Bivalency has evolved as a natural strategy for enhancing the binding strength of protein-protein interactions. Although bivalent antibodies readily occur in nature, engineering bivalent peptides has had limited success, indicating an incomplete understanding of this property. The discovery of several bivalent venom peptides, each containing two homologous and independently folded domains arranged in a tandem repeat architecture, offers a unique opportunity to comprehensively grasp the underlying design principles of bivalency and the emergence of natural bivalent ligands. In previous work, we categorized these bivalent venom peptides into a broader class known as secreted cysteine-rich repeat-proteins (SCREPs). Here, we introduce an online resource called ScrepYard, intended to aid researchers in exploring recognized SCREP sequences of interest and facilitating the characterization of this emerging biomolecular class. ScrepYard compiles information about SCREP component domains, architecture, and taxonomy. Analyzing entries within ScrepYard unveils the prevalence and divergence of SCREPs. These analyses also suggests that ScrepYard might contain entries exhibiting remarkable properties that could position SCREPs as promising drug leads and molecular probes. ScrepYard serves as a valuable tool not only to enhance our understanding of bivalency but also as a useful resource for mining bioactive peptides.