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Information on EC 3.4.21.114 - equine arterivirus serine peptidase
for references in articles please use BRENDA:EC3.4.21.114
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.21 Serine endopeptidases
3.4.21.114 equine arterivirus serine peptidase
IUBMB 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) . 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 in peptidase family S32.
The enzyme appears in viruses and cellular organisms
- 3.4.21.114
- rotavirus
- enterotoxin
- prrsv
- gastroenteritis
-
chikungunya
-
replicase
- vp4
-
chikvs
-
rotavirus-infected
- nsp3
-
viroporins
- astrovirus
-
hp-prrsv
-
anti-prrsv
-
rv-induced
Reaction Schemes
showcleavage of (Glu/Gln)-/-(Gly/Ser/Ala) in arterivirus replicase translation products ORF1a and ORF1ab
Synonyms
nonstructural protein 4, non-structural protein 4, 3c-like serine protease, 3clsp, nsp4 serine protease, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3C-like serine protease
3CLSP
equine arteritis virus serine endopeptidase
-
-
-
-
neutrophil serine protease 4
non-structural protein 4
nonstructural protein 4
nsp4
nsp4 serine protease
PRSS57
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cleavage of (Glu/Gln)-/-(Gly/Ser/Ala) in arterivirus replicase translation products ORF1a and ORF1ab
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cleavage of C-N-linkage
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY
97162-88-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Dabsyl-Lys-Thr-Ala-Tyr-Phe-Gln-Leu-Glu-Gly-Arg-His-Phe-Glu-EDANS + H2O
Dabsyl-Lys-Thr-Ala-Tyr-Phe-Gln-Leu-Glu + Gly-Arg-His-Phe-Glu-EDANS
Substrates: -
Products: -
Products: -
?
guanylate-binding protein 1 + H2O
?
-
Substrates: -
Products: -
Products: -
?
Lys-Asp-Lys-Thr-Ala-Tyr-Phe-Gln-Leu-Glu-Gly-Arg-His-Phe-Thr-Trp + H2O
Lys-Asp-Lys-Thr-Ala-Tyr-Phe-Gln-Leu-Glu + Gly-Arg-His-Phe-Thr-Trp
Substrates: -
Products: -
Products: -
?
Lys-Thr-Ala-Tyr-Phe-Gln-Leu-Glu-Gly-Arg-His-Phe-Thr-Trp-Tyr-Gln + H2O
Lys-Thr-Ala-Tyr-Phe-Gln-Leu-Glu + Gly-Arg-His-Phe-Thr-Trp-Tyr-Gln
Substrates: -
Products: -
Products: -
?
NSP3'4 protein + H2O
?
Substrates: recombinantly expressed substrate NSP3'4 covering the last 8 residues of nonstructural protein 3 and the whole amino acid sequence of nonstructural protein 4 mutant S118A
Products: -
Products: -
?
proform caspase-3 + H2O
mature caspase-3 + ?
Substrates: activation
Products: -
Products: -
?
proform caspase-8 + H2O
mature caspase-8 + ?
Substrates: activation
Products: -
Products: -
?
proform caspase-9 + H2O
mature caspase-9 + ?
Substrates: activation
Products: -
Products: -
?
zinc finger antiviral protein + H2O
?
-
Substrates: the enzyme cleaves zinc finger antiviral protein depending on its protease activity
Products: -
Products: -
?
arterivirus replicase ORF1a + H2O
?
-
Substrates: cleavage sites are Glu1430/Gly and Glu1452/Ser
Products: -
Products: -
?
arterivirus replicase ORF1a + H2O
?
-
Substrates: ORF1a can be cleaved following two alternative pathways. In the majority nsp3-8 precursors are cleaved at the nsp4/5 site yielding nsp3-4 and nsp5-8. The latter product is then cleaved at nsp7/8 only. In the alternative proteolytic cascade the nsp4/5 site remains uncleaved while the nsp5/6 and nsp6/7 sites are processed. nsp3-8 has to interact with cleaved nsp2 to allow processing of the nsp4/5 junction, when nsp2 cofactor is absent the alternative pathway is used
Products: -
Products: -
?
arterivirus replicase ORF1a protein + H2O
?
Substrates: -
Products: -
Products: -
?
arterivirus replicase ORF1a protein + H2O
?
