PROSITE documentation PDOC51436Potyvirus NIa protease (NIa-pro) domain profile
Tobacco etch virus (TEV), tomato vein mottling virus (TVMV), and plum pox virus (PPV) are members of the Potyviridae family [E1]. The potyvirus genome is a (+) stranded RNA and is translated into a single polyprotein upon infection, which is processed by the virally encoded proteases P1, HC-Pro, and NIa. Most of the cleavage events are performed by NIa (nuclear inclusion protein a) protease (NIa-pro). NIa-pro processes seven sites present in the potyvirus polyprotein, named as A, B, C, D, V, E, and F. NIa-pros obtained from potyviruses have similar structures and functions. The potyvirus NIa-pro has a His-Asp-Cys catalytic triad, which is homologous to the trypsin-like proteases (see <PDOC00124>) except for Cys replacing Ser. NIa-pros obtained from potyviruses share certain sequence identities; however they recognize distinct amino acid sequences at each recognition sites. Consequently, they cannot recognize the cleavage sites of each other efficiently [1]. Nia-pro belongs to peptidase family C4 [E2]. In addition to the catalytic activity NIa-pro possesses also sequence non-specific RNA-binding activity and RNA polymerase (NIb) binding activity [3].
The potyvirus NIa protein contains the following two domains; the VPg domain at the N-terminus and the NIa-pro domain at the C-terminus [1,2]. The ~250-amino acid NIaPro domain adopts the characteristic two-domain antiparallel β-barrel fold that is the hallmark of trypsin-like serine proteases, with the catalytic triad residues His, Asp, and Cys located at the interface between domains (see <PDB:1LVM>) [3].
The profile we developed covers the entire potyvirus NIa-pro domain.
Last update:August 2011 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Zheng N. Perez J. de J. Zhang Z. Dominguez E. Garcia J.A. Xie Q. |
| Title | Specific and efficient cleavage of fusion proteins by recombinant plum pox virus NIa protease. | |
| Source | Protein Expr. Purif. 57:153-162(2008). | |
| PubMed ID | 18024078 | |
| DOI | 10.1016/j.pep.2007.10.008 |
| 2 | Authors | Daros J.-A. Carrington J.C. |
| Title | RNA binding activity of NIa proteinase of tobacco etch potyvirus. | |
| Source | Virology 237:327-336(1997). | |
| PubMed ID | 9356344 | |
| DOI | 10.1006/viro.1997.8802 |
| 3 | Authors | Phan J. Zdanov A. Evdokimov A.G. Tropea J.E. Peters H.K. III Kapust R.B. Li M. Wlodawer A. Waugh D.S. |
| Title | Structural basis for the substrate specificity of tobacco etch virus protease. | |
| Source | J. Biol. Chem. 277:50564-50572(2002). | |
| PubMed ID | 12377789 | |
| DOI | 10.1074/jbc.M207224200 |
| E1 | Title | https://viralzone.expasy.org/48?outline=all_by_species |
| E2 | Title | https://www.ebi.ac.uk/merops/cgi-bin/merops.cgi?id=C4 |
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