Protein : Qrob_P0283480.2 Q. robur
Protein Identifier  ? Qrob_P0283480.2 Organism . Name  Quercus robur
Score  0.0 Score Type  egn
Protein Description  (M=17) PTHR13683:SF232 - ASPARTYL PROTEASE FAMILY PROTEIN (PTHR13683:SF232) Code Enzyme  EC:3.4.23.12
Gene Prediction Quality  validated Protein length 

Sequence

Length: 263  
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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.

16 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|cit:102612215 3 262 + 260 Gaps:32 56.48 517 51.71 1e-86 aspartic proteinase-like protein 1-like
blastp_kegg lcl|tcc:TCM_000144 15 262 + 248 Gaps:35 54.53 519 50.18 2e-83 Eukaryotic aspartyl protease family protein putative isoform 1
blastp_kegg lcl|rcu:RCOM_0310740 15 262 + 248 Gaps:31 52.35 533 49.82 8e-83 Aspartic proteinase nepenthesin-1 precursor putative
blastp_kegg lcl|brp:103874100 17 262 + 246 Gaps:32 54.01 511 49.28 4e-79 aspartic proteinase-like protein 1
blastp_kegg lcl|pper:PRUPE_ppa004265mg 16 262 + 247 Gaps:44 52.99 519 54.18 3e-78 hypothetical protein
blastp_kegg lcl|mdm:103455953 16 262 + 247 Gaps:41 53.00 517 52.55 9e-78 aspartic proteinase-like protein 1
blastp_kegg lcl|fve:101313637 15 262 + 248 Gaps:40 52.69 520 51.82 9e-78 aspartic proteinase-like protein 1-like
blastp_kegg lcl|pmum:103340391 16 262 + 247 Gaps:42 53.19 517 53.09 2e-77 aspartic proteinase-like protein 1
blastp_kegg lcl|brp:103845921 17 262 + 246 Gaps:32 53.91 512 48.55 3e-77 aspartic proteinase-like protein 1
blastp_kegg lcl|crb:CARUB_v10016111mg 17 262 + 246 Gaps:33 54.00 513 49.10 4e-77 hypothetical protein
blastp_uniprot_sprot sp|Q9LX20|ASPL1_ARATH 18 251 + 234 Gaps:45 50.95 528 30.48 5e-24 Aspartic proteinase-like protein 1 OS Arabidopsis thaliana GN At5g10080 PE 1 SV 1
rpsblast_cdd gnl|CDD|133143 45 261 + 217 Gaps:103 80.00 265 29.72 1e-11 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|133142 45 192 + 148 Gaps:45 65.57 273 25.70 4e-08 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|133138 28 189 + 162 Gaps:49 71.02 283 21.89 5e-08 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|133139 103 261 + 159 Gaps:18 57.19 299 26.90 1e-07 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_kog gnl|CDD|36553 21 261 + 241 Gaps:51 70.35 398 25.00 1e-19 KOG1339 KOG1339 KOG1339 Aspartyl protease [Posttranslational modification protein turnover chaperones].

7 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Gene3D 27 88 62 G3DSA:2.40.70.10 none none IPR021109
Gene3D 125 258 134 G3DSA:2.40.70.10 none none IPR021109
PANTHER 10 261 252 PTHR13683 none none IPR001461
ProSitePatterns 161 172 12 PS00141 none Eukaryotic and viral aspartyl proteases active site. IPR001969
Pfam 141 261 121 PF14541 none Xylanase inhibitor C-terminal none
SUPERFAMILY 18 261 244 SSF50630 none none IPR021109
PANTHER 10 261 252 PTHR13683:SF232 none none none

0 Localization

0 Qtllist

0 Targeting