Protein : Qrob_P0283490.2 Q. robur
Protein Identifier  ? Qrob_P0283490.2 Organism . Name  Quercus robur
Score  100.0 Score Type  egn
Protein Description  (M=17) PTHR13683:SF232 - ASPARTYL PROTEASE FAMILY PROTEIN (PTHR13683:SF232) Code Enzyme  EC:3.4.23.12
Gene Prediction Quality  validated Protein length 

Sequence

Length: 525  
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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.

32 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pxb:103936704 4 524 + 521 Gaps:16 99.61 517 56.50 0.0 aspartic proteinase-like protein 1
blastp_kegg lcl|pmum:103340391 3 524 + 522 Gaps:21 100.00 517 55.90 0.0 aspartic proteinase-like protein 1
blastp_kegg lcl|tcc:TCM_000144 34 524 + 491 Gaps:35 95.57 519 57.26 0.0 Eukaryotic aspartyl protease family protein putative isoform 1
blastp_kegg lcl|rcu:RCOM_0310740 35 524 + 490 Gaps:28 93.43 533 55.22 0.0 Aspartic proteinase nepenthesin-1 precursor putative
blastp_kegg lcl|pper:PRUPE_ppa004265mg 16 524 + 509 Gaps:18 97.30 519 56.04 0.0 hypothetical protein
blastp_kegg lcl|mdm:103401048 4 524 + 521 Gaps:28 99.62 525 56.60 0.0 aspartic proteinase-like protein 1
blastp_kegg lcl|mdm:103455953 3 524 + 522 Gaps:15 100.00 517 55.90 0.0 aspartic proteinase-like protein 1
blastp_kegg lcl|pxb:103953443 4 523 + 520 Gaps:28 99.62 526 55.73 0.0 aspartic proteinase-like protein 1
blastp_kegg lcl|fve:101313637 22 524 + 503 Gaps:22 95.58 520 54.73 0.0 aspartic proteinase-like protein 1-like
blastp_kegg lcl|sot:102602891 21 522 + 502 Gaps:25 95.92 539 53.00 0.0 aspartic proteinase-like protein 1-like
blastp_pdb 3hd8_C 255 455 + 201 Gaps:32 59.38 389 22.51 1e-08 mol:protein length:389 Xylanase inhibitor
blastp_pdb 3hd8_A 255 455 + 201 Gaps:32 59.38 389 22.51 1e-08 mol:protein length:389 Xylanase inhibitor
blastp_uniprot_sprot sp|Q9LX20|ASPL1_ARATH 14 494 + 481 Gaps:49 89.39 528 38.56 2e-79 Aspartic proteinase-like protein 1 OS Arabidopsis thaliana GN At5g10080 PE 1 SV 1
blastp_uniprot_sprot sp|Q9S9K4|ASPL2_ARATH 40 460 + 421 Gaps:61 84.63 475 28.11 3e-24 Aspartic proteinase-like protein 2 OS Arabidopsis thaliana GN At1g65240 PE 1 SV 2
blastp_uniprot_sprot sp|Q766C2|NEP2_NEPGR 76 460 + 385 Gaps:71 85.39 438 26.47 3e-16 Aspartic proteinase nepenthesin-2 OS Nepenthes gracilis GN nep2 PE 1 SV 1
blastp_uniprot_sprot sp|Q6XBF8|CDR1_ARATH 74 460 + 387 Gaps:79 86.04 437 28.46 9e-16 Aspartic proteinase CDR1 OS Arabidopsis thaliana GN CDR1 PE 1 SV 1
blastp_uniprot_sprot sp|Q766C3|NEP1_NEPGR 114 460 + 347 Gaps:61 77.80 437 27.06 2e-13 Aspartic proteinase nepenthesin-1 OS Nepenthes gracilis GN nep1 PE 1 SV 1
blastp_uniprot_sprot sp|Q0IU52|ASP1_ORYSJ 114 460 + 347 Gaps:60 87.56 410 25.07 5e-11 Aspartic proteinase Asp1 OS Oryza sativa subsp. japonica GN ASP1 PE 2 SV 1
blastp_uniprot_sprot sp|Q9LS40|ASPG1_ARATH 114 460 + 347 Gaps:46 67.80 500 26.55 4e-10 Protein ASPARTIC PROTEASE IN GUARD CELL 1 OS Arabidopsis thaliana GN ASPG1 PE 1 SV 1
blastp_uniprot_sprot sp|A2ZC67|ASP1_ORYSI 114 460 + 347 Gaps:56 87.56 410 24.51 4e-10 Aspartic proteinase Asp1 OS Oryza sativa subsp. indica GN ASP1 PE 2 SV 2
blastp_uniprot_sprot sp|Q9LHE3|ASPG2_ARATH 114 460 + 347 Gaps:63 72.34 470 25.88 6e-10 Protein ASPARTIC PROTEASE IN GUARD CELL 2 OS Arabidopsis thaliana GN ASPG2 PE 2 SV 1
blastp_uniprot_sprot sp|P18242|CATD_MOUSE 108 455 + 348 Gaps:86 80.98 410 27.41 2e-08 Cathepsin D OS Mus musculus GN Ctsd PE 1 SV 1
rpsblast_cdd gnl|CDD|133143 114 460 + 347 Gaps:125 99.62 265 29.17 8e-27 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 114 457 + 344 Gaps:101 100.00 283 29.68 2e-23 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|133142 113 460 + 348 Gaps:102 99.63 273 33.09 1e-22 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|133139 114 460 + 347 Gaps:81 99.67 299 32.55 3e-20 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 74 460 + 387 Gaps:75 87.24 431 28.99 2e-18 PLN03146 PLN03146 aspartyl protease family protein Provisional.
rpsblast_cdd gnl|CDD|133160 114 460 + 347 Gaps:75 98.77 326 24.22 5e-18 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 114 454 + 341 Gaps:78 98.42 316 29.26 1e-14 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|133161 114 351 + 238 Gaps:50 77.70 278 27.78 3e-09 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).

