RvY_15948 is the copper chaperone (CCS homolog), not a SOD. H46->A and H48->C substitutions at the canonical Cu site are consistent with chaperone function. Matches Pfam SODC but neither PROSITE pattern.

Cu/Zn SOD-fold paralogs in R. varieornatus include both atypical SODs and chaperone-like proteins; the RvSOD15 structure (PDB 7ypp/7ypr) demonstrates that even paralogs retaining most canonical residues can be catalytically divergent, supporting careful annotation of fold-family paralogs as enzyme vs chaperone.

This 2024 review summarizes the expanded and diversified SOD repertoire in R. varieornatus, including atypical Cu/Zn SOD paralogs, supporting cautious annotation of SOD-fold proteins as catalytic enzymes versus chaperone-like paralogs when direct biochemical evidence is lacking.

Consistent with the bioinformatic verdict that RvY_15948 is a CCS-like copper chaperone (not a SOD), the deep research underscores that R. varieornatus encodes 17 SOD-fold genes spanning canonical SODs, atypical-active-site SODs, and likely chaperone paralogs; biochemical validation would be needed to definitively assign CCS-style copper-chaperone activity to RvY_15948.