id: Q9VV60
gene_symbol: TyrRS
taxon:
  id: NCBITaxon:7227
  label: Drosophila melanogaster
status: COMPLETE
description: Fly TyrRS has established aminoacylation and regulated extracellular functions. Its secretion
  upon serum deprivation supports the broad starvation-response prediction, while the specific resveratrol-binding
  GO term is obsolete and direct fly binding is unmeasured.
source_documents:
- genes/DROME/TyrRS/TyrRS-protnlm-source.json
- genes/DROME/TyrRS/TyrRS-flybase.txt
- genes/DROME/TyrRS/TyrRS-GO-1905594-quickgo.json
- genes/DROME/TyrRS/TyrRS-ncomms10022.txt
- genes/DROME/TyrRS/TyrRS-hypotheses/fly41-resveratrol-recognition/openscientist.md
predictions:
- source_method: ProtNLM2
  source_version: UniProt API snapshot 2026-09-08
  source_reference_id: file:DROME/TyrRS/TyrRS-protnlm-source.json
  predicted_term:
    id: GO:0042594
    label: response to starvation
  predicted_term_type: GO_BP
  review:
    assessment: CNN
    confidence_score: 2
    summary: The primary fly study detects TyrRS-HA secretion from S2 cells after serum deprivation, with
      membrane-integrity and tubulin controls excluding release by cell lysis. GO:0042594 includes secretion
      changes in response to nourishment deprivation, so this cellular experiment supports the broad claim.
      Existing target GOA contains only a broader stress annotation. This does not establish organismal
      starvation tolerance or the rat donor’s detailed nuclear mechanism; original training-set novelty
      is not known. The function was described in fly literature before this prediction release, so it
      is correct but not biologically novel (CNN); actual inclusion in the model training set is not established.
    supported_by:
    - reference_id: file:DROME/TyrRS/TyrRS-ncomms10022.txt
      supporting_text: presence of secreted TyrRS-HA in the supernatant 24 h after serum deprivation
- source_method: ProtNLM2
  source_version: UniProt API snapshot 2026-09-08
  source_reference_id: file:DROME/TyrRS/TyrRS-protnlm-source.json
  predicted_term:
    id: GO:1905594
    label: resveratrol binding
  predicted_term_type: GO_MF
  review:
    assessment: UNC
    confidence_score: 1
    summary: The exact predicted term, GO:1905594 resveratrol binding, is obsolete, replacement-less
      and explicitly out of scope for evolved molecular functions. OpenScientist found the fly tyrosine
      active-site pocket conserved with the human YARS1 pocket that binds resveratrol, so in-vitro binding
      by fly Q9VV60 remains plausible by homology but unmeasured. The biological prediction therefore
      cannot be validated or refuted with available evidence, and the obsolete xenobiotic-specific GO
      term should not be curated even if an in-vitro fly-binding assay is eventually positive.
    supported_by:
    - reference_id: file:DROME/TyrRS/TyrRS-hypotheses/fly41-resveratrol-recognition/openscientist.md
      supporting_text: Fly TyrRS almost certainly *can* accommodate resveratrol in its conserved tyrosine
        pocket (68.4% identity to human, all nine contact residues identical), but this has never been
        measured in *Drosophila*, represents a xenobiotic pharmacological interaction rather than an evolved
        function
    - reference_id: file:DROME/TyrRS/TyrRS-flybase.txt
      supporting_text: TyrRS-PA FBpp0075168 58.2 525 6.86 Q9VV60 NP_648895 AAF49462
    - reference_id: file:DROME/TyrRS/TyrRS-GO-1905594-quickgo.json
      supporting_text: The reason for obsoletion is that binding to resveratrol is not an evolved molecular
        function.
    - reference_id: PMID:25533949
      supporting_text: 'Here we present a 2.1 Å

        co-crystal structure of resveratrol bound to the active site of TyrRS.'
references:
- id: PMID:26761199
  title: The aminoacyl-tRNA synthetases of Drosophila melanogaster.
  findings: []
- id: file:DROME/TyrRS/TyrRS-flybase.txt
  title: TyrRS-flybase.txt
  findings: []
- id: file:DROME/TyrRS/TyrRS-GO-1905594-quickgo.json
  title: TyrRS-GO-1905594-quickgo.json
  findings: []
- id: PMID:25533949
  title: A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol.
  findings: []
- id: file:DROME/TyrRS/TyrRS-ncomms10022.txt
  title: Primary full text of PMID:26658841 from Nature Communications
  findings: []
- id: file:DROME/TyrRS/TyrRS-hypotheses/fly41-resveratrol-recognition/openscientist.md
  title: OpenScientist audit of the TyrRS resveratrol-binding prediction
  findings:
  - statement: OpenScientist found the fly resveratrol pocket plausible by homology but direct fly binding
      unmeasured and the exact GO term unassignable.
    supporting_text: Fly TyrRS almost certainly *can* accommodate resveratrol in its conserved tyrosine
      pocket (68.4% identity to human, all nine contact residues identical), but this has never been measured
      in *Drosophila*, represents a xenobiotic pharmacological interaction rather than an evolved function