S0EDH7

UniProt ID: S0EDH7
Organism: Fusarium fujikuroi IMI 58289
Review Status: DRAFT
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Gene Description

FFUJ_06423 (UniProt S0EDH7) is a 342-amino-acid uncharacterized protein of the rice bakanae pathogen Fusarium fujikuroi (Gibberella fujikuroi), encoded on chromosome VI. Its C-terminal half (about residues 180-320) adopts the protein kinase-like (PKL) fold, recognised only by fold-level signatures (InterPro IPR011009, SUPFAM SSF56112, Gene3D 1.10.510.10); the N-terminal 180 residues have no recognisable domain. The kinase-like region aligns to the C-lobe of the eukaryotic protein kinase profile below the family threshold and retains a variant catalytic loop (W286-G-D288-G-K290-A-S-N293) and a DFG motif (D307-F-G), whereas the N-lobe glycine-rich loop and beta3 lysine are not detectable. It belongs to a family of uncharacterized proteins found only in Pezizomycotina fungi, with no characterized ortholog and no PANTHER family assignment. It is therefore a predicted, possibly catalytically active, kinase whose phosphoacceptor (protein or small molecule), subcellular location and biological role are unknown; no experimental characterization has been reported.

Core Functions

Predicted kinase of the protein kinase-like (PKL) fold. The C-lobe catalytic machinery is retained (catalytic-loop Asp D288, Lys K290 and Asn N293 in a family-specific WGDGK..N loop; DFG Asp D307), consistent with phosphotransferase activity, but N-lobe ATP-binding elements are not detectable and the best profile match (eukaryotic protein kinase, PF00069) is below threshold, while small-molecule kinase profiles (Kdo, APH) align to the same segment. Protein kinase activity and protein phosphorylation are therefore not asserted.

Molecular Function:
kinase activity
Supporting Evidence:
  • file:GIBF5/S0EDH7/S0EDH7-uniprot.txt
    InterPro; IPR011009; Kinase-like_dom_sf.
  • file:GIBF5/S0EDH7/S0EDH7-uniprot.txt
    SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
  • file:GIBF5/S0EDH7/S0EDH7-bioinformatics/RESULTS.md
    the PF00069 HrDlKpeN position aligns to W286-G287-D288-G289-K290-A291-S292-N293 (catalytic Asp D288, Lys K290, Asn N293) and the DFG motif to D307-F308-G309.
  • file:GIBF5/S0EDH7/S0EDH7-bioinformatics/RESULTS.md
    HMM positions 1-42, which contain the glycine-rich loop and the beta3 lysine, are not aligned in S0EDH7 or in any of the four homologs tested.

References

PMID:23825955
Deciphering the cryptic genome: genome-wide analyses of the rice pathogen Fusarium fujikuroi reveal complex regulation of secondary metabolism and novel metabolites
file:GIBF5/S0EDH7/S0EDH7-bioinformatics/RESULTS.md
S0EDH7 kinase-like domain, catalytic-motif and homolog analysis

Suggested Questions for Experts

Q: Does the Pezizomycotina-specific family containing FFUJ_06423 (variant WGDGK..N catalytic loop, no detectable N-lobe glycine-rich loop) phosphorylate proteins or small molecules, and how is ATP bound without the canonical N-lobe elements?

Q: Does the uncharacterized N-terminal ~180-residue region form part of a divergent N-lobe, or a separate domain that determines substrate or localization?

Suggested Experiments

Experiment: Express recombinant FFUJ_06423 (wild type, D288A and D307A), test ATP binding (thermal shift with ATP/ADP analogues) and ATP turnover (ADP-Glo) with and without generic protein substrates and candidate small-molecule acceptors, and test autophosphorylation by phosphoproteomics.

Hypothesis: FFUJ_06423 is an active kinase whose activity depends on the conserved catalytic-loop Asp D288 and DFG Asp D307.

Experiment: Construct a targeted FFUJ_06423 deletion mutant by homologous recombination and compare growth, conidiation, secondary metabolite (gibberellin, bikaverin) production and rice pathogenicity with the wild-type IMI 58289 strain; localize a GFP fusion.

Hypothesis: Loss of FFUJ_06423 affects growth, development or secondary metabolism in Fusarium fujikuroi.

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.

ProtNLM2 External predictions

View prediction review YAML · S0EDH7-protnlm-predictions-review.yaml · Review status: COMPLETE

FFUJ_06423 (S0EDH7) is an uncharacterized Pezizomycotina-restricted protein whose C-terminal half has only fold-level protein kinase-like signatures. It retains catalytic-loop and DFG residues, but the N-lobe ATP-binding elements are not detectable, the phosphoacceptor class (protein or small molecule) is unknown, and no characterized ortholog, PANTHER family or publication exists. GOA carries no annotations for the gene. Neither ATP binding nor protein phosphorylation can be validated or refuted.

Source documents: genes/GIBF5/S0EDH7/S0EDH7-uniprot.txt · genes/GIBF5/S0EDH7/S0EDH7-goa.tsv · genes/GIBF5/S0EDH7/S0EDH7-ai-review.yaml · genes/GIBF5/S0EDH7/S0EDH7-bioinformatics/RESULTS.md

Review score: 2 = concordant with evidence; 1 = uncertain; 0 = discordant with evidence. This is an assessment score, not a model probability.

GO:0006468 protein phosphorylation GO_BP
UNC — Uncertain Review score: 1/2
Prediction method: ProtNLM2 · Version: UniProt 2024_06 pilot
Review rationale: The gene has no GOA annotations, so the term would be novel, but nothing establishes it. The kinase-like region matches the eukaryotic protein kinase profile (PF00069) only below the gathering threshold, small-molecule kinase profiles (Kdo, APH) align to the same segment, and no characterized relative or phylogenetic node is available for transfer. The gene review asserts only generic kinase activity and explicitly does not assert protein phosphorylation. A PubMed search for FFUJ_06423 and S0EDH7 returned no publications. Whether the protein phosphorylates proteins, small molecules or nothing is unknown.
Supporting Evidence:
GO:0005524 ATP binding GO_MF
UNC — Uncertain Review score: 1/2
Prediction method: ProtNLM2 · Version: UniProt 2024_06 pilot
Review rationale: The gene has no GOA annotations, so the term would be novel, but ATP binding is not established. The conserved catalytic-loop Asp/Lys/Asn and DFG Asp are compatible with an active phosphotransferase, yet the N-lobe glycine-rich loop and beta3 lysine that bind ATP in canonical kinases are not detectable in S0EDH7 or its homologs. No ligand-binding data or characterized relative exist, and no publication on the gene was found in PubMed. ATP binding remains plausible but untested.
Supporting Evidence:

Deep Research

Falcon

(S0EDH7-deep-research-falcon.md)

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📚 Additional Documentation

Notes

(S0EDH7-notes.md)

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Bioinformatics Results

(RESULTS.md)

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📄 View Raw YAML

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