GO_REF:0000015

Use of the ND evidence code for Gene Ontology (GO) terms

GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000108

Automatic assignment of GO terms using logical inference, based on on inter-ontology links

PMID:30358795

The cellular economy of the Saccharomyces cerevisiae zinc proteome.

Bioinformatic definition of the yeast zinc proteome (~582 known or potential zinc-binding proteins via domain and motif searches); SET6 is included as a predicted zinc-binding protein, the basis for the RCA zinc-ion-binding annotation.

PMID:37252976

The protein methylation network in yeast: A landmark in completeness for a eukaryotic post-translational modification.

Only five yeast methyltransferases are predicted to target proteins (Set3, Set4, Set6, Mtf1, YNL092W); of the plausibly active ones, Set6 is singled out as the most likely genuine protein methyltransferase because the SET domain invariably methylates proteins, while Set3/Set4 lack activity due to active-site substitutions.
Whatever Set6 methylates has not been identified; if it is a protein methyltransferase it most likely targets an as-yet undiscovered methylation site.

PMID:31642774

Using Yeast to Define the Regulatory Role of Protein Lysine Methylation.

Set5 and Set6 are homologous to the mammalian SMYD proteins, which have both histone and non-histone targets; the subcellular localization of Set6 is not yet known.

PMID:31685550

Function of the MYND Domain and C-Terminal Region in Regulating the Subcellular Localization and Catalytic Activity of the SMYD Family Lysine Methyltransferase Set5.

S. cerevisiae contains two SMYD proteins, Set5 and Set6, that share structural elements with the mammalian SMYD enzymes.

PMID:14718668

Chemogenomic profiling: identifying the functional interactions of small molecules in yeast.

Genome-wide heterozygous-deletion chemogenomic screen; the YPL165C/SET6 deletion is associated with resistance/sensitivity to compounds targeting ergosterol biosynthesis (fenpropimorph, dyclonine, alverine citrate). This is a fitness-profiling readout, not a molecular-function assay, and does not establish an enzymatic activity or a defined biological process for SET6.

file:yeast/SET6/SET6-bioinformatics/RESULTS.md

SET6 SET-domain integrity, SMYD-family and zinc-architecture analysis (this review)

Reproducible analysis: SET6 has a near-complete SET domain (hmmsearch vs Pfam PF00856, domain E=6.3e-14, residues 23-337, split-SET/SMYD architecture); the invariant catalytic/SAM-binding NHSC pocket (Asn303-His304-Ser305-Cys306) and C-terminal catalytic Tyr337 are intact, unlike the dead Set3/Set4 (Arg-Arg). Set5 is the closest yeast relative. SET6 is Cys-rich (17 Cys, 4.6%) in clusters consistent with SMYD-type zinc binding.