| Analysis | rpsblast_cdd | Start | 39 |
| End | 424 | Strand | + |
| Length | 386 | Note | Gaps:18 |
| Hit Coverage | 96.20 | Hit Length | 237 |
| Hit Pident | 31.14 | E Val | 1e-24 |
| Hit Description | cd03873 Zinc_peptidase_like Zinc peptidases M18 M20 M28 and M42. Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This family corresponds to several clans in the MEROPS database including the MH clan which contains 4 families (M18 M20 M28 M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase peptidase V (PepV) a eukaryotic non-specific dipeptidase and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases and has co-catalytic zinc ions. However several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated with three amino acid ligands plus activated water one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carbxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metalloaminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some of M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacylpeptidase activity (i.e. hydrolysis of acylated N-terminal residues). | Hit Pcons | 9.65 |
| Name | Qrob_P0025130.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0025130.2 | Quercus robur | 87.0 | egn | (M=1) 3.5.1.16 - Acetylornithine deacetylase. | EC:3.5.1.16 | validated |
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