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 IDPPepDB_5149
Peptide NameRNS6_PYRPY
PMID(s)--NA--
Plant Source (Scientific Name)Pyrus pyrifolia, Pyrus serotina
Plant Source (Common Name)Japanese pear
Plant FamilyRosaceae
Peptide Family--NA--
Peptide FunctionSignaling-peptide
Peptide Function DescriptionDirect protein sequencing; Endonuclease; Glycoprotein; Hydrolase; Nuclease; Signal | Ribonuclease S-6 precursor (EC 3.1.27.1) (S6-RNase).
Activity Against--NA--
IC50 value--NA--
SequenceDPPDKLFTVHGLWPSNDVGDDPIYCKNKTIKSQQIGNLTAQLIIIWPNVLDRNLTQFIDCPRSSFKGSPFHCPTNHILYDRTDHVGFWNRQWNKHGSCGKAPTIKDEMHYFKTVIKMYITQKQNVSEILMGITGMIYMVPMVFSLIVLISCSSTMGYNYFQFTQQYQPAVCNSNPTPCKSRAKIEPEGKIRRRDDIINAIRLGTKDKKPKLKCQKNNQTTELVEITICS
Sequence Length229
ValidationExperimental evidence at protein level
Average Molecular Weight (Da)26278.43
Monoisotopic Molecular Weight (Da)26261.26
Isoelectric Point (pI)9.17
Method / Extraction--NA--


Secondary Information
Tertiary Structure and DSSP ReportClick to View Structure
Physico-Chemical Properties of peptidesClick to View Physico-Chemical Details of PPepDB_5149


External links (Uniprot, PDB and Source Information Database)
UniprotO80324
NCBI--NA--
EMBLAB002142
Link to Source DatabasesSPdb243558
Addtional InformationFUNCTION:Self-incompatibility (SI) is the inherited ability of a flowering plant to prevent self-fertilization by discriminating between self and non-self pollen during pollination. In many species, self-incompatibility is controlled by the single, multiallelic locus S.CATALYTIC ACTIVITY:Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.PTM:The N-glycans attached at Asn-188 and Asn-203 consist of either monosaccharide (GlcNAc) or disaccharide (GlcNAc-GlcNAc) that could not be distinguished.SIMILARITY:Belongs to the RNase T2 family.CAUTION:Gln-112 is present instead of the conserved Glu which is expected to act as an active site proton donor.