Protein : Qrob_P0283050.2 Q. robur
Protein Identifier  ? Qrob_P0283050.2 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: 434  
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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.

29 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|vvi:100242231 36 430 + 395 Gaps:12 93.19 426 68.77 0.0 aspartic proteinase Asp1-like
blastp_kegg lcl|pmum:103327082 20 433 + 414 Gaps:15 95.40 435 69.40 0.0 aspartic proteinase Asp1
blastp_kegg lcl|pper:PRUPE_ppa005961mg 26 433 + 408 Gaps:16 95.17 435 68.84 0.0 hypothetical protein
blastp_kegg lcl|tcc:TCM_001596 55 429 + 375 Gaps:8 90.97 421 71.54 0.0 Aspartyl protease family protein isoform 2
blastp_kegg lcl|mdm:103424770 12 433 + 422 Gaps:20 98.14 430 64.93 0.0 aspartic proteinase Asp1-like
blastp_kegg lcl|pxb:103941657 9 433 + 425 Gaps:23 98.14 430 65.88 0.0 aspartic proteinase Asp1-like
blastp_kegg lcl|pxb:103946791 2 433 + 432 Gaps:25 99.30 430 65.34 0.0 aspartic proteinase Asp1-like
blastp_kegg lcl|csv:101208901 18 431 + 414 Gaps:19 99.76 418 65.23 0.0 aspartic proteinase Asp1-like
blastp_kegg lcl|pop:POPTR_0007s04800g 28 429 + 402 Gaps:12 94.42 430 68.72 0.0 POPTRDRAFT_217329 hypothetical protein
blastp_kegg lcl|eus:EUTSA_v10025289mg 58 430 + 373 Gaps:10 90.33 424 67.62 0.0 hypothetical protein
blastp_uniprot_sprot sp|Q0IU52|ASP1_ORYSJ 64 430 + 367 Gaps:23 93.66 410 48.18 2e-112 Aspartic proteinase Asp1 OS Oryza sativa subsp. japonica GN ASP1 PE 2 SV 1
blastp_uniprot_sprot sp|A2ZC67|ASP1_ORYSI 64 430 + 367 Gaps:23 93.66 410 45.83 1e-106 Aspartic proteinase Asp1 OS Oryza sativa subsp. indica GN ASP1 PE 2 SV 2
blastp_uniprot_sprot sp|Q9S9K4|ASPL2_ARATH 58 431 + 374 Gaps:49 81.47 475 28.42 3e-34 Aspartic proteinase-like protein 2 OS Arabidopsis thaliana GN At1g65240 PE 1 SV 2
blastp_uniprot_sprot sp|Q766C3|NEP1_NEPGR 56 421 + 366 Gaps:61 83.98 437 29.16 2e-22 Aspartic proteinase nepenthesin-1 OS Nepenthes gracilis GN nep1 PE 1 SV 1
blastp_uniprot_sprot sp|Q9LX20|ASPL1_ARATH 84 423 + 340 Gaps:70 66.67 528 28.98 2e-19 Aspartic proteinase-like protein 1 OS Arabidopsis thaliana GN At5g10080 PE 1 SV 1
blastp_uniprot_sprot sp|Q766C2|NEP2_NEPGR 78 421 + 344 Gaps:54 78.08 438 28.36 2e-19 Aspartic proteinase nepenthesin-2 OS Nepenthes gracilis GN nep2 PE 1 SV 1
blastp_uniprot_sprot sp|Q9LS40|ASPG1_ARATH 78 421 + 344 Gaps:65 68.20 500 27.57 1e-17 Protein ASPARTIC PROTEASE IN GUARD CELL 1 OS Arabidopsis thaliana GN ASPG1 PE 1 SV 1
blastp_uniprot_sprot sp|Q3EBM5|ASPR1_ARATH 78 421 + 344 Gaps:57 80.76 447 25.48 1e-13 Probable aspartic protease At2g35615 OS Arabidopsis thaliana GN At2g35615 PE 3 SV 1
blastp_uniprot_sprot sp|Q9LZL3|PCS1L_ARATH 98 422 + 325 Gaps:74 77.92 453 26.91 1e-11 Aspartic proteinase PCS1 OS Arabidopsis thaliana GN PCS1 PE 2 SV 1
blastp_uniprot_sprot sp|Q9LHE3|ASPG2_ARATH 50 194 + 145 Gaps:15 29.36 470 31.16 1e-10 Protein ASPARTIC PROTEASE IN GUARD CELL 2 OS Arabidopsis thaliana GN ASPG2 PE 2 SV 1
rpsblast_cdd gnl|CDD|133142 78 421 + 344 Gaps:91 100.00 273 63.00 1e-104 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 80 421 + 342 Gaps:122 99.62 265 38.26 2e-43 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 80 313 + 234 Gaps:41 82.33 283 27.04 6e-30 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 80 421 + 342 Gaps:78 99.67 299 29.19 8e-30 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 78 224 + 147 Gaps:8 34.57 431 33.56 5e-18 PLN03146 PLN03146 aspartyl protease family protein Provisional.
rpsblast_cdd gnl|CDD|133137 82 211 + 130 Gaps:23 100.00 109 28.44 4e-16 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 78 421 + 344 Gaps:96 99.39 326 24.07 1e-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|133156 88 418 + 331 Gaps:69 97.79 362 22.32 5e-09 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 36 422 + 387 Gaps:44 98.74 398 28.75 1e-51 KOG1339 KOG1339 KOG1339 Aspartyl protease [Posttranslational modification protein turnover chaperones].

12 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 8 424 417 PTHR13683 none none IPR001461
Phobius 1 30 30 SIGNAL_PEPTIDE none Signal peptide region none
Phobius 19 30 12 SIGNAL_PEPTIDE_C_REGION none C-terminal region of a signal peptide. none
Phobius 31 433 403 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Gene3D 271 424 154 G3DSA:2.40.70.10 none none IPR021109
Gene3D 65 248 184 G3DSA:2.40.70.10 none none IPR021109
SUPERFAMILY 72 425 354 SSF50630 none none IPR021109
Phobius 6 18 13 SIGNAL_PEPTIDE_H_REGION none Hydrophobic region of a signal peptide. none
Phobius 1 5 5 SIGNAL_PEPTIDE_N_REGION none N-terminal region of a signal peptide. none
Pfam 80 248 169 PF14543 none Xylanase inhibitor N-terminal none
Pfam 283 416 134 PF14541 none Xylanase inhibitor C-terminal none
PANTHER 8 424 417 PTHR13683:SF229 none none none

2 Localization

Analysis Start End Length
SignalP_GRAM_POSITIVE 1 29 28
SignalP_EUK 1 23 22

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

1 Targeting

Analysis Start End Length Location Reliability Signal Peptide Cut Off Mitochondrion Cut Off Network Signal Peptide Length
TargetP 1 23   Secretory pathway 3 0.920 0.373 NON-PLANT 23