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PROSITE documentation PDOC51493

Arterivirus nsp4 proteinase domain profile





Description

Arteriviruses are enveloped, positive-stranded RNA viruses and include pathogens of major economic concern to the swine- and horse-breeding industries [E1]:

  - Equine arteritis virus (EAV).
  - Porcine reproductive and respiratory syndrome virus (PRRSV).
  - Mice actate dehydrogenase-elevating virus.
  - Simian hemorrhagic fever virus.

The arterivirus replicase gene encodes two large precursor polyproteins that are processed by the viral main proteinase nonstructural protein 4 (nsp4). The structure of the enzyme reveals two chymotrypsin-like antiparallel β-barrels and an extra C-terminal α/β domain that may play a role in mediating protein-protein interactions (see <PDB:1MBM; A>). The N-terminal barrel consists of six β-strands (A1 to F1), while the C-terminal barrel is composed of seven (A2 to G2). The core of both β-barrels is comprised of conserved hydrophobic residues. The additional C-terminal domain consists of two pairs of short antiparallel β-sheets and two α-helices. It interacts with the C-terminal barrel through an interface consisting of conserved hydrophobic residues. A canonical catalytic triad that is composed of Ser, His, and Asp is located in the open cleft between the β-barrels domain [1,2]. The nsp4 proteinase domain forms peptidase family S32 [E2].

The profile we developed covers the entire nsp4 proteinase domain.

Last update:

May 2010 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

AV_NSP4_PRO, PS51493; Arterivirus nsp4 proteinase domain profile  (MATRIX)


References

1AuthorsBarrette-Ng I.H. Ng K.K.S. Mark B.L. van Aken D. Cherney M.M. Garen C. Kolodenko Y. Gorbalenya A.E. Snijder E.J. James M.N.G.
TitleStructure of arterivirus nsp4. The smallest chymotrypsin-like proteinase with an alpha/beta C-terminal extension and alternate conformations of the oxyanion hole.
SourceJ. Biol. Chem. 277:39960-39966(2002).
PubMed ID12163505
DOI10.1074/jbc.M206978200

2AuthorsTian X. Lu G. Gao F. Peng H. Feng Y. Ma G. Bartlam M. Tian K. Yan J. Hilgenfeld R. Gao G.F.
TitleStructure and cleavage specificity of the chymotrypsin-like serine protease (3CLSP/nsp4) of Porcine Reproductive and Respiratory Syndrome Virus (PRRSV).
SourceJ. Mol. Biol. 392:977-993(2009).
PubMed ID19646449
DOI10.1016/j.jmb.2009.07.062

E1Titlehttps://viralzone.expasy.org/284?outline=all_by_species

E2Titlehttps://www.ebi.ac.uk/merops/cgi-bin/famsum?family=s32



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