Blast Analysis : gnl|CDD|133143

Analysis  rpsblast_cdd Start  80
End  421 Strand  +
Length  342 Note  Gaps:122
Hit Coverage  99.62 Hit Length  265
Hit Pident  38.26 E Val  2e-43
Hit Description  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. Hit Pcons  13.26
Name  Qrob_P0283050.2

1 Protein

Protein Identifier
Organism . Name
Score Score Type Protein Description Alias (in v1) Code Enzyme Gene Prediction Quality
Qrob_P0283050.2 Quercus robur 100.0 egn (M=4) PTHR13683//PTHR13683:SF229 - ASPARTYL PROTEASES // SUBFAMILY NOT NAMED   EC:3.4.23.12 validated