ID D6MWJ6_RICCO Unreviewed; 529 AA.
AC D6MWJ6;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Preproricin {ECO:0000313|EMBL:ADG29062.1};
DE Flags: Fragment;
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|EMBL:ADG29062.1};
RN [1] {ECO:0000313|EMBL:ADG29062.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20211195; DOI=10.1016/j.toxicon.2010.03.001;
RA Weeks A., Leshin J.A., Dretchen K.L., Skowronski E.W., O'Connell K.P.;
RT "Population-level variation of the preproricin gene contradicts expectation
RT of neutral equilibrium for generalist plant defense toxins.";
RL Toxicon 55:1475-1483(2010).
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:0000256|ARBA:ARBA00000237};
CC -!- SIMILARITY: In the N-terminal section; belongs to the ribosome-
CC inactivating protein family. Type 2 RIP subfamily.
CC {ECO:0000256|ARBA:ARBA00010414}.
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DR EMBL; GQ916853; ADG29062.1; -; Genomic_DNA.
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:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 2.
DR Gene3D; 2.80.10.50; -; 2.
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 InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR33453; -; 1.
DR PANTHER; PTHR33453:SF34; DUF6598 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00652; Ricin_B_lectin; 2.
DR Pfam; PF00161; RIP; 1.
DR PRINTS; PR00396; SHIGARICIN.
DR SMART; SM00458; RICIN; 2.
DR SUPFAM; SSF56371; Ribosome inactivating proteins (RIP); 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 2.
DR PROSITE; PS50231; RICIN_B_LECTIN; 2.
DR PROSITE; PS00275; SHIGA_RICIN; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein synthesis inhibitor {ECO:0000256|ARBA:ARBA00023193};
KW Toxin {ECO:0000256|ARBA:ARBA00022656}.
FT DOMAIN 301..427
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT DOMAIN 431..529
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADG29062.1"
FT NON_TER 529
FT /evidence="ECO:0000313|EMBL:ADG29062.1"
SQ SEQUENCE 529 AA; 58795 MW; 8E20013BFF92E68E CRC64;
GSTSGWSFTL EDNNIFPKQY PIINFTTAGA TVQSYTNFIR AVRGRLTTGA DVRHEIPVLP
NRVGLPINQR FILVELSNHA ELSVTLALDV TNAYVVGYRA GNSAYFFHPD NQEDAEAITH
LFTDVQNRYT FAFGGNYDRL EQLAGNLREN IELGNGPLEE AISALYYYST GGTQLPTLAR
SFIICIQMIS EAARFQYIEG EMRTRIRYNR RSAPDPSVIT LENSWGRLST AIQESNQGAF
ASPIQLQRRN GSKFSVYDVS ILIPIIALMV YRCAPPPSSQ FSLLIRPVVP NFNADVCMDP
EPIVRIVGRN GLCVDVRDGR FHNGNAIQLW PCKSNTDANQ LWTLKRDNTI RSNGKCLTTY
GYSPGVYVMI YDCNTAATDA TRWQIWDNGT IINPRSSLVL AATSGNSGTT LTVQTNIYAV
SQGWLPTNNT QPFVTTIVGL YGXCLQANSG QVWIEDCXSE KAEQQWALYA DGSIRPQQNR
DNCLTSDSNI RETVVKILSC GPASSGQRWM FKNDGTILNL YXGLVLDVR
//
