| Analysis | rpsblast_cdd | Start | 422 |
| End | 531 | Strand | + |
| Length | 110 | Note | Gaps:2 |
| Hit Coverage | 51.18 | Hit Length | 211 |
| Hit Pident | 52.78 | E Val | 7e-42 |
| Hit Description | cd07560 Peptidase_S41_CPP C-terminal processing peptidase serine protease family S41. The C-terminal processing peptidase (CPP EC 3.4.21.102) also known as tail-specific protease (tsp) the photosystem II D1 C-terminal processing protease (D1P) and other related S41 protease family members are present in this CD. CPP is synthesized as a precursor form with a carboxyl-terminal extension. It specifically recognizes a C-terminal tripeptide Xaa-Yaa-Zaa in which Xaa is preferably Ala or Leu Yaa is preferably Ala or Tyr and Zaa is preferably Ala but then cleaves at a variable distance from the C-terminus. The C-terminal carboxylate group is essential and proteins where this group is amidated are not substrates. This family of proteases contains the PDZ domain that promotes protein-protein interactions and is important for substrate recognition. The active site consists of a serine/lysine catalytic dyad. The bacterial CCP-1 is believed to be important for the degradation of incorrectly synthesized proteins as well as protection from thermal and osmotic stresses. In E. coli it is involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). In the plant chloroplast the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II allowing the light-driven assembly of the tetranuclear manganese cluster which is responsible for photosynthetic water oxidation. | Hit Pcons | 12.04 |
| Name | Qrob_P0379730.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0379730.2 | Quercus robur | 100.0 | egn | (M=1) PF03572//PF13180 - Peptidase family S41 // PDZ domain | EC:3.4.21.102 | validated |
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