CG30288 is a predicted secreted S1-family serine endopeptidase. Its 282-residue sequence has an N-terminal signal peptide and retains the annotated histidine-aspartate-serine catalytic triad. Proteolytic potential is supported, while its preferred substrate and physiological role remain unresolved.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004252 serine-type endopeptidase activity | IBA GO_REF:0000033 | ACCEPT | Summary: S1 serine-endopeptidase activity is supported. Reason: The exact sequence contains the annotated H83 D132 S225 triad in its S1 domain; the IBA is consistent with this intact catalytic architecture. Supporting Evidence: file:DROME/CG30288/CG30288-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG30288/CG30288-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG30288/CG30288-uniprot.txt FT SIGNAL 1..23 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG30288/CG30288-uniprot.txt FT DOMAIN 43..275 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" PMID:30367934 The SP-related sequences in each species were divided into SPs or SPHs based on the presence or absence of the His-Asp-Ser catalytic triad |
| GO:0004252 serine-type endopeptidase activity | IEA GO_REF:0000120 | ACCEPT | Summary: The broad serine-protease class fits the sequence. Reason: PROSITE identifies an S1 domain with the retained annotated catalytic residues H83 D132 S225. This does not establish the narrower chymotrypsin substrate preference. Supporting Evidence: file:DROME/CG30288/CG30288-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG30288/CG30288-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG30288/CG30288-uniprot.txt FT SIGNAL 1..23 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG30288/CG30288-uniprot.txt FT DOMAIN 43..275 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" PMID:30367934 The SP-related sequences in each species were divided into SPs or SPHs based on the presence or absence of the His-Asp-Ser catalytic triad |
| GO:0004252 serine-type endopeptidase activity | ISM PMID:30367934 Building a platform for predicting functions of serine prote... | ACCEPT | Summary: The sequence-based activity classification is coherent with the exact record. Reason: PMID:30367934 classifies Drosophila serine proteases using the H-D-S triad and gene models. The exact source retains the annotated catalytic triad; no biochemical substrate specificity is inferred. Supporting Evidence: file:DROME/CG30288/CG30288-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG30288/CG30288-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG30288/CG30288-uniprot.txt FT SIGNAL 1..23 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG30288/CG30288-uniprot.txt FT DOMAIN 43..275 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" PMID:30367934 The SP-related sequences in each species were divided into SPs or SPHs based on the presence or absence of the His-Asp-Ser catalytic triad |
| GO:0005576 extracellular region | IBA GO_REF:0000033 | ACCEPT | Summary: Extracellular localization is supported. Reason: SignalP predicts a cleavable signal peptide at residues 1-23 and no retained transmembrane segment is annotated. This architecture supports the curated IBA extracellular location. Supporting Evidence: file:DROME/CG30288/CG30288-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG30288/CG30288-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG30288/CG30288-uniprot.txt FT SIGNAL 1..23 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG30288/CG30288-uniprot.txt FT DOMAIN 43..275 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" PMID:30367934 The SP-related sequences in each species were divided into SPs or SPHs based on the presence or absence of the His-Asp-Ser catalytic triad |
| GO:0006508 proteolysis | IBA GO_REF:0000033 | ACCEPT | Summary: Proteolysis is a coherent core process. Reason: The intact S1 catalytic architecture supports broad proteolysis; the physiological substrate and tissue context remain unknown. Supporting Evidence: file:DROME/CG30288/CG30288-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG30288/CG30288-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG30288/CG30288-uniprot.txt FT SIGNAL 1..23 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG30288/CG30288-uniprot.txt FT DOMAIN 43..275 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" PMID:30367934 The SP-related sequences in each species were divided into SPs or SPHs based on the presence or absence of the His-Asp-Ser catalytic triad |
| GO:0006508 proteolysis | IEA GO_REF:0000002 | ACCEPT | Summary: The domain-to-proteolysis mapping is biologically reasonable. Reason: A retained H-D-S triad supports a catalytic rather than merely fold-homologous S1 protein. Supporting Evidence: file:DROME/CG30288/CG30288-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG30288/CG30288-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG30288/CG30288-uniprot.txt FT SIGNAL 1..23 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG30288/CG30288-uniprot.txt FT DOMAIN 43..275 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" PMID:30367934 The SP-related sequences in each species were divided into SPs or SPHs based on the presence or absence of the His-Asp-Ser catalytic triad |
| GO:0008233 peptidase activity | IEA GO_REF:0000104 | MODIFY | Summary: The serine-endopeptidase class is more informative. Reason: The S1 domain and annotated H-D-S triad support serine-type endopeptidase activity. Proposed replacements: serine-type endopeptidase activity Supporting Evidence: file:DROME/CG30288/CG30288-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG30288/CG30288-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG30288/CG30288-uniprot.txt FT SIGNAL 1..23 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG30288/CG30288-uniprot.txt FT DOMAIN 43..275 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" PMID:30367934 The SP-related sequences in each species were divided into SPs or SPHs based on the presence or absence of the His-Asp-Ser catalytic triad |
| GO:0016787 hydrolase activity | IEA GO_REF:0000104 | MODIFY | Summary: The generic hydrolase term can be made specific. Reason: S1 catalytic architecture supports serine-type endopeptidase activity. Proposed replacements: serine-type endopeptidase activity Supporting Evidence: file:DROME/CG30288/CG30288-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG30288/CG30288-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG30288/CG30288-uniprot.txt FT SIGNAL 1..23 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG30288/CG30288-uniprot.txt FT DOMAIN 43..275 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" PMID:30367934 The SP-related sequences in each species were divided into SPs or SPHs based on the presence or absence of the His-Asp-Ser catalytic triad |
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