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_5096 |
| Peptide Name | MEP1_SOYBN |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Glycine max |
| Plant Source (Common Name) | Soybean |
| Plant Family | Fabaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease; Protease; Signal; Zinc; Zymogen | Metalloendoproteinase 1 precursor (EC 3.4.24.-) (SMEP1). |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | DINTLKQIMTPRCGVPDIIINTNKTTSFGMISDYTFFKDMPRWQAGTTQLDLESVAVHEIGHLLGLGHSSDLRAIMYPSIPPRTRKVNLAQDDIDGIRKLKNHGDPYPFDGPGGILGHAFAPTDGRCHFDADEYWVASGDVTKSPVTSAFMTLRNHQELLVALATLYFLATSLPSVSAHGPYAWDGEATYKFTTYHPGQNTYAFSPEPRLDDTFKSAIARAFSKWTPVVNIAFQETTSYETANIKILFASYGINPYKGLSNVKNYFHHLGYIPNAPHFDDNFDDTLVSAIKTYQKNYNLNVTGKF |
| Sequence Length | 305 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 34044.33 |
| Monoisotopic Molecular Weight (Da) | 34022.94 |
| Isoelectric Point (pI) | 6.31 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
|---|
| Uniprot | P29136 |
| NCBI | --NA-- |
| EMBL | U63725 |
| Link to Source Databases | SPdb150842 |
|---|
| Addtional Information | FUNCTION:Specificity similar to that of mammalian matrix metalloproteases. May act against cell wall components.COFACTOR:Binds 1 zinc ion per subunit (By similarity).DOMAIN:The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme.The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.SIMILARITY:Belongs to the peptidase M10A family. |
