In nature, the mechanical properties of fibers based on -helical coiled-coil proteins, such as intermediate filament (IF)-proteins, are found between the soft and stretchable elastin and the highly tough and stiff dragline spider silks. Although spider silks have been the focus of many biomimetic studies in recent decades, the design of artificial IF-protein-based fibers has scarcely been studied. The work presented here demonstrates that the recombinant C. elegans (Ce-) lamin, type V IF-protein that constitutes a major component of the nuclear lamina, can be solubilized in and wet-spun into aqueous solutions to produce fibers with a toughness of 150±40 MJ/m3 and a stiffness of 8.4±1.5 GPa but without using chemical crosslinkers. Thus, the Ce-lamin is the first recombinant protein that simultaneously achieves the toughness and stiffness of natural dragline spider silks, the toughest fibers in nature. We posit that the source of the fiber’s stiffness and high toughness is a specific structural organization of Ce-lamin tetramers into paracrystal networks (typical Ce-lamin higher order structures). Raman analysis of drawn and non-drawn fibers showed that enrichment of -sheet structures during the long plastic deformation might be an additional factor for the high toughness. This work demonstrates that certain organizations of recombinant IF-proteins can result in fibers that exhibit outstanding mechanical properties, thus broadening the pool of fibrous proteins that can be used in functional materials across a diverse range of applications.