| Analysis | rpsblast_cdd | Start | 130 |
| End | 317 | Strand | + |
| Length | 188 | Note | Gaps:32 |
| Hit Coverage | 65.56 | Hit Length | 241 |
| Hit Pident | 29.11 | E Val | 7e-18 |
| Hit Description | cd00306 Peptidases_S8_S53 Peptidase domain in the S8 and S53 families. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile aspartate as an electrophile and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family while glutamic acid has the same role here as the histidine base. However the aspartic acid residue that acts as an electrophile is quite different. In S53 it follows glutamic acid while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds some are intracellular while others are extracellular some function at extreme temperatures and others at high or low pH values. | Hit Pcons | 12.03 |
| Name | Qrob_P0036570.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0036570.2 | Quercus robur | 0.0 | egn | (M=44) 3.4.14.10 - Tripeptidyl-peptidase II. | EC:3.4.14.10 | validated |
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