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Information on EC 3.4.22.44 - nuclear-inclusion-a endopeptidase
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EC Tree
3.4.22.44 nuclear-inclusion-a endopeptidaseSpecify your search results
Word Map
- 3.4.22.44
- polyproteins
-
etch
- potyviruses
- hc-pro
- potyviridae
-
turnip
- plum
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cistron
-
genome-linked
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nib-cp
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trimv
- agriculture
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ringspot
- poacevirus
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niapro
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Hydrolyses glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-/-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.
Synonyms
nia protease, nia-pro, nia protein, nia proteins, nuclear inclusion a protease, protease nia, proteinase nia, nuclear inclusion a-protease, potyviral nuclear inclusion a, nuclear inclusion body protein a, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
49 kDa proteinase
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-
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49 kDa-Pro
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NIA
NIa protease
NIa proteins
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NIa-Pro
nuclear inclusion body protein a
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nuclear inclusion protein A protease
potyviral nuclear inclusion a
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polyprotein consisting of two domains, viral protein genome-linked (VPg) and protease (NIaPro), separated by an inefficiently utilized selfproteolytic site
potyvirus NIa protease
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protease NIa
proteinase Nia
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proteinase, polyprotein-processing, Nia
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proteins (specific proteins and subclasses), NIa (nuclear inclusion, a)
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proteins NIa
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proteins, small nuclear inclusion NIa
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NIA
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NIA
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polyprotein consisting of two domains, viral protein genome-linked (VPg) and protease (NIaPro), separated by an inefficiently utilized selfproteolytic site
NIa protease
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nuclear inclusion protein A protease
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protease NIa
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolyses glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-/-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
139946-51-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-Asn-Asn-Val-Arg-Phe-Gln-Ser-Leu-amide + H2O
acetyl-Asn-Asn-Val-Arg-Phe-Gln + Ser-Leu-amide
amyloid beta + H2O
?
-
the enzyme cleaves monomeric and oligomeric amyloid beta at a similar rate in vitro
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-
?
amyloid-beta peptide + H2O
?
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degradation of oligomeric as well as monomeric forms of Amyloid-beta, presence of the consensus sequence, Val12-His-His-Gln15, near the presumptive alpha-secretase cleavage site of the amyloid-beta peptide
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-
?
Pro-Thr-Thr-Glu-Leu-Tyr-Phe-Gln-Ser-Gly-Thr-Val-Asp-Arg-Arg + H2O
Pro-Thr-Thr-Glu-Leu-Tyr-Phe-Gln + Ser-Gly-Thr-Val-Asp-Arg-Arg
acetyl-Arg-Glu-Thr-Val-Arg-Phe-Gln-Ser-Asp-amide + H2O
?
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-
-
-
?
acetyl-Arg-Glu-Thr-Val-Arg-Phe-Gln-Ser-Asp-amide + H2O
?
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-
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?
acetyl-Asn-Asn-Val-Arg-Phe-Gln-Ser-Leu-amide + H2O
acetyl-Asn-Asn-Val-Arg-Phe-Gln + Ser-Leu-amide
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-
-
?
acetyl-Asn-Asn-Val-Arg-Phe-Gln-Ser-Leu-amide + H2O
acetyl-Asn-Asn-Val-Arg-Phe-Gln + Ser-Leu-amide
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-
-
?
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide + H2O
?
turnip mosaic potyvirus
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-
-
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?
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide + H2O
?
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?
nuclear inclusion protein a + H2O
?
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analysis of cleavage sites, specific for its own polypeptide chain, no cleavage of other potyvirus NIa proteins
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?
nuclear inclusion protein a + H2O
?
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analysis of cleavage sites, specific for its own polypeptide chain, no cleavage of other potyvirus NIa proteins
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-
?
nuclear inclusion protein a + H2O
?
turnip mosaic potyvirus
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the nuclear inclusion protein of potyviruses has two domains, the Vpg domain of 22 kDa and the C-terminal domain of 27 kDa which has proteolytic activity. The first cleavage at Ser223-Gly224 produces a 25 kDa protein. TuMV cleaves itself in cis, removing a 20 amino aicd peptide from the C-terminus. A second cleavage is very slow and occurs between Thr207-Ser208, resulting in a 24 kDa protein
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-
?
nuclear inclusion protein a + H2O
?
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the nuclear inclusion protein of potyviruses has two domains, the Vpg domain of 22 kDa and the C-terminal domain of 27 kDa which has proteolytic activity. The first cleavage at Ser223-Gly224 produces a 25 kDa protein. TuMV cleaves itself in cis, removing a 20 amino aicd peptide from the C-terminus. A second cleavage is very slow and occurs between Thr207-Ser208, resulting in a 24 kDa protein
-
-
?
