serinproteins

Serinproteins refer to a proposed superfamily of proteins defined by the presence of a serine-containing motif thought to participate in catalysis or substrate recognition. The name derives from the prominent role of serine residues in the functional chemistry of these proteins. Members are diverse and include enzymes with proteolytic or transferase-like activities as well as non-enzymatic binders that use a serine residue to engage substrates or regulate activity. The defining features vary among families, but many serinproteins rely on a catalytic serine installed in a conserved motif and, in some subgroups, on a catalytic triad consisting of serine, histidine, and aspartate.

Structural data show considerable variety; some serinproteins adopt classic serine protease–like folds, while others display distinct alpha/beta architectures. Motifs containing serine residues near the active site or substrate-binding loops are commonly used to classify members.

Taxonomically, serinproteins are reported across bacteria, archaea, and eukaryotes, indicating broad distribution. Evolutionary analyses point to multiple independent origins and extensive domain shuffling, yielding considerable functional diversity within the superfamily.

In research contexts, serinproteins are investigated for insights into serine-based chemistry and for potential biotechnological applications, including digestion of substrates, peptide processing, and metabolic regulation. The term, however, is variably defined, and different databases may group serinproteins differently or under related enzyme families such as serine hydrolases or serine proteases, depending on interpretation of motifs and folds.