Protein : Qrob_P0283470.2 Q. robur
Protein Identifier  ? Qrob_P0283470.2 Organism . Name  Quercus robur
Score  0.0 Score Type  egn
Protein Description  (M=3) 3.4.23.1 - Pepsin A. Code Enzyme  EC:3.4.23.1
Gene Prediction Quality  validated Protein length 

Sequence

Length: 171  
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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.

14 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|vvi:100853521 19 164 + 146 Gaps:3 94.70 151 55.94 1e-48 aspartic proteinase-like protein 1-like
blastp_kegg lcl|pxb:103936704 4 160 + 157 Gaps:5 29.40 517 59.21 5e-48 aspartic proteinase-like protein 1
blastp_kegg lcl|mdm:103401048 4 160 + 157 Gaps:5 28.95 525 58.55 7e-48 aspartic proteinase-like protein 1
blastp_kegg lcl|mdm:103455953 15 160 + 146 Gaps:3 27.66 517 59.44 3e-46 aspartic proteinase-like protein 1
blastp_kegg lcl|mdm:103418284 15 160 + 146 Gaps:3 26.78 534 59.44 3e-46 aspartic proteinase-like protein 1
blastp_kegg lcl|pxb:103953443 4 160 + 157 Gaps:5 28.90 526 57.89 4e-46 aspartic proteinase-like protein 1
blastp_kegg lcl|pper:PRUPE_ppa004265mg 16 160 + 145 Gaps:4 27.17 519 59.57 9e-46 hypothetical protein
blastp_kegg lcl|pmum:103340391 1 160 + 160 Gaps:7 29.59 517 56.86 3e-45 aspartic proteinase-like protein 1
blastp_kegg lcl|tcc:TCM_000144 34 159 + 126 Gaps:4 23.51 519 63.11 4e-45 Eukaryotic aspartyl protease family protein putative isoform 1
blastp_kegg lcl|pxb:103942516 4 160 + 157 Gaps:5 28.20 539 57.24 4e-45 aspartic proteinase-like protein 1
blastp_uniprot_sprot sp|Q9LX20|ASPL1_ARATH 40 152 + 113 Gaps:9 21.59 528 39.47 1e-12 Aspartic proteinase-like protein 1 OS Arabidopsis thaliana GN At5g10080 PE 1 SV 1
rpsblast_cdd gnl|CDD|133138 114 149 + 36 Gaps:1 13.07 283 40.54 3e-07 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|133143 114 142 + 29 none 10.94 265 44.83 4e-07 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_kog gnl|CDD|36553 78 153 + 76 Gaps:3 18.34 398 35.62 1e-08 KOG1339 KOG1339 KOG1339 Aspartyl protease [Posttranslational modification protein turnover chaperones].

10 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
ProSitePatterns 129 140 12 PS00141 none Eukaryotic and viral aspartyl proteases active site. IPR001969
Pfam 114 150 37 PF00026 none Eukaryotic aspartyl protease IPR001461
Phobius 39 170 132 CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. none
PANTHER 20 149 130 PTHR13683 none none IPR001461
Phobius 20 38 19 TRANSMEMBRANE none Region of a membrane-bound protein predicted to be embedded in the membrane. none
PANTHER 20 149 130 PTHR13683:SF232 none none none
SUPERFAMILY 21 58 38 SSF50630 none none IPR021109
SUPERFAMILY 98 150 53 SSF50630 none none IPR021109
Gene3D 106 149 44 G3DSA:2.40.70.10 none none IPR021109
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

1 Localization

Analysis Start End Length
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 0.864 0.021 NON-PLANT 36