NCU12035 encodes a 232-residue protein made of a single GCN5-related N-acetyltransferase (GNAT) domain (residues 3-184) and a short serine/threonine/proline-rich C-terminal tail. The domain keeps the acetyl-CoA pyrophosphate-binding motif A (R107-x-x-G110-x-G112), so the protein is predicted to transfer an acetyl group from acetyl-CoA to an acceptor. The acceptor is unknown. GNAT enzymes modify protein N-termini, lysine side chains, polyamines, antibiotics and other metabolites, and the domain alone does not say which class this protein acts on. Orthologs are found only in Neurospora species and no PANTHER subfamily is assigned, so no characterised relative is close enough to supply a substrate, pathway or cellular location. No experimental study of NCU12035 has been reported.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0016407 acetyltransferase activity | IEA GO_REF:0000104 | ACCEPT | Summary: Acetyltransferase activity is the most specific function the evidence supports. V5ILC0 has a complete GNAT domain (PROSITE PS51186, residues 3-184; Pfam PF00583) and keeps the acetyl-CoA-binding motif A (RRMGVG, residues 107-112). Acetyl-CoA is the usual donor in GNATs. No acceptor-specific child term (protein N-terminal, lysine, polyamine, aminoglycoside) can be chosen, because the gene has no PANTHER subfamily and its orthologs are confined to Neurospora. Reason: The GNAT domain and conserved motif A support acetyl transfer as a domain-level function. Because acceptor specificity in this superfamily cannot be predicted without a close characterised relative, the generic term is as precise as the evidence allows. Supporting Evidence: file:NEUCR/NCU12035/NCU12035-uniprot.txt DR InterPro; IPR000182; GNAT_dom. file:NEUCR/NCU12035/NCU12035-bioinformatics/RESULTS.md motif A candidate RRMGVG at 107-112 inside_domain=True PMID:33362253 The reaction entails transfer of an acetyl group from a substrate donor, most often acetyl coenzyme A, to a substrate acceptor |
| GO:0016740 transferase activity | IEA GO_REF:0000104 | MODIFY | Summary: Transferase activity is true but uninformative. Its descendant acetyltransferase activity (GO:0016407) is supported by the same UniRule and domain evidence and is already in this review. Reason: A correct but general term whose specific supported descendant, GO:0016407 acetyltransferase activity, the gene already carries. Proposed replacements: acetyltransferase activity Supporting Evidence: file:NEUCR/NCU12035/NCU12035-uniprot.txt DR InterPro; IPR000182; GNAT_dom. file:NEUCR/NCU12035/NCU12035-bioinformatics/RESULTS.md motif A candidate RRMGVG at 107-112 inside_domain=True |
| GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups | IEA GO_REF:0000002 | MODIFY | Summary: This InterPro2GO term is correct but more general than the supported function. GO:0016407 acetyltransferase activity is its is_a child (checked in OLS) and is already annotated from the UniRule. Acetyl-CoA is the usual GNAT donor and motif A is conserved. Reason: The general acyltransferase term should be refined to its descendant GO:0016407 acetyltransferase activity, which the gene already carries. Proposed replacements: acetyltransferase activity Supporting Evidence: file:NEUCR/NCU12035/NCU12035-uniprot.txt DR Pfam; PF00583; Acetyltransf_1; 1. PMID:33362253 The reaction entails transfer of an acetyl group from a substrate donor, most often acetyl coenzyme A, to a substrate acceptor |
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Download this section (compressed HTML)Q: What does NCU12035 acetylate? Its acceptor could be a protein N-terminus, a lysine, a polyamine or another small molecule.
Q: Is NCU12035 expressed, and under which conditions? Its orthologs are found only in Neurospora.
Experiment: Purify recombinant NCU12035 and screen it against a panel of acceptors (peptides, polyamines, aminoglycosides, amino sugars) with a CoA-release assay. Confirm any hit by mass spectrometry of the product, and test an R107A/G110A motif A mutant as a negative control.
Type: in vitro enzyme assay
Experiment: Make a C-terminal GFP fusion at the native locus to find where the protein is in the cell.
Type: fluorescence microscopy
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