CG17404 is a predicted secreted S1-family serine endopeptidase also known as SP149. Its catalytic histidine-aspartate-serine triad is retained, supporting proteolytic potential. Chymotrypsin-like substrate preference and specific equivalence to mammalian CTRL remain unresolved.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004252 serine-type endopeptidase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Serine-endopeptidase activity is supported by the exact architecture. Reason: The S1 domain retains annotated H80 D124 S225, consistent with the existing phylogenetic activity inference. Supporting Evidence: file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG17404/CG17404-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG17404/CG17404-uniprot.txt FT DOMAIN 35..274 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: Broad serine-protease activity is supported independently of the name. Reason: The exact catalytic residues are retained; the narrower chymotrypsin name is not required to justify GO:0004252. Supporting Evidence: file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG17404/CG17404-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG17404/CG17404-uniprot.txt FT DOMAIN 35..274 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:12568721 Serine proteases and their homologs in the Drosophila melano... | ACCEPT | Summary: The older sequence classification supports the broad protease class. Reason: PMID:12568721 is a comparative Drosophila SP/SPH analysis. Its abstract does not establish substrate specificity; the exact record independently retains the annotated catalytic H-D-S residues. Supporting Evidence: file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG17404/CG17404-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG17404/CG17404-uniprot.txt FT DOMAIN 35..274 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 updated SP/SPH analysis is coherent with the exact sequence. Reason: PMID:30367934 separates catalytic proteases from homologs by H-D-S conservation. The annotated catalytic sites in the target retain all three residue types. Supporting Evidence: file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG17404/CG17404-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG17404/CG17404-uniprot.txt FT DOMAIN 35..274 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: A SignalP signal peptide at residues 1-20 and a soluble S1-domain architecture support the curated IBA location. Supporting Evidence: file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG17404/CG17404-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG17404/CG17404-uniprot.txt FT DOMAIN 35..274 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: Broad proteolysis is a reasonable core process. Reason: The intact catalytic triad supports proteolytic potential without identifying a substrate or tissue-specific pathway. Supporting Evidence: file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG17404/CG17404-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG17404/CG17404-uniprot.txt FT DOMAIN 35..274 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-process mapping is sound at this level. Reason: The exact S1 domain retains annotated catalytic residues rather than merely a protease-like fold. Supporting Evidence: file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG17404/CG17404-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG17404/CG17404-uniprot.txt FT DOMAIN 35..274 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 | ISM PMID:12568721 Serine proteases and their homologs in the Drosophila melano... | ACCEPT | Summary: Comparative sequence evidence supports broad proteolysis. Reason: PMID:12568721 provides an SP/SPH classification framework and the exact target retains its annotated H-D-S catalytic triad; this is inferential evidence rather than a substrate assay. Supporting Evidence: file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG17404/CG17404-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG17404/CG17404-uniprot.txt FT DOMAIN 35..274 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 term gives the supported specificity. Reason: S1 architecture with annotated catalytic H80 D124 S225 supports the specific enzyme class. Proposed replacements: serine-type endopeptidase activity Supporting Evidence: file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG17404/CG17404-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG17404/CG17404-uniprot.txt FT DOMAIN 35..274 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: Generic hydrolase activity is less informative than the supported enzyme class. Reason: The S1 catalytic architecture supports serine-type endopeptidase activity. Proposed replacements: serine-type endopeptidase activity Supporting Evidence: file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG17404/CG17404-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG17404/CG17404-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG17404/CG17404-uniprot.txt FT DOMAIN 35..274 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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