Glutaredoxins (Grx) are small proteins, conserved throughout all the kingdoms of life, which are engaged in a wide variety of biological processes. According to the number of cysteines in their active site, Grx are classified as dithiolic or monothiolic (1-C-Grx). In most organisms, 1-C-Grx are implicated in iron-sulfur cluster (FeS) metabolism and utilize glutathione as cofactor. Trypanosomatids are parasitic protozoa of the order Kinetoplastida, which cause severe diseases in humans and domestic animals. These parasites exploit a unique thiol-dependent redox system based on bis(glutathionyl)spermidine (trypanothione) rather than on glutathione. Mitochondrial 1-C-Grx1 from trypanosomes differs from orthologues in several features including the use of trypanothione as ligand for FeS binding and the presence of a parasite-specific N-terminal extension. We have recently shown that 1-C-Grx1 from Trypanosoma brucei is indispensable for parasite survival in mouse, making this protein a potential drug target candidate against trypanosomiasis. However, structural information for the full-length form of 1-C-Grx1 is still lacking. Here, we report the NMR resonance assignment of the mature form of Tb1-C-Grx1 including an N-terminal tail, paving the way to disclose the role of this intrinsically disordered region in the protein function.