Claim · model-written summary
The secondary structure of SlMOB proteins was mainly composed of alpha-helix.
- Outcome
- secondary structure was mainly composed of α-helixe0
Not reportedTaxonMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValueQualifier
Verbatim
e0“The secondary structure was mainly composed of α-helix”
Title
Genome-Scale Bioinformatic Analysis of Mob-Like Proteins in Tomato
Xinyu Na; Yibing Wang; Li Li; et al. Biotechnology Journal International 2026. doi:10.9734/bji/2026/v30i1823
Other claims from this paper (8)
- Observation The tomato SlMOB protein family has three members.
- Observation All three SlMOB proteins contain 215 amino acids.
- Observation SlMOB proteins have no transmembrane regions or signal peptides.
- Observation SlMOB proteins were localized in the cytoplasm and nucleus.
- Observation All SlMOB family members contained the conserved Mob1_phocein domain.
- Observation 3D models of all SlMOB proteins built with 5twg.1.A as template showed high evolutionary conservation.
- Observation Proteins interacting with SlMOB family members mainly included serine/threonine protein kinase 38-like, kinase 39-like and other kinases involved in signal transduction and cell cycle regulation.
- Observation Tomato SlMOB proteins had a close evolutionary relationship with Camellia sinensis MOB proteins.