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 04-NOV-2026, entry version 46. 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, AND GLYCOSYLATION AT RP 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}. 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 PDB; 2OQA; X-ray; 1.00 A; A/B=1-241. DR AlphaFoldDB; P84530; -. DR SMR; P84530; -. DR GlyCosmos; P84530; 5 sites, No reported glycans. DR iPTMnet; P84530; -. DR EvolutionaryTrace; P84530; -. DR GO; GO:0030598; F:rRNA N-glycosylase activity; IEA:UniProtKB-EC. DR GO; GO:0017148; P:negative regulation of translation; IEA:InterPro. DR Gene3D; 3.40.420.10; Ricin (A subunit), domain 1; 1. DR Gene3D; 4.10.470.10; Ricin (A Subunit), domain 2; 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; -; 1. DR PANTHER; PTHR33453:SF34; RIBOSOME-INACTIVATING PROTEIN; 1. DR Pfam; PF00161; RIP; 1. DR PRINTS; PR00396; SHIGARICIN. DR SUPFAM; SSF56371; Ribosome inactivating proteins (RIP); 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 //