Pro-Thr-Thr-Glu-Leu-Tyr-Phe-Gln-Ser-Gly-Thr-Val-Asp-Arg-Arg + H2O
Pro-Thr-Thr-Glu-Leu-Tyr-Phe-Gln + Ser-Gly-Thr-Val-Asp-Arg-Arg
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-
-
?
Pro-Thr-Thr-Glu-Leu-Tyr-Phe-Gln-Ser-Gly-Thr-Val-Asp-Arg-Arg + H2O
Pro-Thr-Thr-Glu-Leu-Tyr-Phe-Gln + Ser-Gly-Thr-Val-Asp-Arg-Arg
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-
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?
turnip mosaic virus polyprotein + H2O
?
turnip mosaic potyvirus
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cleaved at seven differnt locations
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?
turnip mosaic virus polyprotein + H2O
?
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cleaved at seven differnt locations
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?
additional information
?
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interaction between purified recombinant NIa-Pro and VPg domains, overview
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?
additional information
?
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the enzyme interacts with proteins EIF3G, FBPA1, FK506BP, GTPBP, MSRB1, and MTL
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?
additional information
?
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the S3 and S4 pockets are mainly responsible for the substrate specificity, comparison to the specificity of the tobacco etch virus, TEV, protease, structural determinants of substrate specificity, overview. The TVMV protease is less tolerant of variation at the P1' position than TEV protease, and substitutions in the P6 position are more readily tolerated by TVMV than TEV protease
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?
additional information
?
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the S3 and S4 pockets are mainly responsible for the substrate specificity, comparison to the specificity of the tobacco etch virus, TEV, protease, structural determinants of substrate specificity, overview. The TVMV protease is less tolerant of variation at the P1' position than TEV protease, and substitutions in the P6 position are more readily tolerated by TVMV than TEV protease
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?
additional information
?
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turnip mosaic potyvirus
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consensus substrate sequence: Yaa-Val-Arg-His-Gln-/-Ser, with Yaa being a aliphatic amino acid and the scissile bond being located between Gln and Ser
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?
additional information
?
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consensus substrate sequence: Yaa-Val-Arg-His-Gln-/-Ser, with Yaa being a aliphatic amino acid and the scissile bond being located between Gln and Ser
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?
additional information
?
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NIa possesses a relatively strict substrate specificity with a preference for Val-Xaa-His-GlnQ, with the scissile bond located after Gln
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nuclear inclusion protein a + H2O
?
-
analysis of cleavage sites, specific for its own polypeptide chain, no cleavage of other potyvirus NIa proteins
-
-
?
nuclear inclusion protein a + H2O
?
-
analysis of cleavage sites, specific for its own polypeptide chain, no cleavage of other potyvirus NIa proteins
-
-
?
nuclear inclusion protein a + H2O
?
turnip mosaic potyvirus
-
the nuclear inclusion protein of potyviruses has two domains, the Vpg domain of 22 kDa and the C-terminal domain of 27 kDa which has proteolytic activity. The first cleavage at Ser223-Gly224 produces a 25 kDa protein. TuMV cleaves itself in cis, removing a 20 amino aicd peptide from the C-terminus. A second cleavage is very slow and occurs between Thr207-Ser208, resulting in a 24 kDa protein
-
-
?
nuclear inclusion protein a + H2O
?
-
the nuclear inclusion protein of potyviruses has two domains, the Vpg domain of 22 kDa and the C-terminal domain of 27 kDa which has proteolytic activity. The first cleavage at Ser223-Gly224 produces a 25 kDa protein. TuMV cleaves itself in cis, removing a 20 amino aicd peptide from the C-terminus. A second cleavage is very slow and occurs between Thr207-Ser208, resulting in a 24 kDa protein
-
-
?
additional information
?
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-
interaction between purified recombinant NIa-Pro and VPg domains, overview
-
-
?
additional information
?
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the enzyme interacts with proteins EIF3G, FBPA1, FK506BP, GTPBP, MSRB1, and MTL
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-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no competitive inhibition of the proteolytic activity by the presence of excess of different protease mutants
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alzheimer Disease
Expression of the plant viral protease NIa in the brain of a mouse model of Alzheimer's disease mitigates A? pathology and improves cognitive function.
Infections
A set of host proteins interacting with papaya ringspot virus NIa-Pro protein identified in a yeast two-hybrid system.
Infections
A viral protease relocalizes in the presence of the vector to promote vector performance.
Infections
Functional regulation of PVBV Nuclear Inclusion protein-a protease activity upon interaction with Viral Protein genome-linked and phosphorylation.
