Protein : Qrob_P0215160.2 Q. robur
Protein Identifier  ? Qrob_P0215160.2 Organism . Name  Quercus robur
Score  85.0 Score Type  egn
Protein Description  (M=3) PTHR13683//PTHR13683:SF257 - ASPARTYL PROTEASES // SUBFAMILY NOT NAMED Code Enzyme  EC:3.4.23.12
Gene Prediction Quality  validated Protein length 

Sequence

Length: 503  
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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.

34 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pop:POPTR_0002s09270g 32 502 + 471 Gaps:46 80.41 536 67.75 0.0 POPTRDRAFT_710172 hypothetical protein
blastp_kegg lcl|pxb:103938883 36 502 + 467 Gaps:46 80.34 529 67.29 0.0 aspartic proteinase-like protein 1
blastp_kegg lcl|mdm:103407114 36 502 + 467 Gaps:46 91.40 465 66.82 0.0 aspartic proteinase-like protein 1
blastp_kegg lcl|mdm:103402262 36 502 + 467 Gaps:46 91.40 465 66.82 0.0 aspartic proteinase-like protein 1
blastp_kegg lcl|tcc:TCM_034973 1 502 + 502 Gaps:54 86.15 527 66.96 0.0 Eukaryotic aspartyl protease family protein isoform 1
blastp_kegg lcl|pper:PRUPE_ppa004428mg 1 502 + 502 Gaps:72 85.10 510 67.28 0.0 hypothetical protein
blastp_kegg lcl|rcu:RCOM_1033780 1 502 + 502 Gaps:54 84.86 535 65.42 0.0 Aspartic proteinase nepenthesin-2 precursor putative
blastp_kegg lcl|cit:102621755 1 502 + 502 Gaps:52 85.50 538 62.83 0.0 aspartic proteinase-like protein 1-like
blastp_kegg lcl|vvi:100253991 1 502 + 502 Gaps:52 85.50 531 62.33 0.0 aspartic proteinase-like protein 1-like
blastp_kegg lcl|gmx:100819355 32 502 + 471 Gaps:50 81.63 528 63.57 0.0 aspartic proteinase-like protein 1-like
blastp_pdb 3utl_A 246 495 + 250 Gaps:47 74.54 326 29.22 3e-06 mol:protein length:326 Pepsin A
blastp_pdb 1qrp_E 246 495 + 250 Gaps:47 74.54 326 29.22 3e-06 mol:protein length:326 PEPSIN 3A
blastp_pdb 1pso_E 246 495 + 250 Gaps:47 74.54 326 29.22 3e-06 mol:protein length:326 PEPSIN 3A
blastp_pdb 1psn_A 246 495 + 250 Gaps:47 74.54 326 29.22 3e-06 mol:protein length:326 PEPSIN 3A
blastp_pdb 1flh_A 246 495 + 250 Gaps:47 74.54 326 28.81 7e-06 mol:protein length:326 UROPEPSIN
blastp_uniprot_sprot sp|Q9LX20|ASPL1_ARATH 1 502 + 502 Gaps:58 85.98 528 51.54 3e-150 Aspartic proteinase-like protein 1 OS Arabidopsis thaliana GN At5g10080 PE 1 SV 1
blastp_uniprot_sprot sp|Q9S9K4|ASPL2_ARATH 80 501 + 422 Gaps:73 79.79 475 30.61 7e-24 Aspartic proteinase-like protein 2 OS Arabidopsis thaliana GN At1g65240 PE 1 SV 2
blastp_uniprot_sprot sp|Q766C3|NEP1_NEPGR 70 501 + 432 Gaps:93 87.19 437 25.98 8e-13 Aspartic proteinase nepenthesin-1 OS Nepenthes gracilis GN nep1 PE 1 SV 1
blastp_uniprot_sprot sp|Q766C2|NEP2_NEPGR 70 501 + 432 Gaps:93 86.99 438 24.93 1e-12 Aspartic proteinase nepenthesin-2 OS Nepenthes gracilis GN nep2 PE 1 SV 1
blastp_uniprot_sprot sp|Q9LS40|ASPG1_ARATH 79 501 + 423 Gaps:97 76.40 500 28.27 3e-12 Protein ASPARTIC PROTEASE IN GUARD CELL 1 OS Arabidopsis thaliana GN ASPG1 PE 1 SV 1
blastp_uniprot_sprot sp|Q0IU52|ASP1_ORYSJ 113 501 + 389 Gaps:89 87.32 410 24.02 6e-10 Aspartic proteinase Asp1 OS Oryza sativa subsp. japonica GN ASP1 PE 2 SV 1
blastp_uniprot_sprot sp|Q6XBF8|CDR1_ARATH 116 486 + 371 Gaps:85 75.51 437 28.18 3e-09 Aspartic proteinase CDR1 OS Arabidopsis thaliana GN CDR1 PE 1 SV 1
blastp_uniprot_sprot sp|A2ZC67|ASP1_ORYSI 113 501 + 389 Gaps:89 87.32 410 24.30 6e-09 Aspartic proteinase Asp1 OS Oryza sativa subsp. indica GN ASP1 PE 2 SV 2
blastp_uniprot_sprot sp|Q9LZL3|PCS1L_ARATH 200 501 + 302 Gaps:59 73.51 453 23.42 2e-08 Aspartic proteinase PCS1 OS Arabidopsis thaliana GN PCS1 PE 2 SV 1
rpsblast_cdd gnl|CDD|133143 234 501 + 268 Gaps:69 88.68 265 29.79 2e-28 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 116 498 + 383 Gaps:138 98.59 283 31.18 5e-25 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 234 501 + 268 Gaps:30 88.96 299 30.45 3e-21 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|133160 112 501 + 390 Gaps:128 98.77 326 26.40 3e-19 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 225 501 + 277 Gaps:65 87.18 273 32.35 4e-19 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|178691 116 486 + 371 Gaps:96 76.33 431 28.88 1e-15 PLN03146 PLN03146 aspartyl protease family protein Provisional.

