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_5563
Peptide NameRNS2_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 DescriptionEndonuclease; Glycoprotein; Hydrolase; Nuclease; Secreted; Signal | Ribonuclease S-2 precursor (EC 3.1.27.1) (S2-RNase).Secreted, extracellular space.
Activity Against--NA--
IC50 value--NA--
SequenceFWRKQWYKHGSCASPALPNQKHYFETVIRMFLAEKQNVSRILSMATIEPEGKNRTLLEIQNAIRAGTNNMIPKLKCQKVNGMTELVEVTLCHDSNLTQFILFTVHGLWPSTKVGRDPEYCKTKRYRKIQRLEPQLEIIWPNVSDRKANRGMIYIFTMVFSLNVLILSSSAARYDYFQFTQQYQQAFCNSNPTPCKDPPDKNCPRPLPQASPYFCPIDDIQY
Sequence Length221
ValidationExperimental evidence at protein level
Average Molecular Weight (Da)25749.75
Monoisotopic Molecular Weight (Da)25732.99
Isoelectric Point (pI)9.26
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_5563


External links (Uniprot, PDB and Source Information Database)
UniprotQ40965
NCBI--NA--
EMBLD49527
Link to Source DatabasesSPdb243548
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:N-linked core structure at Asn-91, Asn-137, and Asn-153 contains xylose and at Asn-195 contains xylose and fucose.SIMILARITY:Belongs to the RNase T2 family.CAUTION:Gln-105 is present instead of the conserved Glu which is expected to act as an active site proton donor.