Infections
Interaction network of tobacco etch potyvirus NIa protein with the host proteome during infection.
Infections
Localization of a potyvirus and the viral genome-linked protein in wild potato leaves at an early stage of systemic infection.
Infections
Optimizing the PBS1 Decoy System to Confer Resistance to Potyvirus Infection in Arabidopsis and Soybean.
Infections
Soybean RNA interference lines silenced for eIF4E show broad potyvirus resistance.
Infections
Strain-specific interaction of the tobacco etch virus NIa protein with the translation initiation factor eIF4E in the yeast two-hybrid system.
Infections
The NIa-Pro protein of Turnip mosaic virus improves growth and reproduction of the aphid vector, Myzus persicae (green peach aphid).
Infections
The NIa-Protease Protein Encoded by the Pepper Mottle Virus Is a Pathogenicity Determinant and Releases DNA Methylation of Nicotiana benthamiana.
Superinfection
The Coat Protein and NIa Protease of Two Potyviridae Family Members Independently Confer Superinfection Exclusion.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.51
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
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27 kDa full length protease, pH 7.0, 12°C
0.52
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 7.4, 12°C
0.62
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 8.0, 12°C
1.14
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 7.0, 25°C
1.2
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 7.4, 25°C
2.22
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
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27 kDa full length protease
2.64
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
25 kDa protease
2.83
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 8.0, 25°C
0.069
Pro-Thr-Thr-Glu-Leu-Tyr-Phe-Gln-Ser-Gly-Thr-Val-Asp-Arg-Arg
-
27 kDa full length protease
0.271
Pro-Thr-Thr-Glu-Leu-Tyr-Phe-Gln-Ser-Gly-Thr-Val-Asp-Arg-Arg
-
truncated protease
0.082
TETVRFQSGTRR
recombinant wild-type TVMV protease, pH 7.0, 30°C
0.108
TETVRFQSGTRR
recombinant mutant TVMV1-217 protease, pH 7.0, 30°C
0.05
WDGGEVAHQAGESV
-
recombinant S129D NIa-Pro mutant, pH 8.5, 25°C
0.06
WDGGEVAHQAGESV
-
recombinant S129A NIa-Pro mutant, pH 8.5, 25°C
0.15
WDGGEVAHQAGESV
-
recombinant S129D NIa-Pro mutant in presence of the VPg domain, pH 8.5, 25°C
0.45
WDGGEVAHQAGESV
-
recombinant E191A VPg-Pro mutant, pH 8.5, 25°C
0.69
WDGGEVAHQAGESV
-
recombinant W143A NIa-Pro mutant, pH 8.5, 25°C
11.4
WDGGEVAHQAGESV
-
recombinant W143A NIa-Pro mutant in presence of the VPg domain, pH 8.5, 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.12
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 7.0, 12°C
0.19
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 7.0, 25°C
0.22
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 7.4, 12°C
0.32
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease
0.33
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
25 kDa protease
0.34
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 7.4, 25°C
0.373
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 8.0, 12°C
1.01
acetyl-Glu-Pro-Thr-Val-Tyr-His-Gln-Thr-Leu-amide
turnip mosaic potyvirus
-
27 kDa full length protease, pH 8.0, 25°C
0.033
Pro-Thr-Thr-Glu-Leu-Tyr-Phe-Gln-Ser-Gly-Thr-Val-Asp-Arg-Arg
-
truncated protease
0.18
Pro-Thr-Thr-Glu-Leu-Tyr-Phe-Gln-Ser-Gly-Thr-Val-Asp-Arg-Arg
-
27 kDa full length protease
0.092
TETVRFQSGTRR
recombinant wild-type TVMV protease, pH 7.0, 30°C
0.094
TETVRFQSGTRR
recombinant mutant TVMV1-217 protease, pH 7.0, 30°C
0.002
WDGGEVAHQAGESV
-
recombinant W143A NIa-Pro mutant, pH 8.5, 25°C
0.004
WDGGEVAHQAGESV
-
recombinant S129D NIa-Pro mutant, pH 8.5, 25°C
0.005
WDGGEVAHQAGESV
-
recombinant S129A NIa-Pro mutant, pH 8.5, 25°C
0.006
WDGGEVAHQAGESV
-
recombinant S129D NIa-Pro mutant in presence of the VPg domain, pH 8.5, 25°C
0.01
WDGGEVAHQAGESV
-
recombinant W143A NIa-Pro mutant in presence of the VPg domain, pH 8.5, 25°C
0.034
WDGGEVAHQAGESV
-
recombinant wild-type NIa-Pro, pH 8.5, 25°C
0.063
WDGGEVAHQAGESV
-
recombinant E191A VPg-Pro mutant, pH 8.5, 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.87
TETVRFQSGTRR
recombinant mutant TVMV1-217 protease, pH 7.0, 30°C
1.12
TETVRFQSGTRR
recombinant wild-type TVMV protease, pH 7.0, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
amino acid and nucleotide identity percentages across the whole coat protein shown, the coat protein core region and the 3' non-translated region indicated, sequence identity to several Potyvirus strains determined, phylogenetic tree analysis performed