Substrates: nsp4 and an unidentified protease is responsible for the cleavage sites nsp2/3, nsp3/4, nsp4/5 and nsp5/6 in the ORF1a protein
Products: -
Products: -
?
arterivirus replicase ORF1a protein + H2O
?
Substrates: -
Products: -
Products: -
?
arterivirus replicase ORF1ab + H2O
?
-
Substrates: cleavage sites are the junctions at nsp3/4, Nsp4/5, 2 internal nsp5 sites, nsp5/6, p80/p50, p50/p26, p26/p12, enzyme cleaves between Glu and Gly, Glu and Ser or Glu and Lys
Products: -
Products: -
?
arterivirus replicase ORF1ab + H2O
?
-
Substrates: cleavage sites are the junctions at nsp3/4, Nsp4/5, 2 internal nsp5 sites, nsp5/6, p80/p50, p50/p26, p26/p12, enzyme cleaves between Glu and Gly, Glu and Ser or Glu and Lys
Products: -
Products: -
?
arterivirus replicase ORF1b + H2O
?
-
Substrates: protein is processed by nsp4 serine protease
Products: -
Products: -
?
arterivirus replicase ORF1b + H2O
?
-
Substrates: protein is processed by nsp4 serine protease at the following sites: nsp9/10 i.e. p80/p50, cleavage occurs between Glu2370 and Ser, nsp10/11 i.e. p50/p26, cleavage occurs between Gln2837 and Ser, nsp11/12 i.e. nsp26/p12, cleavage between Glu3056 and Gly
Products: -
Products: -
?
arterivirus replicase ORF1b + H2O
?
-
Substrates: protein is processed by nsp4 serine protease
Products: -
Products: -
?
NF-kappaB essential modulator NEMO + H2O
?
-
Substrates: -
Products: -
Products: -
?
NF-kappaB essential modulator NEMO + H2O
?
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: nsp4 cleaves multiple GluX(Gly/Ser/Ala) sites, X: cleavage site
Products: -
Products: -
?
additional information
?
-
-
Substrates: nsp4 cleaves multiple GluX(Gly/Ser/Ala) sites, X: cleavage site
Products: -
Products: -
?
additional information
?
-
-
Substrates: protease has a specificity for Glu/Gly or Glu/Ser substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is the main viral protease
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme controls the maturation of the replicase complex. The C-terminal domain has a modulating role in nsp4-mediated autoprocessing of the arterivirus replicase polyproteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme cleaves the cognate nsp6/7- and nsp7/8 site in in vitro synthesized substrates
Products: -
Products: -
?
additional information
?
-
Substrates: nsp4 cleaves multiple GluX(Gly/Ser/Ala) sites, X: cleavage site
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme activation occurs through cleavage of the amino-terminal signal peptide by a signal peptidase, followed by removal of the two-residue activation peptide by dipeptidyl peptidase 1/cathepsin C
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme has an elastase-like active site and a potential heparin binding site and cleaves preferentially after Arg residues
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme shows a 3C-like serine protease activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows a 3C-like serine protease activity
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
arterivirus replicase ORF1a + H2O
?
-
Substrates: ORF1a can be cleaved following two alternative pathways. In the majority nsp3-8 precursors are cleaved at the nsp4/5 site yielding nsp3-4 and nsp5-8. The latter product is then cleaved at nsp7/8 only. In the alternative proteolytic cascade the nsp4/5 site remains uncleaved while the nsp5/6 and nsp6/7 sites are processed. nsp3-8 has to interact with cleaved nsp2 to allow processing of the nsp4/5 junction, when nsp2 cofactor is absent the alternative pathway is used
Products: -
Products: -
?
guanylate-binding protein 1 + H2O
?
-
Substrates: -
Products: -
Products: -
?
proform caspase-3 + H2O
mature caspase-3 + ?
Substrates: activation
Products: -
Products: -
?
proform caspase-8 + H2O
mature caspase-8 + ?
Substrates: activation
Products: -
Products: -
?
proform caspase-9 + H2O
mature caspase-9 + ?
Substrates: activation
Products: -
Products: -
?
zinc finger antiviral protein + H2O
?
