Zinc finger protein (ZPR1) is a eukaryotic protein that comprises tandem ZPR1 domains and which, in response to growth stimuli, binds to eukaryotic translation elongation factor 1A (eEF1A), assembles into multiprotein complexes with the survival motor neurons (SMN) protein, and accumulates in subnuclear structures, such as gems and Cajal bodies. ZPR1 has a conserved tandem architecture consisting of a duplicated module, the ZPR1 domain, comprised of two apparently modular domains: an elongation initiation factor 2-like zinc finger (ZnF) and a double-stranded beta helix with a helical hairpin insertion (A/B domain). In consequence, the N- and C-terminal ZPR1 domains are referred to as the ZnF1-A domain and ZnF2-B domain modules, respectively. The ZnF2-B domain module is required for viability, whilst the ZnF1-A domain module is required for normal cell growth and proliferation .

Structural domains comprising this superfamily share the structure of the A/B domain found within the ZPR1 domain PMID:17704259.