRUCTURE BY NMR. DOI=10.1038/nsb0697-483; PubMed=9187657 [NCBI, ExPASy, EBI, Israel, Japan] Yu L., Petros A.M., Schnuchel A., Zhong P., Severin J.M., Walter K., Holzman T.F., Fesik S.W.; "Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance."; Nat. Struct. Biol. 4:483-489(1997).
[3]	ERRATUM. Yu L., Petros A.M., Schnuchel A., Zhong P., Severin J.M., Walter K., Holzman T.F., Fesik S.W.; Nat. Struct. Biol. 4:592-592(1997).

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.
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

X52632; -; NOT_ANNOTATED_CDS; Genomic_DNA.

[EMBL / GenBank / DDBJ]

PIR

S12727; S12727.

3D structure databases

PDB

1YUB; NMR; -; A=1-245.

[ExPASy / RCSB / EBI]

1YUB; -.

P21236; 1-245.

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).
GO:0032196;	Biological process: transposition (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.

Other

P21236; -.

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

Keywords

3D-structure; Antibiotic resistance; Methyltransferase; S-adenosyl-L-methionine; Transferase; Transposable element.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 245`	`245`	`rRNA adenine N-6-methyltransferase.`	`PRO_0000101690`
`TURN`	`15 17`	`3`
`HELIX`	`18 24`	`7`
`STRAND`	`29 35`	`7`
`HELIX`	`45 50`	`6`
`STRAND`	`51 60`	`10`
`STRAND`	`62 68`	`7`
`TURN`	`70 73`	`4`
`STRAND`	`75 79`	`5`
`TURN`	`85 88`	`4`
`STRAND`	`92 100`	`9`
`STRAND`	`103 105`	`3`
`HELIX`	`107 116`	`10`
`STRAND`	`120 129`	`10`
`HELIX`	`130 135`	`6`
`HELIX`	`137 139`	`3`
`HELIX`	`141 144`	`4`
`TURN`	`145 148`	`4`
`STRAND`	`153 157`	`5`
`STRAND`	`162 165`	`4`
`STRAND`	`170 175`	`6`
`HELIX`	`184 199`	`16`
`HELIX`	`202 205`	`4`
`STRAND`	`207 209`	`3`
`HELIX`	`210 217`	`8`
`HELIX`	`229 241`	`13`

Sequence information

Length: 245 AA [This is the length of the unprocessed precursor]

Molecular weight: 28783 Da [This is the MW of the unprocessed precursor]

CRC64: 5E3AB1BAAA6511C5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNKNIKYSQN FLTSEKVLNQ IIKQLNLKET DTVYEIGTGK GHLTTKLAKI SKQVTSIELD 

        70         80         90        100        110        120 
SHLFNLSSEK LKLNIRVTLI HQDILQFQFP NKQRYKIVGS IPYHLSTQII KKVVFESHAS 

       130        140        150        160        170        180 
DIYLIVEEGF YKRTLDIHRT LGLLLHTQVS IQQLLKLPAE CFHPKPKVNS VLIKLTRHTT 

       190        200        210        220        230        240 
DVPDKYWKLY TYFVSKWVNR EYRQLFTKNQ FHQAMKHAKV NNLSTITYEQ VLSIFNSYLL 


FNGRK

P21236 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