-
Substrates: the enzyme cleaves zinc finger antiviral protein depending on its protease activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is the main viral protease
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme controls the maturation of the replicase complex. The C-terminal domain has a modulating role in nsp4-mediated autoprocessing of the arterivirus replicase polyproteins
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme shows a 3C-like serine protease activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows a 3C-like serine protease activity
Products: -
Products: -
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,3S)-7-amino-3-[[(1S,2S)-2-[[(2R)-2-amino-1-hydroxy-3-methylbutyl]amino]-1-hydroxy-4-methylpentyl]amino]heptan-2-ol
-
ZINC01510656
(15R,19R)-17-(2,4-dimethylphenyl)-17-azapentacyclo[6.6.5.02,7.09,14.015,19]nonadeca-2,4,6,9,11,13-hexaene-16,18-dione
ZINC08792350
5-[2-oxo-2-(4-phenylcyclohexyl)ethoxy]benzo[h]indeno[1,2,3-de]quinolin-8(7bH)-one
ZINC08877407
1-[(6-methyl-8-oxo-3,4-dihydro-8H-spiro[benzo[1,2-b:5,4-b']dipyran-2,1'-cyclohexan]-7-yl)acetyl]piperidine-4-carboxylic acid
ZINC16919178
5a,6,7,8,8a,14a,15,16,17,17a-decahydroheptacene-5,9,14,18-tetrone
ZINC38167083
3,7-bis(2-oxo-2,6-dihydro-1H-indol-3-yl)pyrrolo[2,3-f]indole-2,6(1H,5H)-dione
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Arteritis
Mutagenesis Analysis of the nsp4 Main Proteinase Reveals Determinants of Arterivirus Replicase Polyprotein Autoprocessing.
Breast Neoplasms
HCV nonstructural protein 4 is associated with aggressiveness features of breast cancer.
Bronchitis
Infectious Bronchitis Virus Nonstructural Protein 4 Alone Induces Membrane Pairing.
Communicable Diseases
Prediction of promiscuous T cell epitopes in RNA dependent RNA polymerase of Chikungunya virus.
Encephalomyelitis, Venezuelan Equine
Nucleotide sequences of the 26S mRNAs of the viruses defining the Venezuelan equine encephalitis antigenic complex.
Gastroenteritis
Rotavirus nonstructural protein NSP4 induces heterotypic antibody responses during natural infection in children.
Gastroenteritis
[Role of rotavirus non-structural protein 4 in causing of acute gastroenteritis]
Hepatitis
Crystal structure of the C-terminal cytoplasmic domain of non-structural protein 4 from mouse hepatitis virus A59.
Hepatitis
Murine Hepatitis Virus Nonstructural Protein 4 Regulates Virus-induced Membrane Modifications and Replication Complex Function.
Hepatitis C
Hepatitis C virus non-structural protein 4 suppresses Th1 responses by stimulating IL-10 production from monocytes.
Hepatitis C
Immunohistostaining of hepatitis C virus non-structural protein 4 in ependymocytes of uninfected mice: an antigenic mimicry?
Hepatitis C
Tracking virus-specific CD4+ T cells during and after acute hepatitis C virus infection.
Hypersensitivity
Prediction of promiscuous T cell epitopes in RNA dependent RNA polymerase of Chikungunya virus.
Infections
Epitope mapping and use of epitope-specific antisera to characterize the VP5* binding site in rotavirus SA11 NSP4.
Infections
Expression of Concern: Rotaviral enterotoxin nonstructural protein 4 targets mitochondria for activation of apoptosis during infection.
Infections
Rotaviral enterotoxin nonstructural protein 4 targets mitochondria for activation of apoptosis during infection.
Infections
Rotaviral nonstructural protein 4 triggers dynamin-related protein 1-dependent mitochondrial fragmentation during infection.
Infections
Tyrosine phosphorylation modulates mitochondrial chaperonin Hsp60 and delays rotavirus NSP4-mediated apoptotic signaling in host cells.
Infections
Withdrawal: Rotaviral enterotoxin nonstructural protein 4 targets mitochondria for activation of apoptosis during infection.
Neoplasms
The effect of bovine rotavirus and its nonstructural protein 4 on ER stress-mediated apoptosis in HeLa and HT-29 cells.
Porcine Reproductive and Respiratory Syndrome
Characterization of the biochemical properties and identification of amino acids forming the catalytic center of 3C-like proteinase of porcine reproductive and respiratory syndrome virus.
