RIPB_LUFAE
ID RIPB_LUFAE Reviewed; 250 AA.
AC P22851;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Ribosome-inactivating protein luffin-B;
DE EC=3.2.2.22;
DE AltName: Full=rRNA N-glycosidase;
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 PROTEIN SEQUENCE.
RC TISSUE=Seed;
RX PubMed=1368666; DOI=10.1271/bbb1961.55.229;
RA Islam M.R., Hirayama H., Funatsu G.;
RT "Complete amino acid sequence of luffin-b, a ribosome-inactivating protein
RT from sponge gourd (Luffa cylindrica) seeds.";
RL Agric. Biol. Chem. 55:229-238(1991).
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 PIR; JN0108; JN0108.
DR PDB; 1NIO; X-ray; 2.00 A; A=1-250.
DR PDBsum; 1NIO; -.
DR AlphaFoldDB; P22851; -.
DR SMR; P22851; -.
DR EvolutionaryTrace; P22851; -.
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; Direct protein sequencing; Hydrolase;
KW Plant defense; Protein synthesis inhibitor; Toxin.
FT CHAIN 1..250
FT /note="Ribosome-inactivating protein luffin-B"
FT /id="PRO_0000221416"
FT ACT_SITE 160
FT /evidence="ECO:0000250"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1NIO"
FT HELIX 12..25
FT /evidence="ECO:0007829|PDB:1NIO"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:1NIO"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1NIO"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:1NIO"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:1NIO"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:1NIO"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1NIO"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1NIO"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:1NIO"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:1NIO"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:1NIO"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:1NIO"
FT HELIX 111..118
FT /evidence="ECO:0007829|PDB:1NIO"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1NIO"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:1NIO"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1NIO"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:1NIO"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:1NIO"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:1NIO"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:1NIO"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:1NIO"
FT HELIX 193..203
FT /evidence="ECO:0007829|PDB:1NIO"
FT TURN 204..208
FT /evidence="ECO:0007829|PDB:1NIO"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:1NIO"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:1NIO"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:1NIO"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:1NIO"
SQ SEQUENCE 250 AA; 27293 MW; F01A8DC8A1078700 CRC64;
ANVSFSLSGA DSKSYSKFIT ALRKALPSKE KVSNIPLLLP SASGASRYIL MQLSNYDAKA
ITMAIDVTNV YIMGYLVNST SYFANESDAK LASQYVFKGS TLVTIPYSGN YERLQNAAGK
IREKIPLGFR ALDSALTSIF HYDSTAAAAA FLVILQTTAE ASRFKYIEGQ IIERIPKNEV
PSPAALSLEN EAWSLLSKQI QLAQTNNGAF RTPVVIIDNK GQRVEITNLA SKVQIKDVNS
KLLLNKQNIA