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Reviewed, UniProtKB/Swiss-Prot P84786 (RIP_DRIMA)

Last modified February 9, 2010. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ribosome-inactivating protein charybdin
    EC=3.2.2.22
Alternative name(s):
    rRNA N-glycosidase
OrganismDrimia maritima (Sea squill) (Charybdis maritima)
Taxonomic identifier82070 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAsparagalesAsparagaceaeScilloideaeCharybdis

Protein attributes

Sequence length257 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Inhibits translation in rabbit reticulocytes. Ref.1

Catalytic activity

Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA. Ref.1

Sequence similarities

Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 257257Ribosome-inactivating protein charybdin
PRO_0000248258

Sites

Active site1671 Ref.1
Site791Important for catalytic activity Ref.1
Site1171Important for catalytic activity Ref.1
Site1701Important for catalytic activity Ref.1

Amino acid modifications

Disulfide bond217 ↔ 254 Ref.1

Secondary structure

................................................ 257
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P84786-1 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 12EB2E35328175AE

FASTA25729,252
        10         20         30         40         50         60 
SQCKAMTVKF TVELDIERLT GQTYTDFIKN LRRSLATWYL HGVPVLPLYN QEADPRGFDL 

        70         80         90        100        110        120 
KLTFRGQVTT VRIHRDDLVL RGYQMQGAGK WLELERPSTQ TGHLIEGSEL LEFGPSYEEL 

       130        140        150        160        170        180 
AAAAQQDILD ISYNKNALQD AVSKLAVSTN TRDRARSLIV VSQMFCEATR FVDIANHFAF 

       190        200        210        220        230        240 
NLESSEPVKL PQWMQNDLEK NWVRFSFMIL KSNADPCYKF EPQTIYGKII KTADELLNFL 

       250 
GIVEQHPDTR SPPCAAG 

« Hide

References

[1]"Isolation, characterization, sequencing and crystal structure of charybdin, a type 1 ribosome-inactivating protein from Charybdis maritima agg."
Touloupakis E., Gessmann R., Kavelaki K., Christofakis E., Petratos K., Ghanotakis D.F.
FEBS J. 273:2684-2692(2006) [PubMed: 16817896] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-14 AND 242-257, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-252, X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY.
Tissue: Bulb.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ323742 Genomic DNA. No translation available.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B7UX-ray1.60A1-257[»]
ModBaseSearch...

Family and domain databases

InterProIPR001574. Ribosome_inactivat_prot.
IPR016138. Ribosome_inactivat_prot_sub1.
IPR017989. Ribosome_inactivat_prot_subgr.
[Graphical view]
Gene3DG3DSA:3.40.420.10. Ribosome_inactivat_prot_sub1. 1 hit.
PfamPF00161. RIP. 1 hit.
[Graphical view]
PRINTSPR00396. SHIGARICIN.
PROSITEPS00275. SHIGA_RICIN. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIP_DRIMA
AccessionPrimary (citable) accession number: P84786
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: February 9, 2010
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents