Protein : Qrob_P0283110.2 Q. robur
Protein Identifier  ? Qrob_P0283110.2 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: 395  
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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.

30 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|vvi:100242231 14 392 + 379 Gaps:1 89.20 426 71.84 0.0 aspartic proteinase Asp1-like
blastp_kegg lcl|pxb:103941657 8 392 + 385 Gaps:2 90.00 430 70.54 0.0 aspartic proteinase Asp1-like
blastp_kegg lcl|pxb:103946791 20 392 + 373 Gaps:2 87.21 430 72.00 0.0 aspartic proteinase Asp1-like
blastp_kegg lcl|pper:PRUPE_ppa005961mg 2 394 + 393 Gaps:3 90.57 435 72.08 0.0 hypothetical protein
blastp_kegg lcl|pmum:103327082 2 394 + 393 Gaps:3 90.57 435 72.59 0.0 aspartic proteinase Asp1
blastp_kegg lcl|mdm:103424770 13 392 + 380 Gaps:3 89.07 430 70.76 0.0 aspartic proteinase Asp1-like
blastp_kegg lcl|aly:ARALYDRAFT_328390 15 392 + 378 Gaps:4 89.88 425 69.11 0.0 hypothetical protein
blastp_kegg lcl|tcc:TCM_001596 13 391 + 379 Gaps:2 90.50 421 71.39 0.0 Aspartyl protease family protein isoform 2
blastp_kegg lcl|pop:POPTR_0005s07070g 3 391 + 389 Gaps:4 99.24 394 73.15 0.0 POPTRDRAFT_207235 hypothetical protein
blastp_kegg lcl|ath:AT4G33490 15 392 + 378 Gaps:4 89.88 425 68.85 0.0 aspartyl protease family protein
blastp_uniprot_sprot sp|Q0IU52|ASP1_ORYSJ 20 391 + 372 Gaps:19 93.41 410 46.74 3e-113 Aspartic proteinase Asp1 OS Oryza sativa subsp. japonica GN ASP1 PE 2 SV 1
blastp_uniprot_sprot sp|A2ZC67|ASP1_ORYSI 20 392 + 373 Gaps:19 93.66 410 45.57 1e-107 Aspartic proteinase Asp1 OS Oryza sativa subsp. indica GN ASP1 PE 2 SV 2
blastp_uniprot_sprot sp|Q9S9K4|ASPL2_ARATH 16 393 + 378 Gaps:45 81.05 475 29.35 2e-36 Aspartic proteinase-like protein 2 OS Arabidopsis thaliana GN At1g65240 PE 1 SV 2
blastp_uniprot_sprot sp|Q9LX20|ASPL1_ARATH 40 385 + 346 Gaps:62 66.67 528 29.26 1e-22 Aspartic proteinase-like protein 1 OS Arabidopsis thaliana GN At5g10080 PE 1 SV 1
blastp_uniprot_sprot sp|Q766C2|NEP2_NEPGR 34 383 + 350 Gaps:54 78.08 438 27.78 9e-22 Aspartic proteinase nepenthesin-2 OS Nepenthes gracilis GN nep2 PE 1 SV 1
blastp_uniprot_sprot sp|Q766C3|NEP1_NEPGR 34 383 + 350 Gaps:70 78.26 437 28.65 9e-22 Aspartic proteinase nepenthesin-1 OS Nepenthes gracilis GN nep1 PE 1 SV 1
blastp_uniprot_sprot sp|Q9LS40|ASPG1_ARATH 34 383 + 350 Gaps:59 68.20 500 30.21 3e-16 Protein ASPARTIC PROTEASE IN GUARD CELL 1 OS Arabidopsis thaliana GN ASPG1 PE 1 SV 1
blastp_uniprot_sprot sp|Q3EBM5|ASPR1_ARATH 34 384 + 351 Gaps:53 80.98 447 27.35 6e-16 Probable aspartic protease At2g35615 OS Arabidopsis thaliana GN At2g35615 PE 3 SV 1
blastp_uniprot_sprot sp|Q9LHE3|ASPG2_ARATH 34 383 + 350 Gaps:52 72.77 470 27.49 1e-12 Protein ASPARTIC PROTEASE IN GUARD CELL 2 OS Arabidopsis thaliana GN ASPG2 PE 2 SV 1
blastp_uniprot_sprot sp|Q9LZL3|PCS1L_ARATH 54 384 + 331 Gaps:76 77.92 453 25.50 7e-12 Aspartic proteinase PCS1 OS Arabidopsis thaliana GN PCS1 PE 2 SV 1
rpsblast_cdd gnl|CDD|133142 34 383 + 350 Gaps:85 100.00 273 64.10 1e-108 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 36 383 + 348 Gaps:118 99.62 265 40.15 2e-47 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 36 383 + 348 Gaps:72 99.67 299 31.54 1e-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 36 274 + 239 Gaps:36 82.33 283 27.47 3e-32 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 34 292 + 259 Gaps:35 63.11 431 29.41 6e-19 PLN03146 PLN03146 aspartyl protease family protein Provisional.
rpsblast_cdd gnl|CDD|133137 38 167 + 130 Gaps:23 100.00 109 28.44 2e-17 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 34 384 + 351 Gaps:104 99.69 326 24.00 6e-13 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|200939 35 381 + 347 Gaps:79 100.00 316 24.68 1e-09 pfam00026 Asp Eukaryotic aspartyl protease. Aspartyl (acid) proteases include pepsins cathepsins and renins. Two-domain structure probably arising from ancestral duplication. This family does not include the retroviral nor retrotransposon proteases (pfam00077) which are much smaller and appear to be homologous to a single domain of the eukaryotic asp proteases.
rpsblast_cdd gnl|CDD|133156 44 377 + 334 Gaps:81 96.96 362 22.51 2e-07 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 11 384 + 374 Gaps:40 93.97 398 30.21 8e-54 KOG1339 KOG1339 KOG1339 Aspartyl protease [Posttranslational modification protein turnover chaperones].

12 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Phobius 1 3 3 SIGNAL_PEPTIDE_N_REGION none N-terminal region of a signal peptide. none
Phobius 21 394 374 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Phobius 16 20 5 SIGNAL_PEPTIDE_C_REGION none C-terminal region of a signal peptide. none
Gene3D 22 204 183 G3DSA:2.40.70.10 none none IPR021109
Gene3D 210 386 177 G3DSA:2.40.70.10 none none IPR021109
Phobius 1 20 20 SIGNAL_PEPTIDE none Signal peptide region none
Pfam 244 378 135 PF14541 none Xylanase inhibitor C-terminal none
Pfam 36 204 169 PF14543 none Xylanase inhibitor N-terminal none
SUPERFAMILY 28 386 359 SSF50630 none none IPR021109
Phobius 4 15 12 SIGNAL_PEPTIDE_H_REGION none Hydrophobic region of a signal peptide. none
PANTHER 20 386 367 PTHR13683:SF229 none none none
PANTHER 20 386 367 PTHR13683 none none IPR001461

1 Localization

Analysis Start End Length
SignalP_EUK 1 21 20

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 21   Secretory pathway 2 0.822 0.093 NON-PLANT 21