| Analysis | rpsblast_cdd | Start | 1 |
| End | 108 | Strand | + |
| Length | 108 | Note | Gaps:5 |
| Hit Coverage | 36.27 | Hit Length | 295 |
| Hit Pident | 33.64 | E Val | 1e-08 |
| Hit Description | cd07474 Peptidases_S8_subtilisin_Vpr-like Peptidase S8 family domain in Vpr-like proteins. The maturation of the peptide antibiotic (lantibiotic) subtilin in Bacillus subtilis ATCC 6633 includes posttranslational modifications of the propeptide and proteolytic cleavage of the leader peptide. Vpr was identified as one of the proteases along with WprA that are capable of processing subtilin. Asp Ser His triadPeptidases S8 or Subtilases are a serine endo- and exo-peptidase clan. They have 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. The stability of subtilases may be enhanced by calcium some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular some function at extreme temperatures and pH values. | Hit Pcons | 19.63 |
| Name | Qrob_P0023150.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0023150.2 | Quercus robur | 0.0 | egn | (M=44) 3.4.14.10 - Tripeptidyl-peptidase II. | EC:3.4.14.10 | validated |
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