GO_REF:0000002

Gene Ontology annotation through association of InterPro records with GO terms

GO_REF:0000003

Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping

GO_REF:0000108

Automatic assignment of GO terms using logical inference, based on on inter-ontology links

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

file:RAMVA/RvY_13070/RvY_13070-bioinformatics/RESULTS.md

Bioinformatics analysis of Cu/Zn SOD paralogs in R. varieornatus

Bioinformatic verdict for RvY_17310: PROBABLY IMPAIRED. 475 aa (455 mature) - 3x larger than canonical CuZnSOD; SOD domain in C-terminus; all 4 Cu His preserved by sequence but PROSITE PS00087 fails

file:RAMVA/RvY_17310/RvY_17310-hypotheses/sod-activity-residue-geometry/openscientist.md

OpenScientist hypothesis run: RvY_17310 Cu/Zn-SOD active-site residues and geometry

Reaches the opposite reading to the local PROSITE-based analysis - all 10 active-site residues are conserved and the AlphaFold active-site geometry matches human SOD1 (high pLDDT, ~53% SOD-domain identity), so PS00087 failure is argued to be a signature-stringency artifact rather than loss of function. No direct enzyme assay; the catalytic call remains unresolved. (Its claim that paralog RvY_13431 is degenerate is not corroborated by repo data and is not relied on here.)

"10/10 critical active-site residues conserved in register and correctly spaced relative to human SOD1."

PMID:37358501

Structure of a superoxide dismutase from a tardigrade: Ramazzottius varieornatus strain YOKOZUNA-1.

Structural and biochemical work on the related paralog RvSOD15 shows atypical Cu coordination (Val replacing a histidine ligand) and impaired canonical activity, supporting the broader pattern of paralog-specific catalytic divergence among R. varieornatus Cu/Zn SODs.

PMID:39125965

Antioxidant Defense in the Toughest Animals on the Earth: Its Contribution to the Extreme Resistance of Tardigrades.

This 2024 review summarizes the expanded R. varieornatus SOD repertoire and highlights that some tardigrade Cu/Zn SOD paralogs are atypical and may have reduced or lost canonical SOD activity, supporting cautious annotation of RvY_17310 without direct biochemical evidence.

file:RAMVA/RvY_17310/RvY_17310-deep-research-falcon.md

Deep research report on RvY_17310 (Falcon/Edison Scientific Literature)

RvY_17310 is an unusually large (~475 aa, 3x canonical CuZnSOD) Cu/Zn SOD-fold protein from R. varieornatus with the SOD domain in the C-terminus; no primary publication directly characterizes this accession, so the most defensible annotation combines the family-level Cu/Zn SOD biology with the bioinformatic observation that PROSITE PS00087 fails despite preserved Cu histidines, plus the lineage-specific paralog divergence demonstrated for RvSOD15 (Sim 2023).