id: S0EDH7 gene_symbol: S0EDH7 product_type: PROTEIN status: DRAFT taxon: id: NCBITaxon:1279085 label: Fusarium fujikuroi IMI 58289 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. references: - id: PMID:23825955 title: >- Deciphering the cryptic genome: genome-wide analyses of the rice pathogen Fusarium fujikuroi reveal complex regulation of secondary metabolism and novel metabolites reference_review: relevance: LOW correctness: VERIFIED review_notes: >- Genome-sequencing paper for F. fujikuroi IMI 58289 (UniProt RN [1], RX PubMed=23825955); source of the FFUJ_06423 gene model only. It does not characterize this protein. - id: file:GIBF5/S0EDH7/S0EDH7-bioinformatics/RESULTS.md title: S0EDH7 kinase-like domain, catalytic-motif and homolog analysis reference_review: relevance: HIGH correctness: VERIFIED review_notes: >- Local hmmscan against 14 kinase-like Pfam HMMs, catalytic-motif mapping in S0EDH7 and four Pezizomycotina homologs, and EBI BLAST against UniProtKB and Swiss-Prot (2026-10-21). Outputs are saved alongside the script. existing_annotations: [] core_functions: - description: >- 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: id: GO:0016301 label: kinase activity knowledge_gaps: - gap_statement: >- Whether the protein is catalytically active, and whether its phosphoacceptor is a protein or a small molecule, are unknown. boundary: >- Only fold-level kinase-like signatures and conservation of catalytic-loop and DFG residues are available; no characterized relative, ligand-binding evidence or activity assay exists. gap_kind: - BIOLOGY dark_aspect: MF_DARK - gap_statement: >- The function of the N-terminal ~180-residue region, the subcellular location and any biological process involving this Pezizomycotina-specific protein are unknown. boundary: >- The N-terminal region matches no domain signature, and no localization, expression or mutant data exist for FFUJ_06423 or any homolog. gap_kind: - BIOLOGY dark_aspect: BP_DARK supported_by: - reference_id: file:GIBF5/S0EDH7/S0EDH7-uniprot.txt record_section: ["DR:InterPro"] supporting_text: >- InterPro; IPR011009; Kinase-like_dom_sf. - reference_id: file:GIBF5/S0EDH7/S0EDH7-uniprot.txt record_section: ["DR:SUPFAM"] supporting_text: >- SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. - reference_id: file:GIBF5/S0EDH7/S0EDH7-bioinformatics/RESULTS.md supporting_text: >- 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. - reference_id: file:GIBF5/S0EDH7/S0EDH7-bioinformatics/RESULTS.md supporting_text: >- 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. suggested_questions: - question: >- 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? - question: >- 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: - hypothesis: >- FFUJ_06423 is an active kinase whose activity depends on the conserved catalytic-loop Asp D288 and DFG Asp D307. description: >- 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: >- Loss of FFUJ_06423 affects growth, development or secondary metabolism in Fusarium fujikuroi. description: >- 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.