Structure, function and evolution of the bacterial DinG-like proteins.

The damage-inducible G (DinG)-like proteins represent a widespread superfamily 2 (SF2) of DNA helicases, exhibiting remarkable diversity in domain architecture, substrate specificity, regulatory mechanisms, biological functions, interaction partners, and taxonomic distribution. Many characterized DinG-like proteins play critical roles in bacterial stress responses and immunity, including the SOS response, DNA repair, and phage interference. This review aims to provide a summary of bacterial DinG-like proteins, categorizing them into subgroups such as DinG, YoaA, CasDinG, CasDinG-HNH, ExoDinG, pExoDinG, EndoDinG, RadC-like DinG, sDinG, and others. This classification provides an analysis of sequence-structure-function relationships within this superfamily. Further sequence clustering revealed inter-cluster relationships and subgroup heterogeneity, suggesting potential functional divergence. Integrating sequence analysis, domain architecture, structural data, and genomic context enabled functional predictions for these DinG-like protein subgroups, shedding light on their evolutionary and biological significance.