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_5062 |
| Peptide Name | GLE_CHLRE |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Chlamydomonas reinhardtii |
| Plant Source (Common Name) | Algae |
| Plant Family | Chlamydomonadaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | Cell wall; Cell wall biogenesis/degradation; Direct protein sequencing; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Signal; Zinc; Zymogen | Autolysin precursor (EC 3.4.24.38) (Gametolysin) (Gamete lytic enzyme),(GLE).Note=Stored in the periplasm of gametes until its release. Secreted concurrently |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | DFSSCKLSGWSAPATLTPEKVTSDMLRGASAPTNNLANYYGACSYEKTLFDWWDLSKYCTASEQQAWERAAEAYAQAIVAQDPNSATGKKLQGILQWRERMSLATRRFGAAAALLVAACVLCTAPAWAQNETTGTGMVKTKSAFRWIRPPNPDNFLVLGPVPVPCIGGVTPPPRPPRPPRPPPRAGSTISSLSRRNDTYDNYGLEHAGRGTLEYGDATDVMGDFNKAGKGLLCPNAPNMYRIGWAKPINEPARPPPFRRPPPAQTPYVHKVEYTELQILCPQTIDSVTGYPMDDPRCNVPPGVAPFQNATGAWGNLTAANFTTDPWIRGLVIPAQGTRDDNMIVVNVGAQQAVVDICRISENGKELSCDDGIDNDCDGLQDNEDPDCQQRTGRVLLATSAELPTPTFRLKSLKSILKGSQKEIYAGKPIDLRTIVYIMRATVAAGEEALTIRNEFELLNGDVLNVTLEEVDTPENPSRRRLLSIIREERRNIYILPPGVKCSWSGYADVTCTSATCSAYVRGYSDTNAMQVIMHEAMHSERVFGFKSNLLDWGPNFQSRSNTWTSPFLAYNNGLGGGVRLVVQSTSDTSTRDGAMKATGAQAYYFSYRIKNTTAGGYDSGLTLDFHKKVLVHAYNGIQ |
| Sequence Length | 638 |
| Validation | Experimental evidence at protein level |
| Average Molecular Weight (Da) | 69832.86 |
| Monoisotopic Molecular Weight (Da) | 69788.66 |
| Isoelectric Point (pI) | 7.53 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
|---|
| Uniprot | P31178 |
| NCBI | --NA-- |
| EMBL | M94265 |
| Link to Source Databases | SPdb95662 |
|---|
| Addtional Information | FUNCTION:Mediates digestion of the cell walls of the 2 mating type gametes during mating as a necessary prelude to cell fusion.This enzyme acts specifically on the framework proteins (inner wall) of the cell wall, cleaving several model peptides at specific sites.CATALYTIC ACTIVITY:Cleavage of the proline- and hydroxyproline- rich proteins of the Chlamydomonas cell wall; also cleaves azocasein, gelatin and Leu-Trp-Met-|-Arg-Phe-Ala.COFACTOR:Binds 1 zinc ion per subunit (By similarity).INDUCTION:By the signal of flagellar agglutination between gametes of the opposite mating type.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.PTM:Present in 2 forms: an inactive V-form in vegetative cells and an active and soluble G-form. The V-form enzyme may be converted to the G-form enzyme during gametic differentiation under nitrogen-starved conditions.SIMILARITY:Belongs to the peptidase M11 family. |
