Eukaryotic aspartyl protease family protein [Arabidopsis thaliana]
Protein Classification
xylanase_inhibitor_I_like domain-containing protein( domain architecture ID 10144609)
xylanase_inhibitor_I_like domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| xylanase_inhibitor_I_like | cd05489 | TAXI-I inhibits degradation of xylan in the cell wall; Xylanase inhibitor-I (TAXI-I) is a ... |
36-392 | 2.05e-150 | ||||||
TAXI-I inhibits degradation of xylan in the cell wall; Xylanase inhibitor-I (TAXI-I) is a member of potent TAXI-type inhibitors of fungal and bacterial family 11 xylanases. Plants developed a diverse battery of defense mechanisms in response to continual challenges by a broad spectrum of pathogenic microorganisms. Their defense arsenal includes inhibitors of cell wall-degrading enzymes, which hinder a possible invasion and colonization by antagonists. Xylanases of fungal and bacterial pathogens are the key enzymes in the degradation of xylan in the cell wall. Plants secrete proteins that inhibit these degradation glycosidases, including xylanase. Surprisingly, TAXI-I displays structural homology with the pepsin-like family of aspartic proteases but is proteolytically nonfunctional, because one or more residues of the essential catalytic triad are absent. The structure of the TAXI-inhibitor, Aspergillus niger xylanase I complex, illustrates the ability of tight binding and inhibition with subnanomolar affinity and indicates the importance of the C-terminal end for the differences in xylanase specificity among different TAXI-type inhibitors. This family also contains pepsin-like aspartic proteinases homologous to TAXI-I. Unlike TAXI-I, they have active site aspartates and are functionally active. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA). : Pssm-ID: 133156 [Multi-domain] Cd Length: 362 Bit Score: 430.23 E-value: 2.05e-150
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| Name | Accession | Description | Interval | E-value | ||||||
| xylanase_inhibitor_I_like | cd05489 | TAXI-I inhibits degradation of xylan in the cell wall; Xylanase inhibitor-I (TAXI-I) is a ... |
36-392 | 2.05e-150 | ||||||
TAXI-I inhibits degradation of xylan in the cell wall; Xylanase inhibitor-I (TAXI-I) is a member of potent TAXI-type inhibitors of fungal and bacterial family 11 xylanases. Plants developed a diverse battery of defense mechanisms in response to continual challenges by a broad spectrum of pathogenic microorganisms. Their defense arsenal includes inhibitors of cell wall-degrading enzymes, which hinder a possible invasion and colonization by antagonists. Xylanases of fungal and bacterial pathogens are the key enzymes in the degradation of xylan in the cell wall. Plants secrete proteins that inhibit these degradation glycosidases, including xylanase. Surprisingly, TAXI-I displays structural homology with the pepsin-like family of aspartic proteases but is proteolytically nonfunctional, because one or more residues of the essential catalytic triad are absent. The structure of the TAXI-inhibitor, Aspergillus niger xylanase I complex, illustrates the ability of tight binding and inhibition with subnanomolar affinity and indicates the importance of the C-terminal end for the differences in xylanase specificity among different TAXI-type inhibitors. This family also contains pepsin-like aspartic proteinases homologous to TAXI-I. Unlike TAXI-I, they have active site aspartates and are functionally active. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA). Pssm-ID: 133156 [Multi-domain] Cd Length: 362 Bit Score: 430.23 E-value: 2.05e-150
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| TAXi_C | pfam14541 | Xylanase inhibitor C-terminal; The N- and C-termini of the members of this family are jointly ... |
238-389 | 4.57e-53 | ||||||
Xylanase inhibitor C-terminal; The N- and C-termini of the members of this family are jointly necessary for creating the catalytic pocket necessary for cleaving xylasnase. Phytopathogens produce xylanase that destroys plant cells, so its destruction through proteolysis is vital for plant-survival. Pssm-ID: 434029 Cd Length: 160 Bit Score: 174.00 E-value: 4.57e-53
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| PLN03146 | PLN03146 | aspartyl protease family protein; Provisional |
161-380 | 1.25e-08 | ||||||
aspartyl protease family protein; Provisional Pssm-ID: 178691 [Multi-domain] Cd Length: 431 Bit Score: 56.56 E-value: 1.25e-08
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| Name | Accession | Description | Interval | E-value | ||||||
| xylanase_inhibitor_I_like | cd05489 | TAXI-I inhibits degradation of xylan in the cell wall; Xylanase inhibitor-I (TAXI-I) is a ... |
36-392 | 2.05e-150 | ||||||
TAXI-I inhibits degradation of xylan in the cell wall; Xylanase inhibitor-I (TAXI-I) is a member of potent TAXI-type inhibitors of fungal and bacterial family 11 xylanases. Plants developed a diverse battery of defense mechanisms in response to continual challenges by a broad spectrum of pathogenic microorganisms. Their defense arsenal includes inhibitors of cell wall-degrading enzymes, which hinder a possible invasion and colonization by antagonists. Xylanases of fungal and bacterial pathogens are the key enzymes in the degradation of xylan in the cell wall. Plants secrete proteins that inhibit these degradation glycosidases, including xylanase. Surprisingly, TAXI-I displays structural homology with the pepsin-like family of aspartic proteases but is proteolytically nonfunctional, because one or more residues of the essential catalytic triad are absent. The structure of the TAXI-inhibitor, Aspergillus niger xylanase I complex, illustrates the ability of tight binding and inhibition with subnanomolar affinity and indicates the importance of the C-terminal end for the differences in xylanase specificity among different TAXI-type inhibitors. This family also contains pepsin-like aspartic proteinases homologous to TAXI-I. Unlike TAXI-I, they have active site aspartates and are functionally active. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA). Pssm-ID: 133156 [Multi-domain] Cd Length: 362 Bit Score: 430.23 E-value: 2.05e-150