17 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Pfam 317 456 140 PF14541 none Xylanase inhibitor C-terminal none
Pfam 114 295 182 PF14543 none Xylanase inhibitor N-terminal none
Phobius 43 505 463 CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. none
Gene3D 111 286 176 G3DSA:2.40.70.10 none none IPR021109
Gene3D 287 468 182 G3DSA:2.40.70.10 none none IPR021109
Phobius 524 524 1 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
PRINTS 432 447 16 PR00792 none Pepsin (A1) aspartic protease family signature IPR001461
PRINTS 120 140 21 PR00792 none Pepsin (A1) aspartic protease family signature IPR001461
PRINTS 336 347 12 PR00792 none Pepsin (A1) aspartic protease family signature IPR001461
PANTHER 20 476 457 PTHR13683 none none IPR001461
SUPERFAMILY 107 462 356 SSF50630 none none IPR021109
Phobius 506 523 18 TRANSMEMBRANE none Region of a membrane-bound protein predicted to be embedded in the membrane. none
PANTHER 20 476 457 PTHR13683:SF232 none none none
ProSitePatterns 336 347 12 PS00141 none Eukaryotic and viral aspartyl proteases active site. IPR001969
Phobius 1 19 19 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
ProSitePatterns 129 140 12 PS00141 none Eukaryotic and viral aspartyl proteases active site. IPR001969
Phobius 20 42 23 TRANSMEMBRANE none Region of a membrane-bound protein predicted to be embedded in the membrane. none

2 Localization

Analysis Start End Length
SignalP_EUK 1 36 35
TMHMM 20 42 22

0 Qtllist

1 Targeting

Analysis Start End Length Location Reliability Signal Peptide Cut Off Mitochondrion Cut Off Network Signal Peptide Length
TargetP 1 36   Secretory pathway 2 0.885 0.019 NON-PLANT 36