RvY_10893

id: A0A1D1VE88
gene_symbol: RvY_10893
product_type: PROTEIN
status: IN_PROGRESS
taxon:
  id: NCBITaxon:947166
  label: Ramazzottius varieornatus
description: >-
  Putative Cu/Zn superoxide dismutase paralog from R. varieornatus, one of approximately 10 CuZnSOD-family proteins encoded by this extremotolerant tardigrade. Bioinformatic analysis (file:RAMVA/RvY_13070/RvY_13070-bioinformatics/RESULTS.md) shows that all four canonical Cu-binding histidines, all four Zn-binding residues, and both intrachain disulfide cysteines are preserved at the sequence level. The protein matches both PROSITE Cu/Zn SOD signatures (PS00087 for the N-terminal Cu coordination loop and PS00332 for the C-terminal disulfide region), as well as the Pfam SODC family (PF00080). This is consistent with canonical Cu/Zn superoxide dismutase activity, although biochemical confirmation has not been published for this specific paralog. 185 aa (166 mature); all residues and PROSITE patterns match canonical CuZnSOD
existing_annotations:
- term:
    id: GO:0004784
    label: superoxide dismutase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  review:
    summary: >-
      All catalytic residues (4 Cu His, 4 Zn ligands, 2 disulfide Cys) are preserved at the sequence level. PROSITE PS00087 (N-terminal Cu coordination signature) and PS00332 (C-terminal disulfide signature) both match. The protein is in Pfam family PF00080 (Sod_Cu). Canonical SOD activity is plausible based on sequence and motif analysis, though biochemical data are lacking for this specific paralog. ACCEPT with the caveat that confidence is limited to sequence-level inference.
    action: ACCEPT
    reason: >-
      All sequence-level criteria for canonical CuZnSOD are met.
    supported_by:
      - reference_id: file:RAMVA/RvY_13070/RvY_13070-bioinformatics/RESULTS.md
        supporting_text: >-
          RvY_10893 | A0A1D1VE88 | bioinformatic verdict: FUNCTIONAL
- term:
    id: GO:0005507
    label: copper ion binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  review:
    summary: >-
      All four canonical Cu-binding histidines are preserved at the sequence level. Copper binding is likely.
    action: ACCEPT
- term:
    id: GO:0006801
    label: superoxide metabolic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  review:
    summary: >-
      Inferred from SOD activity annotation.
    action: ACCEPT
- term:
    id: GO:0019430
    label: removal of superoxide radicals
  evidence_type: IEA
  original_reference_id: GO_REF:0000108
  review:
    summary: >-
      Inferred from SOD activity annotation.
    action: ACCEPT
- term:
    id: GO:0046872
    label: metal ion binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  review:
    summary: >-
      Parent term of the more specific Cu/Zn binding annotations. Both Cu and Zn binding are likely.
    action: KEEP_AS_NON_CORE
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO
    terms
  findings: []
- id: GO_REF:0000108
  title: Automatic assignment of GO terms using logical inference, based on on inter-ontology
    links
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: file:RAMVA/RvY_13070/RvY_13070-bioinformatics/RESULTS.md
  title: Bioinformatics analysis of Cu/Zn SOD paralogs in R. varieornatus
  findings:
  - statement: "Bioinformatic verdict for RvY_10893: FUNCTIONAL. 185 aa (166 mature); all residues and PROSITE patterns match canonical CuZnSOD"