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RIPA_LUFAE
ID   RIPA_LUFAE              Reviewed;         277 AA.
AC   Q00465;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Ribosome-inactivating protein luffin-alpha;
DE            EC=3.2.2.22;
DE   AltName: Full=rRNA N-glycosidase;
DE   Flags: Precursor;
OS   Luffa aegyptiaca (Sponge gourd) (Luffa cylindrica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Sicyoeae; Luffa.
OX   NCBI_TaxID=3670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seed;
RX   PubMed=1600156; DOI=10.1007/bf00047727;
RA   Kataoka J., Habuka N., Miyano M., Masuta C., Koiwai A.;
RT   "Nucleotide sequence of cDNA encoding alpha-luffin, a ribosome-inactivating
RT   protein from Luffa cylindrica.";
RL   Plant Mol. Biol. 18:1199-1202(1992).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of the N-glycosidic bond at one specific
CC         adenosine on the 28S rRNA.; EC=3.2.2.22;
CC   -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC       RIP subfamily. {ECO:0000305}.
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DR   EMBL; X62371; CAA44229.1; -; mRNA.
DR   PIR; S22494; S22494.
DR   PDB; 2OQA; X-ray; 1.40 A; A/B=21-261.
DR   PDBsum; 2OQA; -.
DR   AlphaFoldDB; Q00465; -.
DR   SMR; Q00465; -.
DR   EvolutionaryTrace; Q00465; -.
DR   GO; GO:0030598; F:rRNA N-glycosylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.420.10; -; 1.
DR   Gene3D; 4.10.470.10; -; 1.
DR   InterPro; IPR036041; Ribosome-inact_prot_sf.
DR   InterPro; IPR017989; Ribosome_inactivat_1/2.
DR   InterPro; IPR001574; Ribosome_inactivat_prot.
DR   InterPro; IPR017988; Ribosome_inactivat_prot_CS.
DR   InterPro; IPR016138; Ribosome_inactivat_prot_sub1.
DR   InterPro; IPR016139; Ribosome_inactivat_prot_sub2.
DR   PANTHER; PTHR33453; PTHR33453; 1.
DR   Pfam; PF00161; RIP; 1.
DR   PRINTS; PR00396; SHIGARICIN.
DR   SUPFAM; SSF56371; SSF56371; 1.
DR   PROSITE; PS00275; SHIGA_RICIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antiviral defense; Hydrolase; Plant defense;
KW   Protein synthesis inhibitor; Signal; Toxin.
FT   SIGNAL          1..19
FT   CHAIN           20..277
FT                   /note="Ribosome-inactivating protein luffin-alpha"
FT                   /id="PRO_0000030785"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   277 AA;  30212 MW;  EA17FC27998C25AC CRC64;
     MKRFTVLILA IFVAASTVEA DVRFSLSGSS STSYSKFIGD LRKALPSNGT VYNITLLLSS
     ASGASRYTLM TLSNYDGKAI TVAVDVTNVY IMGYLVNSTS YFFNESDAKL ASQYVFKGST
     IVTLPYSGNY EKLQTAAGKI REKIPLGFPA LDSAITTLFH YDSTAAAAAF LVIIQTTAEA
     SRFKYIEGQI IERISKNQVP SLATISLENE WSALSKQIQL AQTNNGTFKT PVVITDDKGQ
     RVEITNVTSK VVTKNIQLLL NYKQNVAAFD EDVSAKH
 
 
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