CG30287 is a predicted secreted S1-family serine endopeptidase with an intact annotated catalytic triad. The 284-residue product is also called SP224 and historically SPH37, but the latter name alone does not establish catalytic inactivity. Its physiological substrates and relationship to vertebrate PRSS55 remain unresolved.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004252 serine-type endopeptidase activity | IBA GO_REF:0000033 | ACCEPT | Summary: The exact sequence supports serine-endopeptidase activity. Reason: H82 D136 and S232 are retained at the annotated catalytic sites in the S1 domain. The historical SPH37 alias is insufficient to call it a pseudoenzyme. Supporting Evidence: file:DROME/CG30287/CG30287-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG30287/CG30287-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG30287/CG30287-uniprot.txt FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG30287/CG30287-uniprot.txt FT DOMAIN 42..282 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 sequence-supported. Reason: The exact record has an intact annotated H-D-S catalytic triad and a complete S1 domain, supporting the existing broad activity mapping. Supporting Evidence: file:DROME/CG30287/CG30287-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG30287/CG30287-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG30287/CG30287-uniprot.txt FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG30287/CG30287-uniprot.txt FT DOMAIN 42..282 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 sequence-based classification is coherent with catalytic architecture. Reason: PMID:30367934 distinguishes SPs from SPHs using catalytic-residue conservation. The exact sequence has H82 D136 S232 at the annotated sites, supporting proteolytic potential despite older SPH naming. Supporting Evidence: file:DROME/CG30287/CG30287-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG30287/CG30287-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG30287/CG30287-uniprot.txt FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG30287/CG30287-uniprot.txt FT DOMAIN 42..282 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 compatible with the sequence. Reason: A SignalP signal peptide at residues 1-21 and a soluble mature S1-domain architecture support the curated IBA. Supporting Evidence: file:DROME/CG30287/CG30287-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG30287/CG30287-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG30287/CG30287-uniprot.txt FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG30287/CG30287-uniprot.txt FT DOMAIN 42..282 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 supported at a broad level. Reason: The catalytic triad is retained in the S1 domain; no specific physiological substrate is established. Supporting Evidence: file:DROME/CG30287/CG30287-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG30287/CG30287-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG30287/CG30287-uniprot.txt FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG30287/CG30287-uniprot.txt FT DOMAIN 42..282 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: Domain-based proteolysis inference is biologically reasonable. Reason: The annotated H-D-S residues are present and no loss-of-catalysis conclusion follows from the historical SPH37 alias. Supporting Evidence: file:DROME/CG30287/CG30287-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG30287/CG30287-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG30287/CG30287-uniprot.txt FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG30287/CG30287-uniprot.txt FT DOMAIN 42..282 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: Serine-type endopeptidase activity is more specific. Reason: The intact S1 catalytic architecture supports the more informative peptidase class. Proposed replacements: serine-type endopeptidase activity Supporting Evidence: file:DROME/CG30287/CG30287-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG30287/CG30287-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG30287/CG30287-uniprot.txt FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG30287/CG30287-uniprot.txt FT DOMAIN 42..282 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 mapping can be made specific. Reason: The exact domain and catalytic residues support serine-type endopeptidase activity. Proposed replacements: serine-type endopeptidase activity Supporting Evidence: file:DROME/CG30287/CG30287-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG30287/CG30287-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG30287/CG30287-uniprot.txt FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG30287/CG30287-uniprot.txt FT DOMAIN 42..282 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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