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EC 3.4.21.114 is Orphan !
Common name :Equine arterivirus serine peptidase

Systematic name :-

Other names :Arterivirus NSP4
Equine arteritis virus serine peptidase
3C-like serine protease
3C-like Ser protease
3CLSP
Nonstructural protein 4 serine protease
NSP4 serine protease
NSP4 SP
Chymotrypsin-like serine proteinase nsp4
Comments :In the equine arterivirus (EAV), the replicase gene is translated into open reading frame 1a (ORF1a) and ORF1ab polyproteins. This enzyme is the main viral proteinase and processes five cleavage sites in the ORF1a protein and three in the ORF1b-encoded part of the ORF1ab protein to yield nonstructural proteins (nsp5-nsp12) (3). It combines the catalytic system of a chymotrypsin-like serine peptidase (His-Asp-Ser catalytic triad) with the substrate specificity of a 3C-like serine peptidase (Glu or Gln) at the P1 position and a small amino-acid residue (Gly, Ser or Ala) at the P1' position (1). Cleavage of ORF1ab by this enzyme is essential for viral replication (2). Belongs in peptidase family S32. In the equine arterivirus (EAV), the replicase gene is translated into open reading frame 1a (ORF1a) and ORF1ab polyproteins. This enzyme is the main viral proteinase and processes five cleavage sites in the ORF1a protein and three in the ORF1b-encoded part of the ORF1ab protein to yield nonstructural proteins (nsp5-nsp12). It combines the catalytic system of a chymotrypsin-like serine peptidase (His-Asp-Ser catalytic triad) with the substrate specificity of a 3C-like serine peptidase (Glu or Gln) at the P1 position and a small amino-acid residue (Gly, Ser or Ala) at the P1' position. Cleavage of ORF1ab by this enzyme is essential for viral replication. Belongs to peptidase family S32.

Created :EC 3.4.21.114 created 2006

BRENDA organisms :equine arteritis
equine arteritis
porcine reproductive

Swiss-ProtNo protein sequences are associated with EC 3.4.21.114 in Swiss-Prot

TrEMBLNo protein sequences are associated with EC 3.4.21.114 in TrEMBL

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for EC 3.4.21.114.

Links to other databases
NC-IUBMB, INTENZ, ENZYME, PDB, BRENDA, KEGG, BIOCYC, PubMed,NCBI-Entrez

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