Protein : Qrob_P0283100.2 Q. robur
Protein Identifier  ? Qrob_P0283100.2 Organism . Name  Quercus robur
Score  100.0 Score Type  egn
Protein Description  (M=4) PTHR13683//PTHR13683:SF229 - ASPARTYL PROTEASES // SUBFAMILY NOT NAMED Code Enzyme  EC:3.4.23.12
Gene Prediction Quality  validated Protein length 

Sequence

Length: 364  
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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.

28 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pxb:103941657 4 361 + 358 Gaps:7 83.49 430 65.18 4e-157 aspartic proteinase Asp1-like
blastp_kegg lcl|pxb:103946791 4 361 + 358 Gaps:7 83.49 430 65.18 2e-156 aspartic proteinase Asp1-like
blastp_kegg lcl|mdm:103424770 4 361 + 358 Gaps:7 83.49 430 64.90 6e-156 aspartic proteinase Asp1-like
blastp_kegg lcl|vvi:100242231 1 361 + 361 Gaps:6 84.74 426 62.05 2e-155 aspartic proteinase Asp1-like
blastp_kegg lcl|tcc:TCM_001596 3 360 + 358 Gaps:7 85.27 421 64.35 4e-154 Aspartyl protease family protein isoform 2
blastp_kegg lcl|pmum:103327082 4 363 + 360 Gaps:7 82.99 435 66.20 5e-152 aspartic proteinase Asp1
blastp_kegg lcl|pper:PRUPE_ppa005961mg 4 363 + 360 Gaps:7 82.99 435 65.65 9e-152 hypothetical protein
blastp_kegg lcl|cit:102614284 3 362 + 360 Gaps:6 82.57 436 63.33 1e-149 aspartic proteinase Asp1-like
blastp_kegg lcl|cic:CICLE_v10001122mg 3 360 + 358 Gaps:6 79.38 451 63.69 1e-149 hypothetical protein
blastp_kegg lcl|pxb:103946792 4 361 + 358 Gaps:9 83.41 428 63.59 2e-149 aspartic proteinase Asp1-like
blastp_uniprot_sprot sp|Q0IU52|ASP1_ORYSJ 4 360 + 357 Gaps:26 89.51 410 44.41 2e-91 Aspartic proteinase Asp1 OS Oryza sativa subsp. japonica GN ASP1 PE 2 SV 1
blastp_uniprot_sprot sp|A2ZC67|ASP1_ORYSI 4 361 + 358 Gaps:26 89.76 410 43.48 9e-88 Aspartic proteinase Asp1 OS Oryza sativa subsp. indica GN ASP1 PE 2 SV 2
blastp_uniprot_sprot sp|Q9S9K4|ASPL2_ARATH 8 352 + 345 Gaps:46 73.47 475 26.93 1e-25 Aspartic proteinase-like protein 2 OS Arabidopsis thaliana GN At1g65240 PE 1 SV 2
blastp_uniprot_sprot sp|Q9LX20|ASPL1_ARATH 8 350 + 343 Gaps:64 66.10 528 27.51 8e-17 Aspartic proteinase-like protein 1 OS Arabidopsis thaliana GN At5g10080 PE 1 SV 1
blastp_uniprot_sprot sp|Q9LZL3|PCS1L_ARATH 22 353 + 332 Gaps:55 77.92 453 28.05 2e-16 Aspartic proteinase PCS1 OS Arabidopsis thaliana GN PCS1 PE 2 SV 1
blastp_uniprot_sprot sp|Q766C2|NEP2_NEPGR 6 350 + 345 Gaps:44 76.94 438 26.41 1e-15 Aspartic proteinase nepenthesin-2 OS Nepenthes gracilis GN nep2 PE 1 SV 1
blastp_uniprot_sprot sp|Q766C3|NEP1_NEPGR 6 350 + 345 Gaps:72 77.12 437 27.89 1e-15 Aspartic proteinase nepenthesin-1 OS Nepenthes gracilis GN nep1 PE 1 SV 1
blastp_uniprot_sprot sp|Q3EBM5|ASPR1_ARATH 4 346 + 343 Gaps:55 79.19 447 27.40 3e-13 Probable aspartic protease At2g35615 OS Arabidopsis thaliana GN At2g35615 PE 3 SV 1
blastp_uniprot_sprot sp|Q9LS40|ASPG1_ARATH 8 350 + 343 Gaps:55 66.80 500 28.14 1e-12 Protein ASPARTIC PROTEASE IN GUARD CELL 1 OS Arabidopsis thaliana GN ASPG1 PE 1 SV 1
blastp_uniprot_sprot sp|Q9LHE3|ASPG2_ARATH 6 349 + 344 Gaps:48 71.49 470 28.57 3e-12 Protein ASPARTIC PROTEASE IN GUARD CELL 2 OS Arabidopsis thaliana GN ASPG2 PE 2 SV 1
rpsblast_cdd gnl|CDD|133142 3 352 + 350 Gaps:88 99.63 273 57.35 7e-90 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|133143 6 352 + 347 Gaps:123 98.87 265 40.08 8e-44 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 6 350 + 345 Gaps:72 98.66 299 31.53 5e-35 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|133138 6 348 + 343 Gaps:92 99.29 283 24.56 9e-29 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|178691 8 149 + 142 Gaps:12 32.95 431 33.80 8e-17 PLN03146 PLN03146 aspartyl protease family protein Provisional.
rpsblast_cdd gnl|CDD|133137 6 137 + 132 Gaps:25 100.00 109 30.28 9e-12 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|133160 3 352 + 350 Gaps:83 99.08 326 22.60 3e-08 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 3 348 + 346 Gaps:38 86.93 398 30.64 1e-48 KOG1339 KOG1339 KOG1339 Aspartyl protease [Posttranslational modification protein turnover chaperones].

7 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Pfam 6 174 169 PF14543 none Xylanase inhibitor N-terminal none
Pfam 213 347 135 PF14541 none Xylanase inhibitor C-terminal none
SUPERFAMILY 4 350 347 SSF50630 none none IPR021109
Gene3D 6 174 169 G3DSA:2.40.70.10 none none IPR021109
Gene3D 183 351 169 G3DSA:2.40.70.10 none none IPR021109
PANTHER 3 355 353 PTHR13683 none none IPR001461
PANTHER 3 355 353 PTHR13683:SF229 none none none

0 Localization

2 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran2_2002_QTL13_peak_Bud_burst_3P Qrob_Chr10 10 s_1B1AG7_637 s_1A3A1N_709 19,44 0 49,44 lod 3 5,6
Champenoux_2015_nPriLBD_3P Qrob_Chr10 10 v_15000_157 v_15000_310 15,68 15,9 15,91 lod 2.4 5.5

0 Targeting