Protein : Qrob_P0283450.2 Q. robur
Protein Identifier  ? Qrob_P0283450.2 Organism . Name  Quercus robur
Score  0.0 Score Type  egn
Protein Description  (M=17) PTHR13683:SF232 - ASPARTYL PROTEASE FAMILY PROTEIN (PTHR13683:SF232) Gene Prediction Quality  validated
Protein length 

Sequence

Length: 188  
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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.

17 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pxb:103936704 13 180 + 168 Gaps:55 43.13 517 47.09 7e-53 aspartic proteinase-like protein 1
blastp_kegg lcl|mdm:103455953 13 180 + 168 Gaps:55 43.13 517 46.64 1e-52 aspartic proteinase-like protein 1
blastp_kegg lcl|pmum:103340367 13 184 + 172 Gaps:59 46.20 500 45.02 2e-51 aspartic proteinase-like protein 1
blastp_kegg lcl|pmum:103340391 13 184 + 172 Gaps:56 44.10 517 45.18 5e-50 aspartic proteinase-like protein 1
blastp_kegg lcl|pxb:103953443 13 180 + 168 Gaps:56 42.59 526 45.54 8e-49 aspartic proteinase-like protein 1
blastp_kegg lcl|pxb:103942516 13 180 + 168 Gaps:56 41.56 539 45.54 8e-49 aspartic proteinase-like protein 1
blastp_kegg lcl|pxb:103942515 13 180 + 168 Gaps:56 41.56 539 45.54 8e-49 aspartic proteinase-like protein 1
blastp_kegg lcl|pper:PRUPE_ppa004265mg 13 184 + 172 Gaps:56 43.93 519 43.42 9e-49 hypothetical protein
blastp_kegg lcl|ath:AT2G17760 13 180 + 168 Gaps:59 44.25 513 41.41 1e-48 aspartyl protease family protein
blastp_kegg lcl|crb:CARUB_v10016111mg 13 180 + 168 Gaps:59 44.25 513 42.29 1e-48 hypothetical protein
blastp_uniprot_sprot sp|Q9LX20|ASPL1_ARATH 6 181 + 176 Gaps:62 44.32 528 31.62 5e-27 Aspartic proteinase-like protein 1 OS Arabidopsis thaliana GN At5g10080 PE 1 SV 1
rpsblast_cdd gnl|CDD|133143 15 180 + 166 Gaps:46 75.47 265 25.00 5e-18 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 15 177 + 163 Gaps:35 68.55 283 27.84 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 13 180 + 168 Gaps:39 72.89 273 28.64 5e-13 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|133139 15 130 + 116 Gaps:17 41.14 299 33.33 3e-08 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|133160 15 180 + 166 Gaps:49 64.72 326 20.38 2e-07 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_kog gnl|CDD|36553 15 180 + 166 Gaps:22 46.73 398 25.27 7e-16 KOG1339 KOG1339 KOG1339 Aspartyl protease [Posttranslational modification protein turnover chaperones].

8 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
SUPERFAMILY 14 180 167 SSF50630 none none IPR021109
PANTHER 13 180 168 PTHR13683:SF232 none none none
Gene3D 13 62 50 G3DSA:2.40.70.10 none none IPR021109
Pfam 15 127 113 PF00026 none Eukaryotic aspartyl protease IPR001461
PANTHER 13 180 168 PTHR13683 none none IPR001461
ProSitePatterns 114 125 12 PS00141 none Eukaryotic and viral aspartyl proteases active site. IPR001969
Gene3D 134 181 48 G3DSA:2.40.70.10 none none IPR021109
Gene3D 63 131 69 G3DSA:2.40.70.10 none none IPR021109

0 Localization

0 Qtllist

1 Targeting

Analysis Start End Length Location Reliability Signal Peptide Cut Off Mitochondrion Cut Off Network Signal Peptide Length
TargetP 1 18   Secretory pathway 3 0.791 0.024 NON-PLANT 18