Alignment of the amino acid sequences of TcAAD with other organism’s AADs, and its predicted 3-D structure. (A) Sequence alignment: TcAAD (this study), TvAAD (Trametes versicolor FP-101664 SS1, EIW61070), CcAAD (Coprinopsis cinerea okayama7#130, XP_002911316), PsAAD (Punctularia strigosozonata HHB-11173 SS5, EIN04988), ShAAD (Stereum hirsutum FP-91666 SS1, EIM87563), CnAAD (Cryptococcus neoformans var. neoformans JEC21, XP_567886), CvAAD (Coriolus versicolor, AB070838). Protein secondary structure was predicted by SWISS-MODEL program and represented as α-helices and β-strands. The triangle indicates putative active site. (B) The structural model of TcAAD was predicted based on the known crystal structure of a shaker family voltage-dependent potassium channels (Kv1) subunit beta-2 from Rattus norvegicus (PDB code: 3EAU) via SWISS-MODEL program. TcAAD (light white) and template (light yellow, PDB code: 3EAU) was shown using protein solid ribbons. TcADD belongs to the aldo-keto-reductases superfamily with catalytic tetrad, Asp62, Tyr67, Lys95, and His153, which are conserved as they are present in almost all members of the superfamily (NCBI AKR superfamily conserved domain search). His153 is one of the catalytic tetrad and is the putative active site.