ID   RIP_DRIMA               Reviewed;         257 AA.
AC   P84786;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Ribosome-inactivating protein charybdin;
DE            EC=3.2.2.22;
DE   AltName: Full=rRNA N-glycosidase;
OS   Drimia maritima (Sea squill) (Charybdis maritima).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Hyacinthaceae;
OC   Urgineoideae; Squilla.
OX   NCBI_TaxID=82070;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-14 AND 242-257, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF
RP   4-252, X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), FUNCTION, AND CATALYTIC
RP   ACTIVITY.
RC   TISSUE=Bulb {ECO:0000269|PubMed:16817896};
RX   PubMed=16817896; DOI=10.1111/j.1742-4658.2006.05287.x;
RA   Touloupakis E., Gessmann R., Kavelaki K., Christofakis E., Petratos K.,
RA   Ghanotakis D.F.;
RT   "Isolation, characterization, sequencing and crystal structure of
RT   charybdin, a type 1 ribosome-inactivating protein from Charybdis maritima
RT   agg.";
RL   FEBS J. 273:2684-2692(2006).
CC   -!- FUNCTION: Inhibits translation in rabbit reticulocytes.
CC       {ECO:0000269|PubMed:16817896}.
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         Evidence={ECO:0000269|PubMed:16817896};
CC   -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC       RIP subfamily. {ECO:0000269|PubMed:16817896}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ323742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PDB; 2B7U; X-ray; 1.60 A; A=1-257.
DR   PDBsum; 2B7U; -.
DR   AlphaFoldDB; P84786; -.
DR   SMR; P84786; -.
DR   EvolutionaryTrace; P84786; -.
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:0006952; P:defense response; 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; 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.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Plant defense; Protein synthesis inhibitor; Toxin.
FT   CHAIN           1..257
FT                   /note="Ribosome-inactivating protein charybdin"
FT                   /id="PRO_0000248258"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000269|PubMed:16817896"
FT   SITE            79
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000269|PubMed:16817896"
FT   SITE            117
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000269|PubMed:16817896"
FT   SITE            170
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000269|PubMed:16817896"
FT   DISULFID        217..254
FT                   /evidence="ECO:0000269|PubMed:16817896"
FT   STRAND          7..16
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   HELIX           21..35
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   STRAND          37..40
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   STRAND          43..45
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   STRAND          56..64
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   STRAND          67..74
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   TURN            75..77
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   STRAND          80..84
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   STRAND          86..88
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   STRAND          91..93
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   HELIX           117..124
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   HELIX           128..130
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   HELIX           135..147
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   HELIX           151..164
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   HELIX           166..170
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   HELIX           172..180
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   TURN            181..183
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   HELIX           192..196
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   HELIX           199..201
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   HELIX           202..214
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   STRAND          223..225
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   STRAND          228..230
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   HELIX           233..237
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   STRAND          240..243
FT                   /evidence="ECO:0007829|PDB:2B7U"
FT   HELIX           247..250
FT                   /evidence="ECO:0007829|PDB:2B7U"
SQ   SEQUENCE   257 AA;  29252 MW;  12EB2E35328175AE CRC64;
     SQCKAMTVKF TVELDIERLT GQTYTDFIKN LRRSLATWYL HGVPVLPLYN QEADPRGFDL
     KLTFRGQVTT VRIHRDDLVL RGYQMQGAGK WLELERPSTQ TGHLIEGSEL LEFGPSYEEL
     AAAAQQDILD ISYNKNALQD AVSKLAVSTN TRDRARSLIV VSQMFCEATR FVDIANHFAF
     NLESSEPVKL PQWMQNDLEK NWVRFSFMIL KSNADPCYKF EPQTIYGKII KTADELLNFL
     GIVEQHPDTR SPPCAAG