Protein : Qrob_P0283380.2 Q. robur
Protein Identifier  ? Qrob_P0283380.2 Organism . Name  Quercus robur
Protein Description  (M=17) PTHR13683:SF232 - ASPARTYL PROTEASE FAMILY PROTEIN (PTHR13683:SF232) Alias (in v1)  Qrob_P0593890.1
Code Enzyme  EC:3.4.23.12 Gene Prediction Quality  manual_v1
Protein length 

Sequence

Length: 223  
Paste the following link
Lists
This Protein isn't in any lists. Upload a list.

Sequence Feature Displayer

Protein Sequence Displayer

J Browse Displayer

0 Synonyms

2 GO Terms

Identifier Name Description
GO:0006508 proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
GO:0004190 aspartic-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile.

20 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|cic:CICLE_v10025374mg 9 212 + 204 Gaps:9 54.01 387 55.50 2e-62 hypothetical protein
blastp_kegg lcl|ath:AT2G17760 11 210 + 200 Gaps:9 39.96 513 55.12 8e-62 aspartyl protease family protein
blastp_kegg lcl|cit:102612215 9 212 + 204 Gaps:9 40.43 517 55.98 1e-61 aspartic proteinase-like protein 1-like
blastp_kegg lcl|aly:ARALYDRAFT_480670 11 210 + 200 Gaps:9 39.96 513 54.63 3e-61 aspartyl protease family protein
blastp_kegg lcl|pmum:103340391 8 206 + 199 Gaps:11 39.85 517 56.31 5e-60 aspartic proteinase-like protein 1
blastp_kegg lcl|rcu:RCOM_0310740 10 212 + 203 Gaps:9 39.02 533 54.81 2e-59 Aspartic proteinase nepenthesin-1 precursor putative
blastp_kegg lcl|pper:PRUPE_ppa004265mg 8 206 + 199 Gaps:11 39.69 519 56.31 2e-59 hypothetical protein
blastp_kegg lcl|pmum:103340367 8 206 + 199 Gaps:14 41.80 500 55.98 5e-59 aspartic proteinase-like protein 1
blastp_kegg lcl|brp:103845921 14 210 + 197 Gaps:9 39.45 512 54.46 5e-59 aspartic proteinase-like protein 1
blastp_kegg lcl|brp:103874100 11 206 + 196 Gaps:9 39.33 511 54.23 7e-59 aspartic proteinase-like protein 1
blastp_uniprot_sprot sp|Q9LX20|ASPL1_ARATH 15 203 + 189 Gaps:17 38.26 528 39.11 2e-28 Aspartic proteinase-like protein 1 OS Arabidopsis thaliana GN At5g10080 PE 1 SV 1
blastp_uniprot_sprot sp|Q9S9K4|ASPL2_ARATH 14 205 + 192 Gaps:28 46.32 475 25.91 4e-08 Aspartic proteinase-like protein 2 OS Arabidopsis thaliana GN At1g65240 PE 1 SV 2
blastp_uniprot_sprot sp|Q766C2|NEP2_NEPGR 18 206 + 189 Gaps:27 45.21 438 30.81 5e-07 Aspartic proteinase nepenthesin-2 OS Nepenthes gracilis GN nep2 PE 1 SV 1
rpsblast_cdd gnl|CDD|133143 42 200 + 159 Gaps:34 63.02 265 29.94 1e-17 cd05476 pepsin_A_like_plant 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.
rpsblast_cdd gnl|CDD|133138 21 222 + 202 Gaps:34 76.33 283 25.00 2e-13 cd05471 pepsin_like 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).
rpsblast_cdd gnl|CDD|133142 50 222 + 173 Gaps:26 69.96 273 27.23 5e-10 cd05475 nucellin_like Nucellins plant aspartic proteases specifically expressed in nucellar cells during degradation. Nucellins are important regulators of nucellar cell's progressive degradation after ovule fertilization. This degradation is a characteristic of programmed cell death. Nucellins are plant aspartic proteases specifically expressed in nucellar cells during degradation. 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 and two other regions nearly identical to two regions of plant aspartic proteases. 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. Although the three-dimensional structures of the two lobes are very similar the amino acid sequences are more divergent except for the conserved catalytic site motif.
rpsblast_cdd gnl|CDD|133160 19 216 + 198 Gaps:33 67.79 326 22.17 2e-09 cd06096 Plasmepsin_5 Plasmepsins are a class of aspartic proteinases produced by the plasmodium parasite. The family contains a group of aspartic proteinases homologous to plasmepsin 5. Plasmepsins are a class of at least 10 enzymes produced by the plasmodium parasite. Through their haemoglobin-degrading activity they are an important cause of symptoms in malaria sufferers. This family of enzymes is a potential target for anti-malarial drugs. Plasmepsins are aspartic acid proteases which means their active site contains two aspartic acid residues. These two aspartic acid residue act respectively as proton donor and proton acceptor catalyzing the hydrolysis of peptide bond in proteins. Aspartic proteinases are composed of two structurally similar beta barrel lobes each lobe contributing an aspartic acid residue to form a catalytic dyad that acts to cleave the substrate peptide bond. The catalytic Asp residues are contained in an Asp-Thr-Gly-Ser/thr motif in both N- and C-terminal lobes of the enzyme. There are four types of plasmepsins closely related but varying in the specificity of cleavage site. The name plasmepsin may come from plasmodium (the organism) and pepsin (a common aspartic acid protease with similar molecular structure). This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A clan AA).
rpsblast_cdd gnl|CDD|133139 50 201 + 152 Gaps:24 52.84 299 32.28 5e-09 cd05472 cnd41_like 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).
rpsblast_cdd gnl|CDD|133156 20 173 + 154 Gaps:35 51.10 362 27.57 1e-08 cd05489 xylanase_inhibitor_I_like 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).
rpsblast_kog gnl|CDD|36553 18 207 + 190 Gaps:24 51.76 398 31.55 8e-24 KOG1339 KOG1339 KOG1339 Aspartyl protease [Posttranslational modification protein turnover chaperones].

7 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 9 217 209 PTHR13683:SF232 none none none
Pfam 17 144 128 PF14543 none Xylanase inhibitor N-terminal none
Gene3D 24 129 106 G3DSA:2.40.70.10 none none IPR021109
SUPERFAMILY 13 208 196 SSF50630 none none IPR021109
ProSitePatterns 184 195 12 PS00141 none Eukaryotic and viral aspartyl proteases active site. IPR001969
PANTHER 9 217 209 PTHR13683 none none IPR001461
Gene3D 130 207 78 G3DSA:2.40.70.10 none none IPR021109

0 Localization

0 Qtllist

0 Targeting