Porcine Reproductive and Respiratory Syndrome
Induction of Apoptosis by the Nonstructural Protein 4 and 10 of Porcine Reproductive and Respiratory Syndrome Virus.
Porcine Reproductive and Respiratory Syndrome
Intracellularly expressed nanobodies against non-structural protein 4 of porcine reproductive and respiratory syndrome virus inhibit virus replication.
Porcine Reproductive and Respiratory Syndrome
Nonstructural Protein 4 of Porcine Reproductive and Respiratory Syndrome Virus Modulates Cell Surface Swine Leukocyte Antigen Class I Expression by Downregulating ?2-Microglobulin Transcription.
Porcine Reproductive and Respiratory Syndrome
Porcine reproductive and respiratory syndrome virus nonstructural protein 4 antagonizes beta interferon expression by targeting the NF-?B essential modulator.
Porcine Reproductive and Respiratory Syndrome
Porcine Reproductive and Respiratory Syndrome Virus Nonstructural Protein 4 Cleaves Porcine DCP1a To Attenuate Its Antiviral Activity.
Porcine Reproductive and Respiratory Syndrome
Porcine reproductive and respiratory syndrome virus nonstructural protein 4 induces apoptosis dependent on its 3C-like serine protease activity.
Porcine Reproductive and Respiratory Syndrome
Serodiagnosis, targeting nonstructural protein 4, of porcine reproductive and respiratory syndrome virus.
Porcine Reproductive and Respiratory Syndrome
The amino acid at residue 155 in nonstructural protein 4 of porcine reproductive and respiratory syndrome virus contributes to its inhibitory effect for interferon-? transcription in vitro.
Rotavirus Infections
Rotavirus enterotoxin NSP4 binds to the extracellular matrix proteins laminin-beta3 and fibronectin.
Rotavirus Infections
Silencing of the Rotavirus NSP4 Protein Decreases the Incidence of Biliary Atresia in Murine Model.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.24
dabsyl-Lys-Thr-Ala-Tyr-Phe-Gln-Leu-Glu-Gly-Arg-His-Phe-Glu-EDANS
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0073
dabsyl-Lys-Thr-Ala-Tyr-Phe-Gln-Leu-Glu-Gly-Arg-His-Phe-Glu-EDANS
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
malfunction
the ability of nsp4 to induce apoptosis is significantly impaired by His39, Asp64, and Ser118 mutations
malfunction
-
in granulocyte-macrophage progenitors (GMPs), loss of enzyme results in the decrease of cellular levels of histamine, serotonin and heparin/heparin sulfate. Mast cells that are derived from enzyme-deficient GMPs have abnormal secretory granule morphology and a sustained reduction in histamine and serotonin levels. Consequently, in passive cutaneous anaphylaxis and acute arthritis models, mast cell-mediated vascular leakage in the skin and joints is substantially reduced in enzyme-deficient mice
physiological function
porcine reproductive and respiratory syndrome virus nonstructural protein 4 is a critical apoptosis inducer dependent on its serine protease activity, the full-length of nsp4 structure is required for its apoptosis-inducing activity, the enzyme can induce apoptosis in diverse cell lines, e.g. in HeLa cells, overview
physiological function
-
nsp4 inhibits virus-induced IFN-beta production by targeting NF-kappaB essential modulator NEMO for proteolytic cleavage. The scission occurs at sites E166, E171, Q205, and E349
physiological function
nsp4 inhibits virus-induced IFN-beta production by targeting NF-kappaB essential modulator NEMO for proteolytic cleavage. The scission occurs at sites E166, E171, Q205, and E349. NEMO cleavage at E349 alone may not be sufficient to completely inactivate the interferon response via this signaling adaptor
physiological function
-
enzyme expression during the early stages of mast cell development regulates mast cell-mediated vascular leakage
physiological function
-
the enzyme antagonizes the antiviral activity of zinc finger antiviral protein
physiological function
-
the enzyme cleaves guanylate-binding protein 1 at E338 to antagonize the antiviral effect of the substrate
additional information
residues His39, Asp64, and Ser118 are essential for the enzyme to trigger apoptosis
additional information
-
residues His39, Asp64, and Ser118 are essential for the enzyme to trigger apoptosis
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A1E8J1_PRRSV
2473
0
269138
TrEMBL
other Location (Reliability: 3)
E3V2B5_PRRSV
2473
0
268921
TrEMBL
-
RPOA_EAVBU
3175
10
345384
Swiss-Prot
-
Q91F54_PRRSV
2503
0
