PPepDB-ID	"Peptide Name"	PMID	"Plant source"	"Plant Family"	"Peptide Family"	"Peptide function"	"Peptide function description"	"Activity against"	Sequence	"Sequence Length"	Validation	"Avg. Molecular wt(Da)"	"Monoisotopic molecular wt(Da)"	pI	Method	"Additional information"
PPepDB_5242	RIP3_MOMCH	--NA--	"Momordica charantia"	Cucurbitaceae	--NA--	Signaling-peptide	"3D-structure; Antiviral protein; Direct protein sequencing; Glycoprotein; Hydrolase; Plant defense; Protein synthesis inhibitor; Signal; Toxin | Ribosome-inactivating protein beta-momorcharin precursor (EC 3.2.2.22),(rRNA N-glycosidase) (MAP 30) (B-MMC)."	--NA--	DVSYFFKESPPEAYNILFKGTRKITLPYTGNYENLQTAAHKIRENIDLGLKPNLAIISLENQWSALSKQIFLAQNQGGKFRNPVDLIKPTGERFQVTNVDMVKCLLLSFLIIAIFIGVPTAKGDVNFDLSTATAKTYTKFIEDFRATLPFPALSSAITTLFYYNAQSAPSALLVLIQTTAEAARFKYIERHVAKYVATNFSDVVKGNIKLLLNSRASTADENFITTMTLLGESVVNSHKVYDIPLLYSTISDSRRFILLNLTSYAYETISVAIDVTNVYVVAYRTR	286	"Experimental evidence at protein level"	32030.88	32010.95	9.08	--NA--	"FUNCTION:Irreversibly relaxes supercoiled DNA and catalyzes double-stranded breakage. Acts also as a ribosome inactivating protein.CATALYTIC ACTIVITY:Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.PTM:Bound to a branched hexasaccharide.MISCELLANEOUS:Possesses anti-HIV and antitumoral activities.Inhibits HIV-1 integrase.MISCELLANEOUS:Manganese or zinc required for enhancing substrate binding rather than catalysis.MISCELLANEOUS:The oligosaccharide does not influence the fold of the polypeptide chain and probably does not play a role in the enzymatic function.MISCELLANEOUS:Is not toxic to uninfected normal cells as it cannot enter into them.SIMILARITY:Belongs to the ribosome-inactivating protein family.Type 1 RIP subfamily."
