Wss1 is a nuclear Wss1-like metalloprotease with a conserved WLM catalytic domain and a C-terminal SUMO-interaction motif. Its role in proteolytic repair of covalent DNA-protein cross-links is inferred from the characterized budding-yeast Wss1 family and curated phylogenetic evidence. Removal of the cross-linked protein allows downstream DNA repair or lesion bypass. Direct biochemical characterization of the fission-yeast protein remains limited.
Summary: The target carries the diagnostic WLM domain and conserved metal-binding/catalytic residues.
Reason: The target carries the diagnostic WLM domain and conserved metal-binding/catalytic residues. Curated orthology and PAINT ancestry support inheritance of the Wss1 protease/DNA-repair function, whose mechanistic foundation is DNA-dependent proteolysis of cross-linked proteins in the characterized yeast homolog. This is a justified family inference, not target-specific experimental proof.
HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ...
ACCEPT
Summary: Nuclear localization is supported by the reviewed record citing target localization measurements (PMID:16823372) and is consistent with conserved Wss1 action on DNA-protein cross-links.
Reason: Nuclear localization is supported by the reviewed record citing target localization measurements (PMID:16823372) and is consistent with conserved Wss1 action on DNA-protein cross-links. The IBA adds a curated ancestral localization inference.
Supporting Evidence:
file:SCHPO/wss1/wss1-uniprot.txt
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
Summary: Nuclear localization is supported by the reviewed record citing target localization measurements (PMID:16823372) and is consistent with conserved Wss1 action on DNA-protein cross-links.
Reason: Nuclear localization is supported by the reviewed record citing target localization measurements (PMID:16823372) and is consistent with conserved Wss1 action on DNA-protein cross-links. The IBA adds a curated ancestral localization inference.
Supporting Evidence:
file:SCHPO/wss1/wss1-uniprot.txt
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
Summary: Nuclear localization is supported by the reviewed record citing target localization measurements (PMID:16823372) and is consistent with conserved Wss1 action on DNA-protein cross-links.
Reason: Nuclear localization is supported by the reviewed record citing target localization measurements (PMID:16823372) and is consistent with conserved Wss1 action on DNA-protein cross-links. The IBA adds a curated ancestral localization inference.
Supporting Evidence:
file:SCHPO/wss1/wss1-uniprot.txt
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
Summary: The target carries the diagnostic WLM domain and conserved metal-binding/catalytic residues.
Reason: The target carries the diagnostic WLM domain and conserved metal-binding/catalytic residues. Curated orthology and PAINT ancestry support inheritance of the Wss1 protease/DNA-repair function, whose mechanistic foundation is DNA-dependent proteolysis of cross-linked proteins in the characterized yeast homolog. This is a justified family inference, not target-specific experimental proof.
Summary: The target carries the diagnostic WLM domain and conserved metal-binding/catalytic residues.
Reason: The target carries the diagnostic WLM domain and conserved metal-binding/catalytic residues. Curated orthology and PAINT ancestry support inheritance of the Wss1 protease/DNA-repair function, whose mechanistic foundation is DNA-dependent proteolysis of cross-linked proteins in the characterized yeast homolog. This is a justified family inference, not target-specific experimental proof.
Summary: Wss1-mediated proteolytic removal of DNA-cross-linked proteins can permit downstream lesion bypass; participation in translesion synthesis does not assert that Wss1 is a DNA polymerase.
Reason: Wss1-mediated proteolytic removal of DNA-cross-linked proteins can permit downstream lesion bypass; participation in translesion synthesis does not assert that Wss1 is a DNA polymerase. Retain the curated orthology inference at that pathway-participation scope.
Summary: The target carries the diagnostic WLM domain and conserved metal-binding/catalytic residues.
Reason: The target carries the diagnostic WLM domain and conserved metal-binding/catalytic residues. Curated orthology and PAINT ancestry support inheritance of the Wss1 protease/DNA-repair function, whose mechanistic foundation is DNA-dependent proteolysis of cross-linked proteins in the characterized yeast homolog. This is a justified family inference, not target-specific experimental proof.
Q: Does Wss1 associate with any nuclear membrane or membrane-bound complex, or is its nuclear signal restricted to soluble chromatin-associated pools?
External Prediction Reviews
These computational predictions are reviewed separately from the GOA annotation set used for this review. The assessments below are from this project and do not constitute official GO annotations or endorsement by GO/UniProt. They are not included in the existing annotation review above.
Review rationale: The reviewed target record places Wss1 in the nucleus and identifies a soluble WLM metalloprotease domain; it does not establish membrane residence. The original XML hydrates the membrane claim from KW-0539, which is the UniProt keyword Nucleus, not a membrane-specific observation. Nuclear residence alone does not entail association with the nuclear envelope, and the family DNA-protein-crosslink repair mechanism does not require a membrane. Nevertheless, lack of a transmembrane helix would not exclude peripheral membrane association, so the broad claim cannot be conclusively refuted solely from these data. Direct membrane fractionation, colocalization or an established membrane-associated complex is missing.