CG5565

UniProt ID: Q9VQ04
Organism: Drosophila melanogaster
Review Status: COMPLETE
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Gene Description

CG5565 is a 240-residue haloacid dehalogenase-family protein predicted to dephosphorylate pseudouridine 5′-phosphate, based on its relationship to the characterized human PUDP enzyme. This activity removes phosphate from a modified nucleotide derived from RNA. Its precise substrate range, physiological role and subcellular location have not been directly established in Drosophila.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0016791 phosphatase activity
IBA
GO_REF:0000033 		MODIFY
Summary: The general phosphatase assignment is supported. Manual ortholog transfer to characterized human PUDP provides the more informative pseudouridine 5′-phosphatase activity; target-specific substrate kinetics remain unmeasured.
Reason: The general phosphatase assignment is supported. Manual ortholog transfer to characterized human PUDP provides the more informative pseudouridine 5′-phosphatase activity; target-specific substrate kinetics remain unmeasured.
Supporting Evidence:
PMID:20722631
Purified human recombinant HDHD1 dephosphorylated pseudouridine 5'-phosphate with a kcat of 1.6 s-1, a Km of 0.3 μM and a catalytic efficiency at least 1000-fold higher than that on which it acted on other phosphate esters, including 5'-UMP.
file:DROME/CG5565/CG5565-uniprot.txt
DR InterPro; IPR023198; PGP-like.
file:DROME/CG5565/CG5565-bioinformatics/RESULTS.md
Human annotated catalytic Asp14 and Asp16 map to target Asp16 and Asp18.
GO:0016791 phosphatase activity
IEA
GO_REF:0000002 		MODIFY
Summary: The general phosphatase assignment is supported. Manual ortholog transfer to characterized human PUDP provides the more informative pseudouridine 5′-phosphatase activity; target-specific substrate kinetics remain unmeasured.
Reason: The general phosphatase assignment is supported. Manual ortholog transfer to characterized human PUDP provides the more informative pseudouridine 5′-phosphatase activity; target-specific substrate kinetics remain unmeasured.
Supporting Evidence:
PMID:20722631
Purified human recombinant HDHD1 dephosphorylated pseudouridine 5'-phosphate with a kcat of 1.6 s-1, a Km of 0.3 μM and a catalytic efficiency at least 1000-fold higher than that on which it acted on other phosphate esters, including 5'-UMP.
file:DROME/CG5565/CG5565-uniprot.txt
DR InterPro; IPR023198; PGP-like.
file:DROME/CG5565/CG5565-bioinformatics/RESULTS.md
Human annotated catalytic Asp14 and Asp16 map to target Asp16 and Asp18.
GO:1990738 pseudouridine 5'-phosphatase activity
ISS
GO_REF:0000024 		ACCEPT
Summary: Retain the curator-reviewed ortholog transfer from human Q08623/PUDP, whose purified enzyme has strong kinetic specificity for pseudouridine 5′-phosphate. The complete fly protein has compatible phosphatase architecture. This is supported functional transfer, not a claim that the fly enzyme was assayed.
Reason: Retain the curator-reviewed ortholog transfer from human Q08623/PUDP, whose purified enzyme has strong kinetic specificity for pseudouridine 5′-phosphate. The complete fly protein has compatible phosphatase architecture. This is supported functional transfer, not a claim that the fly enzyme was assayed.
Supporting Evidence:
PMID:20722631
Purified human recombinant HDHD1 dephosphorylated pseudouridine 5'-phosphate with a kcat of 1.6 s-1, a Km of 0.3 μM and a catalytic efficiency at least 1000-fold higher than that on which it acted on other phosphate esters, including 5'-UMP.
file:DROME/CG5565/CG5565-uniprot.txt
DR InterPro; IPR023198; PGP-like.
file:DROME/CG5565/CG5565-bioinformatics/RESULTS.md
Human annotated catalytic Asp14 and Asp16 map to target Asp16 and Asp18.

Core Functions

Dephosphorylation of pseudouridine 5′-phosphate, inferred from curated orthology to characterized human PUDP.

Molecular Function:
pseudouridine 5'-phosphatase activity
Supporting Evidence:
  • PMID:20722631
    Purified human recombinant HDHD1 dephosphorylated pseudouridine 5'-phosphate with a kcat of 1.6 s-1, a Km of 0.3 μM and a catalytic efficiency at least 1000-fold higher than that on which it acted on other phosphate esters, including 5'-UMP.
  • file:DROME/CG5565/CG5565-uniprot.txt
    DR InterPro; IPR023198; PGP-like.
  • file:DROME/CG5565/CG5565-bioinformatics/RESULTS.md
    Human annotated catalytic Asp14 and Asp16 map to target Asp16 and Asp18.

References

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External Prediction Reviews

These computational predictions are reviewed separately from the GOA annotation set used for this review. The assessments below are from this project and do not constitute official GO annotations or endorsement by GO/UniProt. They are not included in the existing annotation review above.

ProtNLM External predictions

View prediction review YAML · CG5565-protnlm-predictions-review.yaml · Review status: COMPLETE

The ProtNLM2 API snapshot retrieved 2026-09-08 contains no GO-term predictions for Q9VQ04. Phosphatase activity (GO:0016791) is a supported omission candidate; pseudouridine 5'-phosphatase activity (GO:1990738) is a more specific candidate supported by FlyBase's manual ortholog transfer to experimentally characterized human PUDP, together with near-complete sequence alignment and retained catalytic Asp positions. The substrate assignment is an orthology-based inference, not a direct CG5565 assay; the alignment alone does not establish substrate specificity. The separate FUNCTION claim of in-vitro D,L-glyceraldehyde 3-phosphate dephosphorylation remains UNC and is not disproved by the better-supported physiological substrate. This completed record assesses the absence of GO output; predictions is empty because no GO or EC prediction was emitted. The narrative judgment remains in the linked function review and is not a score assigned to the omission.

Source documents: genes/DROME/CG5565/CG5565-protnlm-source.json · projects/PROTNLM_EVALUATION/fly-benchmark/manifest.json · genes/DROME/CG5565/CG5565-protnlm-function-review.md · genes/DROME/CG5565/CG5565-uniprot.txt · genes/DROME/CG5565/CG5565-bioinformatics/RESULTS.md · publications/PMID_20722631.md

No GO/EC predictions in the reviewed source.

Deep Research

Falcon

(CG5565-deep-research-falcon.md)

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📚 Additional Documentation

Notes

(CG5565-notes.md)

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Bioinformatics Results

(RESULTS.md)

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Protnlm Function Review

(CG5565-protnlm-function-review.md)

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📄 View Raw YAML

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