CG43742 is a secretory serine-protease-family protein with tandem protease and protease-like domains. Its first domain retains the annotated histidine-aspartate-serine catalytic triad, supporting proteolytic potential; substrate specificity and physiological substrates remain unresolved. It is distinct from the clip-domain protease Snake.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003674 molecular_function | ND GO_REF:0000015 | MODIFY | Summary: Broad serine-endopeptidase activity is supported more specifically than the unknown-function placeholder. Reason: The exact sequence retains the annotated H73 D121 S207 triad in the N-terminal protease domain. PMID:30367934 classifies SP251 as a tandem PD/PLD protein; this supports generic catalytic potential without specifying a substrate. Proposed replacements: serine-type endopeptidase activity Supporting Evidence: file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG43742/CG43742-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG43742/CG43742-uniprot.txt FT DOMAIN 35..258 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" |
| GO:0004252 serine-type endopeptidase activity | IEA GO_REF:0000120 | ACCEPT | Summary: The N-terminal domain supports serine-type endopeptidase activity. Reason: The retained annotated H73 D121 S207 triad and intact S1 domain support broad serine proteolysis. The C-terminal protease-like domain does not imply that both domains are catalytic. Supporting Evidence: file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG43742/CG43742-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG43742/CG43742-uniprot.txt FT DOMAIN 35..258 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" PMID:30367934 SP49, SP77, SP222, SP248, and SP251 contain a PD and a PLD; 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 SP251 classification supports proteolytic potential. Reason: PMID:30367934 explicitly places SP251 among proteins with a protease domain and a protease-like domain. This is comparative sequence evidence rather than a substrate assay; the exact source sequence retains the first-domain triad. Supporting Evidence: file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG43742/CG43742-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG43742/CG43742-uniprot.txt FT DOMAIN 35..258 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" PMID:30367934 SP49, SP77, SP222, SP248, and SP251 contain a PD and a PLD; 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:0005575 cellular_component | ND GO_REF:0000015 | MODIFY | Summary: Secretory architecture supports extracellular localization. Reason: The N-terminal SignalP feature at residues 1-20 supports entry into the secretory pathway and the mature protein lacks a retained transmembrane segment; extracellular localization is consistent with the IBA. Proposed replacements: extracellular region Supporting Evidence: file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG43742/CG43742-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG43742/CG43742-uniprot.txt FT DOMAIN 35..258 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" |
| GO:0005576 extracellular region | IBA GO_REF:0000033 | ACCEPT | Summary: Extracellular localization is supported by architecture and phylogenetic inference. Reason: The signal peptide and soluble tandem protease-domain architecture support the existing curated IBA extracellular annotation. Supporting Evidence: file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG43742/CG43742-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG43742/CG43742-uniprot.txt FT DOMAIN 35..258 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" PMID:30367934 SP49, SP77, SP222, SP248, and SP251 contain a PD and a PLD; 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: Proteolysis is the plausible core biochemical process. Reason: The first S1 domain retains the annotated H-D-S triad and the second is protease-like. Broad proteolysis is supported without specifying cleavage targets or a developmental cascade. Supporting Evidence: file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG43742/CG43742-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG43742/CG43742-uniprot.txt FT DOMAIN 35..258 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" PMID:30367934 SP49, SP77, SP222, SP248, and SP251 contain a PD and a PLD; 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:0008150 biological_process | ND GO_REF:0000015 | MODIFY | Summary: Proteolytic participation is supported more specifically than the unknown-process placeholder. Reason: The intact first-domain catalytic triad supports generic proteolysis; physiological substrate and context remain unresolved. Proposed replacements: proteolysis Supporting Evidence: file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG43742/CG43742-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG43742/CG43742-uniprot.txt FT DOMAIN 35..258 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" |
| GO:0008233 peptidase activity | IEA GO_REF:0000104 | MODIFY | Summary: Serine-type endopeptidase activity is more specific than peptidase activity. Reason: The S1 catalytic architecture supports the existing serine-type endopeptidase term. Proposed replacements: serine-type endopeptidase activity Supporting Evidence: file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG43742/CG43742-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG43742/CG43742-uniprot.txt FT DOMAIN 35..258 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" PMID:30367934 SP49, SP77, SP222, SP248, and SP251 contain a PD and a PLD; 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: Serine-type endopeptidase activity is more informative than hydrolase activity. Reason: The first S1 domain and retained catalytic triad support the specific peptidase class rather than a generic hydrolase label. Proposed replacements: serine-type endopeptidase activity Supporting Evidence: file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG43742/CG43742-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG43742/CG43742-uniprot.txt FT DOMAIN 35..258 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" PMID:30367934 SP49, SP77, SP222, SP248, and SP251 contain a PD and a PLD; 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:0045087 innate immune response | IBA GO_REF:0000033 | UNDECIDED | Summary: A specific immune role is unresolved despite extracellular protease architecture. Reason: The IBA is a curated phylogenetic hypothesis; the exact target is SP251 rather than Snake and tandem PD/PLD architecture alone does not identify an immune cascade or substrate. The relevant ancestral immune assertion requires inspection. Supporting Evidence: file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG43742/CG43742-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG43742/CG43742-uniprot.txt FT DOMAIN 35..258 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" PMID:30367934 SP49, SP77, SP222, SP248, and SP251 contain a PD and a PLD; 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:0051604 protein maturation | IEA GO_REF:0000117 | UNDECIDED | Summary: Protein maturation is more specific than generic proteolysis. Reason: The source sequence supports serine protease potential but no physiological maturation substrate or activation cascade is established for CG43742. Supporting Evidence: file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR009003; Peptidase_S1_PA. file:DROME/CG43742/CG43742-uniprot.txt DR InterPro; IPR001314; Peptidase_S1A. file:DROME/CG43742/CG43742-uniprot.txt FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" file:DROME/CG43742/CG43742-uniprot.txt FT DOMAIN 35..258 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" PMID:30367934 SP49, SP77, SP222, SP248, and SP251 contain a PD and a PLD; 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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