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RIP_LUFAC
ID   RIP_LUFAC               Reviewed;         241 AA.
AC   P84530;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 2.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Ribosome-inactivating protein luffaculin 1 {ECO:0000303|PubMed:17470286};
DE            EC=3.2.2.22;
DE   AltName: Full=rRNA N-glycosidase {ECO:0000303|PubMed:17470286};
OS   Luffa acutangula (Ridged gourd) (Cucumis acutangulus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Sicyoeae; Luffa.
OX   NCBI_TaxID=56866;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-10, X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS), AND
RP   GLYCOSYLATION AT ASN-77 AND ASN-84.
RC   TISSUE=Seed {ECO:0000269|PubMed:17470286};
RX   PubMed=17470286; DOI=10.1186/1472-6807-7-29;
RA   Hou X., Chen M., Chen L., Meehan E.J., Xie J., Huang M.;
RT   "X-ray sequence and crystal structure of luffaculin 1, a novel type 1
RT   ribosome-inactivating protein.";
RL   BMC Struct. Biol. 7:29-29(2007).
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; Evidence={ECO:0000305};
CC   -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC       RIP subfamily. {ECO:0000255}.
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DR   PDB; 2OQA; X-ray; 1.00 A; A/B=1-241.
DR   PDBsum; 2OQA; -.
DR   AlphaFoldDB; P84530; -.
DR   SMR; P84530; -.
DR   iPTMnet; P84530; -.
DR   EvolutionaryTrace; P84530; -.
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; 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; Direct protein sequencing; Glycoprotein; Hydrolase;
KW   Plant defense; Protein synthesis inhibitor; Toxin.
FT   CHAIN           1..241
FT                   /note="Ribosome-inactivating protein luffaculin 1"
FT                   /id="PRO_0000221417"
FT   ACT_SITE        159
FT                   /evidence="ECO:0000250|UniProtKB:P16094"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17470286"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17470286"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   HELIX           11..24
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   STRAND          27..31
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   STRAND          34..37
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   HELIX           43..46
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   STRAND          47..53
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   STRAND          59..65
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   TURN            66..68
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   STRAND          71..76
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   STRAND          79..82
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   HELIX           86..91
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   TURN            92..94
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   STRAND          99..103
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   HELIX           110..117
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   HELIX           121..123
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   HELIX           128..139
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   TURN            143..145
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   HELIX           146..156
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   HELIX           158..162
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   HELIX           164..172
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   HELIX           182..201
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   TURN            202..206
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   STRAND          207..215
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   STRAND          221..226
FT                   /evidence="ECO:0007829|PDB:2OQA"
FT   HELIX           230..233
FT                   /evidence="ECO:0007829|PDB:2OQA"
SQ   SEQUENCE   241 AA;  25891 MW;  233F2B6D72A95CF3 CRC64;
     DVSFSLSGSS STSYSKFIGA LRKALPSNGT VYNITLLLSS ASGASRYTLM KLSNYDGKAI
     TVAIDVTNVY IMGYLVNSTS YFFNESDAKL ASQYVFAGST IVTLPYSGNY EKLQTAAGKI
     REKIPLGFPA LDSAITTLFH YDSTAAAAAF LVIIQTTAES SRFKYIEGQI IMRISKNGVP
     SLATISLENE WSALSKQIQL AQTNNGTFKT PVVIMDAGGQ RVEIGNVGSK VVTKNIQLLL
     N
 
 
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