Substrate-recognition component of the SCF(Met30) complex, an E3 ubiquitin ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:9716410, PubMed:10637232, PubMed:14660673). Negatively regulates sulfur amino acids biosynthesis genes expression (PubMed:8524217, PubMed:15689486, PubMed:15870262). Controls cell cycle function (being required for the G1/S transition and M-phase but not the S-phase), sulfur metabolism, and methionine biosynthesis as part of the SCF(Met30) complex (PubMed:8524217, PubMed:15689486, PubMed:15870262). Required for the efficient binding of CDC45 and MCM proteins to origins of replication (PubMed:8524217, PubMed:15689486, PubMed:15870262). Required for efficient expression of G1 cyclins (PubMed:15870262). The SCF(Met30) complex catalyzes ubiquitination and degradation of the Cdk-inhibitory kinase SWE1 (PubMed:9716410). Involved in the S-adenosylmethionine (AdoMet)-mediated inhibition of the transcription function of MET4 (PubMed:8524217, PubMed:10637232). The SCF(Met30) complex mediates ubiquitination and subsequent degradation of MET4 and the cellular response to cadmium (PubMed:10637232). The SCF(Met30) complex acts as an inhibitor of autophagy by promoting ubiquitination and degradation of ATG9 in normal conditions (PubMed:33443148). Protein modification; protein ubiquitination. Homomultimer (PubMed:14660673). Interacts with CDC53 and SKP1/CBF3D to form the E3 ubiquitin ligase complex SCF(Met30) (PubMed:14660673, PubMed:9499404, PubMed:9716410, PubMed:33443148). Interacts with MET4 (PubMed:10637232, PubMed:15883825, PubMed:8524217). Transcriptional activation requires MET4 as well as MET31 and MET32. Regulated by intracellular AdoMet levels. L-methionine regulates the abundance of MET30. The amount of MET30 regulates the activity of the E3 ubiquitin ligase complex SCF(Met30). Present with 217 molecules/cell in log phase SD medium. Belongs to the WD repeat MET30/SCONB/SCON-2 family.