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| TAXi_C | pfam14541 | Xylanase inhibitor C-terminal; The N- and C-termini of the members of this family are jointly ... |
238-389 | 4.57e-53 | ||||||
Xylanase inhibitor C-terminal; The N- and C-termini of the members of this family are jointly necessary for creating the catalytic pocket necessary for cleaving xylasnase. Phytopathogens produce xylanase that destroys plant cells, so its destruction through proteolysis is vital for plant-survival. Pssm-ID: 434029 Cd Length: 160 Bit Score: 174.00 E-value: 4.57e-53
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| pepsin_A_like_plant | cd05476 | Chroloplast Nucleoids DNA-binding Protease and Nucellin, pepsin-like aspartic proteases from ... |
122-388 | 1.38e-27 | ||||||
Chroloplast Nucleoids DNA-binding Protease and Nucellin, pepsin-like aspartic proteases from plants; This family contains pepsin like aspartic proteases from plants including Chloroplast Nucleoids DNA-binding Protease and Nucellin. Chloroplast Nucleoids DNA-binding Protease catalyzes the degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) in senescent leaves of tobacco and Nucellins are important regulators of nucellar cell's progressive degradation after ovule fertilization. Structurally, aspartic proteases are bilobal enzymes, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except the vicinity of the active site. This suggests that the enzymes evolved by an ancient duplication event. The enzymes specifically cleave bonds in peptides which have at least six residues in length with hydrophobic residues in both the P1 and P1' positions. The active site is located at the groove formed by the two lobes, with an extended loop projecting over the cleft to form an 11-residue flap, which encloses substrates and inhibitors in the active site. Specificity is determined by nearest-neighbor hydrophobic residues surrounding the catalytic aspartates, and by three residues in the flap. The enzymes are mostly secreted from cells as inactive proenzymes that activate autocatalytically at acidic pH. Pssm-ID: 133143 [Multi-domain] Cd Length: 265 Bit Score: 110.05 E-value: 1.38e-27
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| cnd41_like | cd05472 | Chloroplast Nucleoids DNA-binding Protease, catalyzes the degradation of ribulose-1, ... |
123-390 | 7.74e-22 | ||||||
Chloroplast Nucleoids DNA-binding Protease, catalyzes the degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase; Chloroplast Nucleoids DNA-binding Protease catalyzes the degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) in senescent leaves of tobacco. Antisense tobacco with reduced amount of CND41 maintained green leaves and constant protein levels, especially Rubisco. CND41 has DNA-binding as well as aspartic protease activities. The pepsin-like aspartic protease domain is located at the C-terminus of the protein. The enzyme is characterized by having two aspartic protease catalytic site motifs, the Asp-Thr-Gly-Ser in the N-terminal and Asp-Ser-Gly-Ser in the C-terminal region. Aspartic proteases are bilobal enzymes, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. One lobe may be evolved from the other through ancient gene-duplication event. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA). Pssm-ID: 133139 [Multi-domain] Cd Length: 299 Bit Score: 94.65 E-value: 7.74e-22
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| TAXi_N | pfam14543 | Xylanase inhibitor N-terminal; The N- and C-termini of the members of this family are jointly ... |
63-210 | 9.18e-11 | ||||||
Xylanase inhibitor N-terminal; The N- and C-termini of the members of this family are jointly necessary for creating the catalytic pocket necessary for cleaving xylanase. Phytopathogens produce xylanase that destroys plant cells, so its destruction through proteolysis is vital for plant-survival. Pssm-ID: 464203 [Multi-domain] Cd Length: 172 Bit Score: 60.37 E-value: 9.18e-11
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| pepsin_like | cd05471 | Pepsin-like aspartic proteases, bilobal enzymes that cleave bonds in peptides at acidic pH; ... |
87-388 | 9.46e-11 | ||||||
Pepsin-like aspartic proteases, bilobal enzymes that cleave bonds in peptides at acidic pH; Pepsin-like aspartic proteases are found in mammals, plants, fungi and bacteria. These well known and extensively characterized enzymes include pepsins, chymosin, renin, cathepsins, and fungal aspartic proteases. Several have long been known to be medically (renin, cathepsin D and E, pepsin) or commercially (chymosin) important. Structurally, aspartic proteases are bilobal enzymes, each lobe contributing a catalytic Aspartate residue, with an extended active site cleft localized between the two lobes of the molecule. The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except the vicinity of the active site. This suggests that the enzymes evolved by an ancient duplication event. Most members of the pepsin family specifically cleave bonds in peptides that are at least six residues in length, with hydrophobic residues in both the P1 and P1' positions. The active site is located at the groove formed by the two lobes, with an extended loop projecting over the cleft to form an 11-residue flap, which encloses substrates and inhibitors in the active site. Specificity is determined by nearest-neighbor hydrophobic residues surrounding the catalytic aspartates, and by three residues in the flap.The enzymes are mostly secreted from cells as inactive proenzymes that activate autocatalytically at acidic pH. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA). Pssm-ID: 133138 [Multi-domain] Cd Length: 283 Bit Score: 62.06 E-value: 9.46e-11
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| PLN03146 | PLN03146 | aspartyl protease family protein; Provisional |
161-380 | 1.25e-08 | ||||||
aspartyl protease family protein; Provisional Pssm-ID: 178691 [Multi-domain] Cd Length: 431 Bit Score: 56.56 E-value: 1.25e-08
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| Blast search parameters | ||||
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