The dataset of predicted trypsin serine peptidases and their inactive homologs in Tenebrio molitor transcriptomes
Nikita I. Zhiganov,
Valeriia F. Tereshchenkova,
Brenda Oppert,
Irina Y. Filippova,
Nataliya V. Belyaeva,
Yakov E. Dunaevsky,
Mikhail A. Belozersky,
Elena N. Elpidina
Affiliations
Nikita I. Zhiganov
Division of Entomology, Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia
Valeriia F. Tereshchenkova
Division of Natural Compounds, Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia
Brenda Oppert
USDA Agricultural Research Service, Center for Grain and Animal Health Research, Manhattan, KS 66502, USA
Irina Y. Filippova
Division of Natural Compounds, Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia
Nataliya V. Belyaeva
Division of Entomology, Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia
Yakov E. Dunaevsky
Department of Plant Proteins, A.N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia
Mikhail A. Belozersky
Department of Plant Proteins, A.N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia
Elena N. Elpidina
Department of Plant Proteins, A.N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia; Corresponding author.
Tenebrio molitor is an important coleopteran model insect and agricultural pest from the Tenebrionidae family. We used RNA-Seq transcriptome data from T. molitor to annotate trypsin-like sequences from the chymotrypsin S1 family of serine peptidases, including sequences of active serine peptidases (SerP) and their inactive homologs (SerPH) in T. molitor transcriptomes. A total of 63 S1 family tryspin-like serine peptidase sequences were de novo assembled. Among the sequences, 58 were predicted to be active trypsins and five inactive SerPH. The length of preproenzyme and mature form of the predicted enzyme, position of signal peptide and proenzyme cleavage sites, molecular mass, active site and S1 substrate binding subsite residues, and transmembrane and regulatory domains were analyzed using bioinformatic tools. The data can be used for further physiological, biochemical, and phylogenetic study of tenebrionid pests and other animal systems.
