*4.3. Assessing Structural Disorder of Linkers*

Structural disorder of processive enzymes was predicted by the IUPred algorithm [41], which is based on estimating the total pairwise inter-residue interaction energy gained upon folding of a polypeptide chain. The predictor returns a position-specific disorder score in the range 0.0–1.0, and a residue with score ≥0.5 is considered as locally disordered. To characterize the disorder tendency of domains and linkers, we calculated the ratio of disordered residues within the given region.

#### *4.4. Flexibility of Linker Regions*

To quantify the flexibility of linkers, we used DynaMine [45], a backbone dynamics predictor that has been trained on proteins for which NMR-based chemical shifts and experimental amide bond order parameters (S2) were available. Its score falls between 0.0 and 1.0, with a threshold 0.78 separating flexible (below) and rigid (above) regions. Residue-level DynaMine values were averaged for the entire sequence of linkers to calculate an overall measure of flexibility.
