Protein : Qrob_P0283370.2 Q. robur
Protein Identifier  ? Qrob_P0283370.2 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: 163  
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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.

16 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|vvi:100853521 13 148 + 136 Gaps:1 90.73 151 61.31 1e-51 aspartic proteinase-like protein 1-like
blastp_kegg lcl|pper:PRUPE_ppa004265mg 15 148 + 134 none 25.82 519 61.94 8e-51 hypothetical protein
blastp_kegg lcl|pmum:103340391 12 161 + 150 Gaps:5 28.05 517 60.00 1e-49 aspartic proteinase-like protein 1
blastp_kegg lcl|pmum:103340367 15 161 + 147 Gaps:5 28.40 500 60.56 2e-49 aspartic proteinase-like protein 1
blastp_kegg lcl|mdm:103401048 6 161 + 156 Gaps:6 28.95 525 57.89 5e-49 aspartic proteinase-like protein 1
blastp_kegg lcl|pxb:103936704 6 148 + 143 Gaps:1 27.85 517 59.03 2e-48 aspartic proteinase-like protein 1
blastp_kegg lcl|mdm:103455953 12 161 + 150 Gaps:6 28.24 517 60.27 3e-48 aspartic proteinase-like protein 1
blastp_kegg lcl|mdm:103418284 12 161 + 150 Gaps:6 27.34 534 60.27 5e-48 aspartic proteinase-like protein 1
blastp_kegg lcl|pxb:103953443 6 148 + 143 Gaps:1 27.38 526 56.94 3e-47 aspartic proteinase-like protein 1
blastp_kegg lcl|pxb:103942516 6 148 + 143 Gaps:1 26.72 539 56.25 6e-47 aspartic proteinase-like protein 1
blastp_uniprot_sprot sp|Q9LX20|ASPL1_ARATH 40 142 + 103 Gaps:7 20.08 528 39.62 1e-15 Aspartic proteinase-like protein 1 OS Arabidopsis thaliana GN At5g10080 PE 1 SV 1
blastp_uniprot_sprot sp|D4B385|CARP_ARTBC 89 142 + 54 Gaps:1 13.75 400 43.64 1e-07 Probable vacuolar protease A OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) GN PEP2 PE 3 SV 1
blastp_uniprot_sprot sp|D4DEN7|CARP_TRIVH 89 142 + 54 Gaps:1 13.75 400 43.64 2e-07 Probable vacuolar protease A OS Trichophyton verrucosum (strain HKI 0517) GN PEP2 PE 3 SV 1
blastp_uniprot_sprot sp|C5FS55|CARP_ARTOC 89 142 + 54 Gaps:1 13.92 395 43.64 3e-07 Vacuolar protease A OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) GN PEP2 PE 3 SV 1
rpsblast_cdd gnl|CDD|133138 112 158 + 47 Gaps:1 16.96 283 39.58 2e-08 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_kog gnl|CDD|36553 83 158 + 76 Gaps:1 18.84 398 32.00 2e-08 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 18 29 12 SIGNAL_PEPTIDE_H_REGION none Hydrophobic region of a signal peptide. none
ProSitePatterns 127 138 12 PS00141 none Eukaryotic and viral aspartyl proteases active site. IPR001969
Pfam 112 156 45 PF00026 none Eukaryotic aspartyl protease IPR001461
SUPERFAMILY 20 58 39 SSF50630 none none IPR021109
SUPERFAMILY 96 152 57 SSF50630 none none IPR021109
Gene3D 109 154 46 G3DSA:2.40.70.10 none none IPR021109
Phobius 37 162 126 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Phobius 1 36 36 SIGNAL_PEPTIDE none Signal peptide region none
PANTHER 20 144 125 PTHR13683:SF232 none none none
PANTHER 20 144 125 PTHR13683 none none IPR001461
Phobius 1 17 17 SIGNAL_PEPTIDE_N_REGION none N-terminal region of a signal peptide. none
Phobius 30 36 7 SIGNAL_PEPTIDE_C_REGION none C-terminal region of a signal peptide. none

2 Localization

Analysis Start End Length
SignalP_EUK 1 36 35
TMHMM 7 29 22

0 Qtllist

0 Targeting