22 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Phobius 30 502 473 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Pfam 373 497 125 PF14541 none Xylanase inhibitor C-terminal none
Phobius 5 20 16 SIGNAL_PEPTIDE_H_REGION none Hydrophobic region of a signal peptide. none
PANTHER 67 145 79 PTHR13683 none none IPR001461
PANTHER 6 46 41 PTHR13683 none none IPR001461
PANTHER 196 502 307 PTHR13683 none none IPR001461
SUPERFAMILY 198 501 304 SSF50630 none none IPR021109
PANTHER 67 145 79 PTHR13683:SF257 none none none
PANTHER 6 46 41 PTHR13683:SF257 none none none
Phobius 1 29 29 SIGNAL_PEPTIDE none Signal peptide region none
SUPERFAMILY 108 173 66 SSF50630 none none IPR021109
PANTHER 196 502 307 PTHR13683:SF257 none none none
Phobius 21 29 9 SIGNAL_PEPTIDE_C_REGION none C-terminal region of a signal peptide. none
Gene3D 109 142 34 G3DSA:2.40.70.10 none none IPR021109
Gene3D 208 335 128 G3DSA:2.40.70.10 none none IPR021109
Gene3D 342 502 161 G3DSA:2.40.70.10 none none IPR021109
Pfam 115 335 221 PF14543 none Xylanase inhibitor N-terminal none
PRINTS 473 488 16 PR00792 none Pepsin (A1) aspartic protease family signature IPR001461
PRINTS 118 138 21 PR00792 none Pepsin (A1) aspartic protease family signature IPR001461
PRINTS 377 388 12 PR00792 none Pepsin (A1) aspartic protease family signature IPR001461
ProSitePatterns 377 388 12 PS00141 none Eukaryotic and viral aspartyl proteases active site. IPR001969
Phobius 1 4 4 SIGNAL_PEPTIDE_N_REGION none N-terminal region of a signal peptide. none

1 Localization

Analysis Start End Length
TMHMM 7 29 22

1 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran2_2015_nEpis_3P Qrob_Chr12 12 s_1AOES6_1466 s_1B0DDG_1094 28,97 28,55 30,1 lod 3.6 8.4

1 Targeting

Analysis Start End Length Location Reliability Signal Peptide Cut Off Mitochondrion Cut Off Network Signal Peptide Length
TargetP 1 26   Secretory pathway 2 0.876 0.098 NON-PLANT 26