Gene Ontology annotation through association of InterPro records with GO terms
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Combined Automated Annotation using Multiple IEA Methods
Bioinformatics analysis of Cu/Zn SOD paralogs in R. varieornatus
Structure of a superoxide dismutase from a tardigrade: Ramazzottius varieornatus strain YOKOZUNA-1.
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Crystal structures of RvSOD15 (PDB 7ypp WT 2.20 A; 7ypr V87H mutant 2.10 A) show an unusual T-shaped Cu coordination site with only three histidines (Val87 replaces a canonical His ligand) and Cu-water distances 2.6-3.4 A; V87H rescue does not restore canonical activity, supporting paralog-specific catalytic divergence in R. varieornatus Cu/Zn SODs.
Antioxidant Defense in the Toughest Animals on the Earth: Its Contribution to the Extreme Resistance of Tardigrades.
Deep research report on RvY_00650/A0A1D1UDY8 (Falcon/Edison Scientific Literature)
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A0A1D1UDY8 is annotated as a Cu/Zn SOD-family protein from R. varieornatus; no primary publication directly characterizes this specific accession, so functional inference relies on the Cu/Zn SOD family canonical mechanism plus direct evidence from the closely related paralog RvSOD15 (Sim 2023) and the 2024 tardigrade antioxidant defense review (Sadowska-Bartosz 2024).
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Combined with the existing bioinformatic verdict (PROSITE PS00087 fails despite preserved Cu histidines), the most defensible annotation is "Cu/Zn SOD-like protein; likely antioxidant superoxide dismutase activity, but paralog-specific divergence makes activity uncertain" - downstream annotations should be cautious and biochemical assay would be needed for definitive functional assignment.