272488
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
ORF1a is subject to at least 5 proteolytic cleavages, resulting in five non-structural protein 1-6
proteolytic modification
replicase of EAV processed by at least 3 viral proteases, resulting in the generation of non-structural proteins Nsp1-6
proteolytic modification
-
replicase of EAV processed by at least 3 viral proteases, resulting in the generation of non-structural proteins Nsp1-6
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
hanging drop vapor diffusion method
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R82S
-
the mutation provides a greater selective advantage in human cells than in Aedes albopictus. The mutation does not provide competitive fitness advantage in Aedes albopictus
D1129E
mutant is able to cleave the Nsp4/5 site with wild-type efficiently but does not process the Nsp3/4 and Nsp5/6 junctions
S1184I
T1179N
retains wild-type activity towards Nsp4/5, cleaves Nsp5/6 with increased efficiency
D64A
H39A
S118A
S180N
-
the degradation of zinc finger antiviral protein induced by the mutant enzyme is attenuated, compared with that by the wild type enzyme
T492I
-
the substitution associates with the increased infectivity, transmissibility, and attenuated pathogenicity observed in severe acute respiratory syndrome coronavirus 2 variants, including Delta and Omicron. Mechanistically, the mutation alters non-structural protein cleavage, which changes viral properties. The mutation increases the replication capacity and infectiveness of the virus and improves its ability to evade host immune responses. Non-structural protein 5 cleavage of mutant 492I substrate is more efficient than cleavage of control substrate (2.37fold increase in catalytic efficiency)
D64A
site-directed mutagenesis, the mutant shows significantly reduced ability to induce apoptosis compared to the wild-type enzyme
H39A
site-directed mutagenesis, the mutant shows significantly reduced ability to induce apoptosis compared to the wild-type enzyme
S118A
catalytic residue, mutant protein inactive
S118A
site-directed mutagenesis, the mutant shows significantly reduced ability to induce apoptosis compared to the wild-type enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose affinity chromatography, gel filtration
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3).
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
GST fusion protein expressed in Escherichia coli BL21(DE3)
large scale production of recombinant nsp4 in Escherichia coli. The nsp4 proteinase is expressed either fused to maltose binding protein or carrying a C-terminal hexahistidine tag
-
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)., recombinant expression in HeLa cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme transcription is downregulated as granulocyte macrophage progenitors differentiate into mature granulocytes
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Snijder, E.J.; Wassenaar, A.L.; Spaan, W.J.
Proteolytic processing of the N-terminal region of the equine arteritis virus replicase
Adv. Exp. Med. Biol.
342
227-232
1993
equine arteritis virus (P19811)
brenda
Snijder, E.J.; Wassenaar, A.L.; van Dinten, L.C.; Spaan, W.J.; Gorbalenya, A.E.
The arterivirus nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases
J. Biol. Chem.
271
4864-4871
1996
equine arteritis virus (P19811), equine arteritis virus, equine arteritis virus Bucyrus (P19811)
brenda
Barrette-Ng, I.H.; Ng, K.K.; Mark, B.L.; Van Aken, D.; Cherney, M.M.; Garen, C.; Kolodenko, Y.; Gorbalenya, A.E.; Snijder, E.J.; James, M.N.
Structure of arterivirus nsp4. The smallest chymotrypsin-like proteinase with an alpha/beta C-terminal extension and alternate conformations of the oxyanion hole
J. Biol. Chem.
277
39960-39966
2002
equine arteritis virus (P19811), equine arteritis virus
brenda
den Boon, J.A.; Snijder, E.J.; Chirnside, E.D.; de Vries, A.A.; Horzinek, M.C.; Spaan, W.J.
Equine arteritis virus is not a togavirus but belongs to the coronaviruslike superfamily
J. Virol.
65
2910-2920
1991
equine arteritis virus (P19811)
brenda
van Dinten, L.C.; Wassenaar, A.L.; Gorbalenya, A.E.; Spaan, W.J.; Snijder, E.J.
Processing of the equine arteritis virus replicase ORF1b protein: identification of cleavage products containing the putative viral polymerase and helicase domains
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