Protein : Qrob_P0126240.2 Q. robur
Protein Identifier  ? Qrob_P0126240.2 Organism . Name  Quercus robur
Score  0.0 Score Type  egn
Protein Description  (M=17) PTHR13683:SF223 - ASPARTYL PROTEASE FAMILY PROTEIN (PTHR13683:SF223) Code Enzyme  EC:3.4.23.12
Gene Prediction Quality  validated Protein length 

Sequence

Length: 396  
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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.

31 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|zma:103645762 4 394 + 391 Gaps:35 80.60 464 32.35 8e-53 protein ASPARTIC PROTEASE IN GUARD CELL 2
blastp_kegg lcl|sbi:SORBI_06g032900 15 394 + 380 Gaps:35 77.92 471 32.70 7e-51 SORBIDRAFT_06g032900 Sb06g032900 hypothetical protein
blastp_kegg lcl|cic:CICLE_v10025623mg 34 394 + 361 Gaps:27 79.00 438 35.55 2e-50 hypothetical protein
blastp_kegg lcl|cit:102623581 34 394 + 361 Gaps:27 79.00 438 35.26 7e-50 aspartic proteinase nepenthesin-1-like
blastp_kegg lcl|sita:101769974 30 394 + 365 Gaps:31 74.79 468 34.00 1e-49 protein ASPARTIC PROTEASE IN GUARD CELL 2-like
blastp_kegg lcl|zma:103645760 4 394 + 391 Gaps:39 84.16 461 31.96 7e-49 protein ASPARTIC PROTEASE IN GUARD CELL 2-like
blastp_kegg lcl|sita:101781702 36 394 + 359 Gaps:27 81.09 439 33.15 2e-48 aspartic proteinase nepenthesin-1-like
blastp_kegg lcl|cam:101513423 25 394 + 370 Gaps:34 99.20 373 33.24 2e-48 protein ASPARTIC PROTEASE IN GUARD CELL 1-like
blastp_kegg lcl|brp:103838036 33 394 + 362 Gaps:24 68.54 499 37.13 2e-48 protein ASPARTIC PROTEASE IN GUARD CELL 1
blastp_kegg lcl|mus:103983456 33 394 + 362 Gaps:28 68.20 522 36.80 5e-48 protein ASPARTIC PROTEASE IN GUARD CELL 1-like
blastp_uniprot_sprot sp|Q9LS40|ASPG1_ARATH 33 394 + 362 Gaps:24 68.40 500 35.09 2e-46 Protein ASPARTIC PROTEASE IN GUARD CELL 1 OS Arabidopsis thaliana GN ASPG1 PE 1 SV 1
blastp_uniprot_sprot sp|Q766C2|NEP2_NEPGR 33 394 + 362 Gaps:33 78.31 438 32.07 4e-46 Aspartic proteinase nepenthesin-2 OS Nepenthes gracilis GN nep2 PE 1 SV 1
blastp_uniprot_sprot sp|Q9LHE3|ASPG2_ARATH 1 394 + 394 Gaps:30 80.00 470 31.65 5e-41 Protein ASPARTIC PROTEASE IN GUARD CELL 2 OS Arabidopsis thaliana GN ASPG2 PE 2 SV 1
blastp_uniprot_sprot sp|Q766C3|NEP1_NEPGR 33 394 + 362 Gaps:33 78.49 437 32.07 2e-39 Aspartic proteinase nepenthesin-1 OS Nepenthes gracilis GN nep1 PE 1 SV 1
blastp_uniprot_sprot sp|Q6XBF8|CDR1_ARATH 33 394 + 362 Gaps:32 79.63 437 31.03 8e-32 Aspartic proteinase CDR1 OS Arabidopsis thaliana GN CDR1 PE 1 SV 1
blastp_uniprot_sprot sp|Q3EBM5|ASPR1_ARATH 8 357 + 350 Gaps:29 78.52 447 28.49 7e-28 Probable aspartic protease At2g35615 OS Arabidopsis thaliana GN At2g35615 PE 3 SV 1
blastp_uniprot_sprot sp|Q9LZL3|PCS1L_ARATH 45 394 + 350 Gaps:51 79.69 453 29.09 2e-26 Aspartic proteinase PCS1 OS Arabidopsis thaliana GN PCS1 PE 2 SV 1
blastp_uniprot_sprot sp|Q9S9K4|ASPL2_ARATH 34 347 + 314 Gaps:62 66.11 475 28.98 4e-21 Aspartic proteinase-like protein 2 OS Arabidopsis thaliana GN At1g65240 PE 1 SV 2
blastp_uniprot_sprot sp|Q9LX20|ASPL1_ARATH 35 394 + 360 Gaps:61 67.23 528 23.10 1e-13 Aspartic proteinase-like protein 1 OS Arabidopsis thaliana GN At5g10080 PE 1 SV 1
blastp_uniprot_sprot sp|A2ZC67|ASP1_ORYSI 34 387 + 354 Gaps:60 81.46 410 25.15 6e-08 Aspartic proteinase Asp1 OS Oryza sativa subsp. indica GN ASP1 PE 2 SV 2
rpsblast_cdd gnl|CDD|133143 36 394 + 359 Gaps:105 99.62 265 34.47 4e-42 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|133139 36 394 + 359 Gaps:73 99.67 299 32.21 1e-41 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|178691 39 357 + 319 Gaps:54 71.69 431 31.07 6e-39 PLN03146 PLN03146 aspartyl protease family protein Provisional.
rpsblast_cdd gnl|CDD|133138 36 329 + 294 Gaps:78 91.17 283 28.68 8e-26 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|133156 36 375 + 340 Gaps:64 95.03 362 23.26 1e-13 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_cdd gnl|CDD|133160 33 283 + 251 Gaps:67 76.69 326 27.20 5e-11 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|133142 34 283 + 250 Gaps:82 71.79 273 34.18 5e-11 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|133137 39 174 + 136 Gaps:32 99.08 109 33.33 2e-09 cd05470 pepsin_retropepsin_like Cellular and retroviral pepsin-like aspartate proteases. This family includes both cellular and retroviral pepsin-like aspartate proteases. The cellular pepsin and pepsin-like enzymes are twice as long as their retroviral counterparts. The cellular pepsin-like aspartic proteases are found in mammals plants fungi and bacteria. These well known and extensively characterized enzymes include pepsins chymosin rennin cathepsins and fungal aspartic proteases. Several have long been known to be medically (rennin cathepsin D and E pepsin) or commercially (chymosin) important. The eukaryotic pepsin-like proteases contain two domains possessing similar topological features. The N- and C-terminal domains