3.4.21.115: infectious pancreatic necrosis birnavirus Vp4 peptidase
This is an abbreviated version!
For detailed information about infectious pancreatic necrosis birnavirus Vp4 peptidase, go to the full flat file.
Word Map on EC 3.4.21.115
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3.4.21.115
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polyprotein
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rubella
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nonstructural
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lamins
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replicase
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papain-like
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baculoviruses
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ca2+-regulated
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replicons
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catalytic-site
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multicatalytic
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zn2+-binding
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virol
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nucleocytoplasmic
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alphaviruses
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self-cleavage
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minidomain
- 3.4.21.115
- polyprotein
- rubella
-
nonstructural
- lamins
-
replicase
-
papain-like
-
baculoviruses
-
ca2+-regulated
-
replicons
-
catalytic-site
-
multicatalytic
-
zn2+-binding
-
virol
-
nucleocytoplasmic
- alphaviruses
-
self-cleavage
-
minidomain
Reaction
cleaves the (Ser/Thr)-Xaa-Ala-/-(Ser/Ala)-Gly motif in the polyprotein NH2-pVP2-VP4-VP3-COOH of infectious pancreatic necrosis virus at the pVP2-VP4 and VP4-VP3 junctions =
Synonyms
avian infectious busrsal disease birnavirus Vp4 endopeptidase, blotched snakehead birnavirus endopeptidase, Drosophila X virus Vp4 protease, equine arterivirus serine peptidase, infectious pancreatic necrosis birnavirus Vp4 protease, NS, NS protease, S50.001, VP4
ECTree
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Substrates Products
Substrates Products on EC 3.4.21.115 - infectious pancreatic necrosis birnavirus Vp4 peptidase
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REACTION DIAGRAM
NH2-pVP2-X-VP4-VP3-COOH + H2O
pVP2 + peptide X + VP4 + VP3
VP4 is encoded as part of the 1114-residue long segment A polyprotein NH2-pVP2-X-VP4-VP3-COOH. It cleaves after amino acid residue positions 512, 618, and 830 to yield capsid precursor protein pVP2, peptide X, VP4 itself, and ribonucleoprotein VP3. Additional cleavage sites were found at the C-terminal side of amino acids 451, 492, and 499 within the pVP2 region
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pVP2 + VP3 + VP4
cleaves at the (Ser/Thr)-X-Ala-/-(Ser/Ala)-Gly motif, -/- = cleavage site
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polyprotein of IPNV + H2O
pVP2 + VP3 + VP4
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the viral NS protease is active and cleaves the polyprotein when it is expressed in Escherichia coli
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acyl-enzyme complex for intermolecular self-cleavage reaction determined by crystallization, conserved overall structure of VP4 determined despite of only 20% sequence identity between different VP4 proteins
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additional information
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cleavage sites of the MABV polyprotein at the pVP2-VP4 junction determined, VP4 protease activity determined, expression patterns of pVP2, VP4 and VP3 in four infected cell lines shown, VP4 protease activity determined
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