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Marchler-Bauer, A., Bo, Y., Han, L., He, J., Lanczycki, C.J., Lu, S., Chitsaz, F., Derbyshire, M.K., Geer, R.C., Gonzales, N.R., et al. (2017) CDD/SPARCLE: Functional Classification of Proteins via Subfamily Domain Architectures. Nucleic Acids Research, 45, D200-D203.
https://doi.org/10.1093/nar/gkw1129

has been cited by the following article:

• TITLE: Structural and Functional Annotation of Hypothetical Protein of Fusobacterium nucleatum Strain MJR7757B: An in Silico Approach

  AUTHORS: Md. Isrfil Hossen, Fouzia Mostafa, Nusrat Jahan, Jannatul Ferdaus, Amgad Albahi, Sayed Mashequl Bari

  KEYWORDS: Fusobacterium nucleatum, In Silico, Bacteria, Hypothetical Protein, Molecular Docking

  JOURNAL NAME: Computational Molecular Bioscience, Vol.14 No.1, February 19, 2024

  ABSTRACT: Fusobacterium nucleatum is an anaerobic, commensal, gram-negative oral bacterium that is carcinogenic and causes a wide range of human diseases. The present study focused on the analysis of the hypothetical protein, HMPREF3221_01179, derived from F. nucleatum strain MJR7757B, employing various computational methods to anticipate both its structure and functional characteristics. NCBI conserved domain analysis, NCBI BLASTp and MEGA Phylogenetic tree study characterize the target protein as an outer membrane efflux protein (ToIC family) which facilitate the bacterial transmembrane transport. With a molecular weight of 52120.02 Da, an isoelectric point (pI) of 8.33, and an instability index of 29.47, the protein is anticipated to exhibit good solubility in the extracellular space and crucial stability for pharmaceutical applications. The protein’s structure meets quality standards during the construction and refinement of its 3D model. The efflux inhibitor Arginine beta-naphthylamide exhibits a significant binding affinity (-7.1 kcal/mol) to the binding site of the target protein. The in-silico analysis improves the understanding of the protein and facilitates future investigations into therapeutic medication.