Blast Analysis : gnl|CDD|133138

Analysis	rpsblast_cdd	Start	6
End	348	Strand	+
Length	343	Note	Gaps:92
Hit Coverage	99.29	Hit Length	283
Hit Pident	24.56	E Val	9e-29
Hit Description	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).	Hit Pcons	17.79
Name	Qrob_P0283100.2

1 Protein

Protein Identifier	Organism . Name	Score	Score Type	Protein Description	Alias (in v1)	Code Enzyme	Gene Prediction Quality
Qrob_P0283100.2	Quercus robur	100.0	egn	(M=4) PTHR13683//PTHR13683:SF229 - ASPARTYL PROTEASES // SUBFAMILY NOT NAMED		EC:3.4.23.12	validated

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