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Protein

23S rRNA (guanine(2535)-N(1))-methyltransferase

Gene

aviRa

Organism
Streptomyces viridochromogenes
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Specifically methylates the guanine-2535 in 23S ribosomal RNA. Confers resistance to antibiotic avilamycin, an orthosomycin antibiotic.2 Publications

Catalytic activityi

S-adenosyl-L-methionine + guanine(2535) in 23S rRNA = S-adenosyl-L-homocysteine + N(1)-methylguanine(2535) in 23S rRNA.1 Publication

GO - Molecular functioni

  • rRNA (guanine-N1-)-methyltransferase activity Source: UniProtKB

GO - Biological processi

  • methylation Source: UniProtKB
  • response to antibiotic Source: UniProtKB
  • rRNA methylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16329.
BRENDAi2.1.1.209. 6116.

Names & Taxonomyi

Protein namesi
Recommended name:
23S rRNA (guanine(2535)-N(1))-methyltransferase (EC:2.1.1.209)
Alternative name(s):
Avilamycin resistance protein A
Gene namesi
Name:aviRa
OrganismiStreptomyces viridochromogenes
Taxonomic identifieri1938 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25025023S rRNA (guanine(2535)-N(1))-methyltransferasePRO_0000418460Add
BLAST

Structurei

Secondary structure

1
250
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Helixi14 – 163Combined sources
Turni18 – 203Combined sources
Helixi33 – 4513Combined sources
Beta strandi47 – 493Combined sources
Beta strandi53 – 575Combined sources
Helixi64 – 729Combined sources
Helixi74 – 763Combined sources
Beta strandi77 – 859Combined sources
Helixi87 – 9812Combined sources
Helixi102 – 11918Combined sources
Helixi122 – 14019Combined sources
Beta strandi147 – 1515Combined sources
Helixi157 – 1593Combined sources
Helixi160 – 1645Combined sources
Beta strandi170 – 1756Combined sources
Helixi178 – 1803Combined sources
Beta strandi181 – 1866Combined sources
Helixi190 – 20314Combined sources
Beta strandi209 – 2179Combined sources
Beta strandi227 – 2326Combined sources
Beta strandi235 – 2417Combined sources
Helixi242 – 2476Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O9GX-ray1.50A1-250[»]
1O9HX-ray2.40A1-250[»]
ProteinModelPortaliQ9F5K5.
SMRiQ9F5K5. Positions 2-250.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9F5K5.

Family & Domainsi

Family and domain databases

Gene3Di1.10.287.540. 1 hit.
3.40.50.150. 2 hits.
InterProiIPR024268. AviRa.
IPR029063. SAM-dependent_MTases.
IPR023218. UPF0291_struct_dom.
[Graphical view]
PfamiPF11599. AviRa. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9F5K5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAYRHAVER IDSSDLACGV VLHSAPGYPA FPVRLATEIF QRALARLPGD
60 70 80 90 100
GPVTLWDPCC GSGYLLTVLG LLHRRSLRQV IASDVDPAPL ELAAKNLALL
110 120 130 140 150
SPAGLTAREL ERREQSERFG KPSYLEAAQA ARRLRERLTA EGGALPCAIR
160 170 180 190 200
TADVFDPRAL SAVLAGSAPD VVLTDLPYGE RTHWEGQVPA QPVAGLLRSL
210 220 230 240 250
ASALPAHAVI AVTDRSRKIP VAPVKALERL KIGTRSAVLV RAADVLEAGP
Length:250
Mass (Da):26,636
Last modified:July 5, 2004 - v2
Checksum:iE2F972770DA5A853
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF333038 Genomic DNA. Translation: AAG32067.2.

Genome annotation databases

KEGGiag:AAG32067.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF333038 Genomic DNA. Translation: AAG32067.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O9GX-ray1.50A1-250[»]
1O9HX-ray2.40A1-250[»]
ProteinModelPortaliQ9F5K5.
SMRiQ9F5K5. Positions 2-250.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAG32067.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16329.
BRENDAi2.1.1.209. 6116.

Miscellaneous databases

EvolutionaryTraceiQ9F5K5.

Family and domain databases

Gene3Di1.10.287.540. 1 hit.
3.40.50.150. 2 hits.
InterProiIPR024268. AviRa.
IPR029063. SAM-dependent_MTases.
IPR023218. UPF0291_struct_dom.
[Graphical view]
PfamiPF11599. AviRa. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "An ATP-binding cassette transporter and two rRNA methyltransferases are involved in resistance to avilamycin in the producer organism Streptomyces viridochromogenes Tu57."
    Weitnauer G., Gaisser S., Trefzer A., Stockert S., Westrich L., Quiros L.M., Mendez C., Salas J.A., Bechthold A.
    Antimicrob. Agents Chemother. 45:690-695(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: Tu57.
  2. "The avilamycin resistance determinants AviRa and AviRb methylate 23S rRNA at the guanosine 2535 base and the uridine 2479 ribose."
    Treede I., Jakobsen L., Kirpekar F., Vester B., Weitnauer G., Bechthold A., Douthwaite S.
    Mol. Microbiol. 49:309-318(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
    Strain: Tu57.
  3. "Crystal structure of the avilamycin resistance-conferring methyltransferase AviRa from Streptomyces viridochromogenes."
    Mosbacher T.G., Bechthold A., Schulz G.E.
    J. Mol. Biol. 329:147-157(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
    Strain: Tu57.

Entry informationi

Entry nameiAVRA_STRVR
AccessioniPrimary (citable) accession number: Q9F5K5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: July 5, 2004
Last modified: May 11, 2016
This is version 51 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.