id: A0A6I8W8A2
gene_symbol: A0A6I8W8A2
taxon:
  id: NCBITaxon:46245
  label: Drosophila pseudoobscura pseudoobscura
status: COMPLETE
description: >-
  The 169-residue RCC1-like sequence does not contain a ligase catalytic module.
source_documents:
  - genes/DROPS/A0A6I8W8A2/A0A6I8W8A2-uniprot.txt
  - genes/DROPS/A0A6I8W8A2/A0A6I8W8A2-goa.tsv
  - genes/DROPS/A0A6I8W8A2/A0A6I8W8A2-hypotheses/prediction-ligase-activity/openscientist.md
predictions:
  - source_method: ProtNLM2
    source_version: UniProt 2024_06 pilot
    predicted_term:
      id: GO:0016874
      label: ligase activity
    predicted_term_type: GO_MF
    review:
      assessment: NPI
      error_type: DOMAIN_ARCHITECTURE_MISMATCH
      confidence_score: 0
      summary: >-
        The deposited sequence is a short RCC1-repeat protein with RCC1/BLIP-II fold assignments and no
        HECT or other ligase catalytic module. An RCC1 region from a larger HERC-like protein does not
        carry the catalytic activity of that protein's separate HECT domain. The prediction of intrinsic
        ligase activity is therefore incompatible with the available domain architecture. This assessment
        concerns the deposited sequence; it does not establish whether a longer gene model at the locus
        encodes a ligase.
      supported_by:
        - reference_id: file:DROPS/A0A6I8W8A2/A0A6I8W8A2-uniprot.txt
          supporting_text: >-
            ID   A0A6I8W8A2_DROPS        Unreviewed;       169 AA. ... DR   InterPro; IPR009091; RCC1/BLIP-II.
            ... DR   InterPro; IPR000408; Reg_chr_condens.
        - reference_id: file:DROPS/A0A6I8W8A2/A0A6I8W8A2-hypotheses/prediction-ligase-activity/openscientist.md
          supporting_text: none is a ligase catalytic signature
references:
  - id: file:DROPS/A0A6I8W8A2/A0A6I8W8A2-uniprot.txt
    title: A0A6I8W8A2-uniprot.txt
  - id: file:DROPS/A0A6I8W8A2/A0A6I8W8A2-hypotheses/prediction-ligase-activity/openscientist.md
    title: Focused OpenScientist report on A0A6I8W8A2 ligase prediction
    reference_review:
      relevance: HIGH
      review_notes: >-
        Substantive computational synthesis directly addressing the ligase prediction. The report's
        domain-architecture finding agrees with the cached UniProt InterPro/Pfam record: the deposited
        sequence has RCC1/BLIP-II and regulator-of-chromosome-condensation signatures but no HECT, RING,
        U-box, or other ligase catalytic module. The assessment applies to the current short deposited
        sequence and does not establish whether a longer locus-level gene model could encode a HECT-containing
        HERC-like ligase.