P56930 · RL25_THETH

  • Protein
    Large ribosomal subunit protein bL25
  • Gene
    rplY
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

This is one of 3 proteins that mediate the attachment of the 5S rRNA onto the large ribosomal subunit.

Miscellaneous

Despite its considerably larger size this protein can substitute for the endogenous E.coli bL25 protein in vitro.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytosolic large ribosomal subunit
Molecular Function5S rRNA binding
Molecular Functionstructural constituent of ribosome
Biological Processtranslation

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Large ribosomal subunit protein bL25
  • Alternative names
    • 50S ribosomal protein L25 (TL5
      )

Gene names

    • Name
      rplY
    • Synonyms
      rpl25, rptL5

Organism names

  • Taxonomic identifier
  • Strain
    • VK1
  • Taxonomic lineage
    Bacteria > Deinococcota > Deinococci > Thermales > Thermaceae > Thermus

Accessions

  • Primary accession
    P56930
  • Secondary accessions
    • Q7M0Q3

Subcellular Location

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis10Destabilizes formation of the 5S rRNA/N-terminal bL25 complex.
Mutagenesis14No effect on 5S rRNA/N-terminal bL25 complex formation.
Mutagenesis16No effect on 5S rRNA/N-terminal bL25 complex formation.
Mutagenesis19Destabilizes formation of the 5S rRNA/N-terminal bL25 complex.
Mutagenesis20No effect on 5S rRNA/N-terminal bL25 complex formation.
Mutagenesis29No 5S rRNA/N-terminal bL25 complex formed.
Mutagenesis85Destabilizes formation of the 5S rRNA/N-terminal bL25 complex.
Mutagenesis85No 5S rRNA/N-terminal bL25 complex formed.
Mutagenesis87Strongly destabilizes formation of the 5S rRNA/N-terminal bL25 complex.
Mutagenesis87No 5S rRNA/N-terminal bL25 complex formed.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001816091-206Large ribosomal subunit protein bL25

Interaction

Subunit

Part of the 50S ribosomal subunit. Contacts the 5S rRNA.

Family & Domains

Features

Showing features for region, compositional bias.

Type
IDPosition(s)Description
Region1-91bL25 domain
Region92-206CTC domain
Region184-206Disordered
Compositional bias195-206Basic and acidic residues

Domain

The N-terminal 91 amino acids are capable of binding to 5S rRNA and also of displacing full-length protein bound to 5S rRNA. The first 80 amino acids are not sufficient.

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    206
  • Mass (Da)
    23,219
  • Last updated
    2005-03-29 v3
  • MD5 Checksum
    12ADD7DF7391FE76A0B77825A56EBAC2
MEYRLKAYYREGEKPSALRRAGKLPGLMYNRHLNRKVYVDLVEFDKVFRQASIHHVIVLELPDGQSLPTLVRQVNLDKRRRRPEHVDFFVLSDEPVEMYVPLRFVGTPAGVRAGGVLQEIHRDILVKVSPRNIPEFIEVDVSGLEIGDSLHASDLKLPPGVELAVSPEETIAAVVPPEDVEKLAEEAAAEVAEPEVIKKGKEEEEE

Features

Showing features for sequence conflict, compositional bias.

Type
IDPosition(s)Description
Sequence conflict27in Ref. 2; AA sequence
Compositional bias195-206Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X94435
EMBL· GenBank· DDBJ
CAA64209.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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