Fig. 1

Comparative analysis of human and trypanosomal XPF proteins. (A) Schematic representation of XPF proteins. Human domains were represented according to UniProtKB/SwissProt (Q92889.3). Human XPF has a helicase-like ___domain that lacks key residues essential for ATP binding and hydrolysis activity. T. brucei protein domains were identified using the InterPro protein signature databases. No significant similarity to the human helicase-like ___domain was found in TbXPF (B) Sequence alignment of T. brucei and human XPF nuclease domains. The XPF nuclease ___domain extends from amino acid 658 to 813 of human XPF. Residues in this ___domain involved in catalysis (*) and those associated with clinical phenotypes (▲) are indicated. Mutation R689S was found in patient FA104 associated to Fanconi anemia disorder; patient XP42RO with Xeroderma pigmentosum was homozygous for mutation R799W¹⁰. (C) Sequence alignment of helix hairpin helix (HhH) domains. Sequence alignment was generated using MultAlin⁵⁷ and the final format was obtained with ESPript⁵⁸. XPF protein sequences were retrieved from NCBI RefSeq: Homo sapiens (NP_005227.1); Trypanosoma brucei (XP_845037.1).