Putative Cu/Zn superoxide dismutase from the tardigrade Ramazzottius varieornatus, one of approximately 16 CuZnSOD paralogs in the expanded antioxidant gene family of this extremotolerant organism. Sequence analysis shows 66% identity to human SOD1 (the highest among the paralogs analyzed) and preserves all four Cu-binding histidines (H46, H48, H63, H120), the four Zn-binding residues (H63, H71, H80, D83), and both intrachain disulfide cysteines (C57, C146). This is consistent with canonical SOD activity, though functional confirmation is lacking. No gene symbol "RvSOD" number has been assigned in the primary literature (only RvSOD15 = RvY_13070 is explicitly mapped).
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004784 superoxide dismutase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Sequence conservation analysis (see file:RAMVA/RvY_13070/RvY_13070-bioinformatics/RESULTS.md) shows all four Cu-binding histidines, all four Zn-binding residues, and both disulfide cysteines are preserved. At 66% identity to human SOD1, this is the most conserved paralog analyzed. Canonical SOD activity is plausible but not experimentally verified. Note that Sim & Inoue (PMID:37358501) caution that some R. varieornatus SOD paralogs have subtle structural defects (electrostatic loop deletions, Ξ²3 sheet truncations) not detectable by primary sequence alone. Reason: All catalytic residues are preserved at the sequence level. Without biochemical data to contradict the family-based annotation, ACCEPT is appropriate, though the confidence is limited to sequence-level inference. Supporting Evidence: file:RAMVA/RvY_13070/RvY_13070-bioinformatics/RESULTS.md RvY_00651 | A0A1D1UKR0 | 154 | 4/4 | 4/4 | 2/2 | 66.0% | Likely functional |
| GO:0005507 copper ion binding | IEA GO_REF:0000002 | ACCEPT | Summary: All four canonical Cu-binding histidine residues are preserved in the sequence. Copper binding is very likely. |
| GO:0006801 superoxide metabolic process | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Redundant parent term of GO:0019430 (removal of superoxide radicals), which is the more specific and preferred annotation. Both are currently present. Reason: Technically correct but less informative than GO:0019430. Kept as non-core. |
| GO:0019430 removal of superoxide radicals | IEA GO_REF:0000108 | ACCEPT | Summary: This is the expected biological process for a canonical CuZnSOD and is inferred by logical reasoning from the enzymatic activity annotation. |
| GO:0046872 metal ion binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Parent term of the more specific GO:0005507 (copper ion binding) already annotated. Both copper and zinc binding are expected for this protein, but this generic parent term is less informative. Reason: Redundant with the more specific Cu/Zn binding annotations. Kept as non-core. |
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