although structurally related by a 2-fold axis have only limited sequence homology except in the vicinity of the active site. This suggests that the enzymes evolved by an ancient duplication event. The eukaryotic pepsin-like proteases have two active site ASP residues with each N- and C-terminal lobe contributing one residue. While the fungal and mammalian pepsins are bilobal proteins retropepsins function as dimers and the monomer resembles structure of the N- or C-terminal domains of eukaryotic enzyme. The active site motif (Asp-Thr/Ser-Gly-Ser) is conserved between the retroviral and eukaryotic proteases and between the N-and C-terminal of eukaryotic pepsin-like proteases. The retropepsin-like family includes pepsin-like aspartate proteases from retroviruses retrotransposons and retroelements as well as eukaryotic DNA-damage-inducible proteins (DDIs) and bacterial aspartate peptidases. Retropepsin is synthesized as part of the POL polyprotein that contains an aspartyl-protease a reverse transcriptase RNase H and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A) and A2 (retropepsin family).
rpsblast_cdd gnl|CDD|133161 36 190 + 155 Gaps:37 46.04 278 30.47 4e-07 cd06097 Aspergillopepsin_like Aspergillopepsin_like aspartic proteases of fungal origin. The members of this family are aspartic proteases of fungal origin including aspergillopepsin rhizopuspepsin endothiapepsin and rodosporapepsin. The various fungal species in this family may be the most economically important genus of fungi. They may serve as virulence factors or as industrial aids. For example Aspergillopepsin from A. fumigatus is involved in invasive aspergillosis owing to its elastolytic activity and Aspergillopepsins from the mold A. saitoi are used in fermentation industry. Aspartic proteinases are a group of proteolytic enzymes in which the scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in a DT(S)G motif at the active site. They have a similar fold composed of two beta-barrel domains. Between the N-terminal and C-terminal domains each of which contributes one catalytic aspartic residue there is an extended active-site cleft capable of interacting with multiple residues of a substrate. Although members of the aspartic protease family of enzymes have very similar three-dimensional structures and catalytic mechanisms each has unique substrate specificity. The members of this family has an optimal acidic pH (5.5) and cleaves protein substrates with similar specificity to that of porcine pepsin A preferring hydrophobic residues at P1 and P1' in the cleave site. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A clan AA).
rpsblast_cdd gnl|CDD|133141 121 288 + 168 Gaps:50 58.31 295 24.42 6e-07 cd05474 SAP_like SAPs pepsin-like proteinases secreted from pathogens to degrade host proteins. SAPs (Secreted aspartic proteinases) are secreted from a group of pathogenic fungi predominantly Candida species. They are secreted from the pathogen to degrade host proteins. SAP is one of the most significant extracellular hydrolytic enzymes produced by C. albicans. SAP proteins encoded by a family of 10 SAP genes. All 10 SAP genes of C. albicans encode preproenzymes approximately 60 amino acid longer than the mature enzyme which are processed when transported via the secretory pathway. The mature enzymes contain sequence motifs typical for all aspartyl proteinases including the two conserved aspartate residues other active site and conserved cysteine residues implicated in the maintenance of the three-dimensional structure. Most Sap proteins contain putative N-glycosylation sites but it remains to be determined which Sap proteins are glycosylated. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A clan AA). The overall structure of Sap protein conforms to the classical aspartic proteinase fold typified by pepsin. SAP is a bilobal enzyme 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. More recently evolved enzymes have similar three-dimensional structures however their amino acid sequences are more divergent except for the conserved catalytic site motif. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A clan AA).

10 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Pfam 36 196 161 PF14543 none Xylanase inhibitor N-terminal none
Pfam 231 389 159 PF14541 none Xylanase inhibitor C-terminal none
SUPERFAMILY 29 394 366 SSF50630 none none IPR021109
PANTHER 14 93 80 PTHR13683 none none IPR001461
PANTHER 115 394 280 PTHR13683 none none IPR001461
PANTHER 14 93 80 PTHR13683:SF223 none none none
PANTHER 115 394 280 PTHR13683:SF223 none none none
Gene3D 32 196 165 G3DSA:2.40.70.10 none none IPR021109
ProSitePatterns 267 278 12 PS00141 none Eukaryotic and viral aspartyl proteases active site. IPR001969
Gene3D 214 394 181 G3DSA:2.40.70.10 none none IPR021109

0 Localization

0 Qtllist

0 Targeting