Detailed Peptide Information
This page shows detailed information of individual peptides present in PlantPepDB database. The page is majorly divided into 3 sections. The first sections contains primary information like peptide activity, source, sequence, etc. In the secondary information section user can access the tertiary structure as well as the physico-chemical properties by clicking the respective links. Further there is also link of the source database and research article from which the peptide data is retrieved. Download the information by clicking
| Primary Information |
|---|
| PPepDB ID | PPepDB_5735 |
| Peptide Name | PAPA4_CARPA |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Carica papaya |
| Plant Source (Common Name) | Papaya |
| Plant Family | Caricaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | 3D-structure; Direct protein sequencing; Hydrolase; Protease; Signal; Thiol protease; Zymogen | Papaya proteinase 4 precursor (EC 3.4.22.25) (Papaya proteinase IV),(PPIV) (Papaya peptidase B) (Glycyl endopeptidase). |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | GSLLNAIAHQPVSVVVESAGRDFQNYKGGIFEGSCGTKVDHAVTAVGYGKMAIICSFSKLLFVAICLFGHMSLSYCDFSIVGYSQDDLTSTERLIQLFNSNDEFKEKYVGSLPEDYTNQPYDEEFVNEDIVDLPESVDWRAKGAVTPVKHQGYCESCWAFSTVATVEGINKIKTGNLVELSEQELVDCDKQSYGCNRGYQSGGKGYILIKNSWGPGWGENGYIRIRRASGNSPGVCGVYRSSYYPIKNSTSLQYVAQNGIHLRAKYPYIAKQQTCRANQVGGPKVKTNGVGRVQSNNEWMLKHNKNYKNVDEKLYRFEIFKDNLKYIDERNKMINGYWLGLNEFSDLS |
| Sequence Length | 348 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 39023.9 |
| Monoisotopic Molecular Weight (Da) | 38999.18 |
| Isoelectric Point (pI) | 7.11 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
|---|
| Uniprot | P05994 |
| NCBI | --NA-- |
| EMBL | X78056 |
| Link to Source Databases | SPdb183865 |
|---|
| Addtional Information | FUNCTION:Thiol protease with a substrate specificity very different from the other thiol proteases.CATALYTIC ACTIVITY:Preferential cleavage: Gly-|-Xaa, in proteins and in small molecule substrates.ENZYME REGULATION:Not inhibited by cystatin.MISCELLANEOUS:Substitution of the conserved Gly residue by Glu- 155 could possibly explain the unusual specificity.SIMILARITY:Belongs to the peptidase C1 family. |