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
25
15
turnip mosaic potyvirus
-
temperature optimum of the 27 kDa full length protease. The optimum is not related to the C-terminal cleavage site but to the stability or flexibility of the structure of the NIa protease
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
polyprotein, part of the nuclear inclusion protein gene NIa of Vanilla mosaic virus-CI; VanMV, isolate from Vanilla tahitensis
SwissProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
NIa-Pro localizes in the cytoplasm and in the nucleus. In the presence of the insect vector, NIa-Pro relocalizes to the vacuole of the cell and this relocalization is essential for its ability to decrease plant defences and increase aphid performance on host plants
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
-
the nuclear inclusion a protease of turnip mosaic virus is responsible for the processing of the viral polyprotein into functional proteins. Degradation of Amyloid-beta in the cytoplasm can be a novel strategy to control the levels of Amyloid-beta, plaque formation, and the associated cell death
physiological function
the TVMV genome is translated into a single large polyprotein that is subsequently processed by three virally encoded proteases. Seven of the nine cleavage events are carried out by the NIa protease
physiological function
-
oligomeric amyloid beta-induced cytotoxicity and mitochondrial dysfunction are significantly ameliorated by the enzyme. The enzyme prevents mitochondrial deposition of amyloid beta
physiological function
-
potyviral protein genome-linked, established as an intrinsically disordered domain, undergoes plausible structural alterations upon interaction with globular nuclear inclusion-a protease which induces the ATPase activity
physiological function
-
protease NIa not only reduces amyloid-beta pathology, but also improves behavioral deficits in mice
physiological function
-
the nuclear inclusion a-protease domain increases Myzus persicae growth and reproduction on both Nicotiana benthamiana and Arabidopsis thaliana
physiological function
-
NIa-Pro responds to the presence of the aphid vector during infection by relocalizing to the vacuole. Remarkably, vacuolar localization is required for the ability of NIa-Pro to enhance aphid reproduction on host plants, vacuole localization disappears when aphids are removed
physiological function
-
potyviral NIa targets many host elements during infection, establishing a network in which information is efficiently transmitted
additional information
-
overexpression of NIa in rat B103 neuroblastoma cells results in a significant reduction in cell death caused by both intracellularly generated and exogenously added Amyloidbeta. Moreover, lentiviral-mediated expression of NIa in APPsw/PS1 transgenic mice significantly reduces the levels of Amyloid-beta and plaques in the brain
additional information
-
the full-length potyviral genome protease, VPg-Pro, has two domains: an N-terminal viral protein genome-linked, VPg, and a C-terminal protease NIa-Pro. Regulation of nuclear inclusion protein-a protease is crucial for polyprotein processing and hence, for successful infection by potyviruses, mechanisms regulating nuclear inclusion protein-a protease activity. Firstly, the influence of the VPg domain on the proteolytic activity of NIa-Pro increases when the two domains interact each other. Secondly, the protease activity of NIa-Pro can also be modulated by phosphorylation at Ser129. interaction with VPg as well as phosphorylation of Ser129 relays a signal through Trp143 present at the protein surface to the active site pocket by subtle conformational changes, thus modulating protease activity of NIa-Pro, molecular modeling, homology modeling, and molecular dynamics simulations, overview
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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). POL1_BAYMJ
Barley yellow mosaic virus (strain Japanese II-1)
2410
3
270770
Swiss-Prot
other Location (Reliability: 2)
POL1_BAYMY
Barley yellow mosaic virus (isolate China/Yancheng/1998)
2410
3
270904
Swiss-Prot
other Location (Reliability: 3)
POLG_LMV0
Lettuce mosaic virus (strain 0 / isolate French)
3255
0
367571
Swiss-Prot
other Location (Reliability: 2)
POLG_LMVE
3255
0
367624
Swiss-Prot
other Location (Reliability: 2)
POLG_BCMNN
3066
0
350390
Swiss-Prot
other Location (Reliability: 2)
POLG_BSTV1
3093
0
348106
Swiss-Prot
other Location (Reliability: 5)
POLG_BSTVG
942
0
105547
Swiss-Prot
other Location