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P00655 (RNAS_ASPGI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease alpha-sarcin

EC=3.1.27.10
Alternative name(s):
rRNA endonuclease
Gene names
Name:sar
OrganismAspergillus giganteus
Taxonomic identifier5060 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Alpha-sarcin is specific for purines in both single- and double-stranded RNA. Its toxic action on eukaryotic cells is the result of cleavage of a single phosphodiester bond in the 60S subunit of ribosomes.

Catalytic activity

Hydrolysis of the phosphodiester linkage between guanosine and adenosine residues at one specific position in 28S rRNA from rat ribosomes.

Subcellular location

Secreted.

Sequence similarities

Belongs to the ribonuclease U2 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Nuclease
Protein synthesis inhibitor
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processnegative regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: InterPro

rRNA endonuclease activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.3
Chain28 – 177150Ribonuclease alpha-sarcin
PRO_0000030836

Sites

Active site771
Active site1231Proton acceptor
Active site1641Proton donor

Amino acid modifications

Disulfide bond33 ↔ 175
Disulfide bond103 ↔ 159

Secondary structure

.................................. 177
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00655 [UniParc].

Last modified March 1, 1992. Version 2.
Checksum: 6C711D9482DC9DD1

FASTA17719,724
        10         20         30         40         50         60 
MVAIKNLVLV ALTAVTALAV PSPLEARAVT WTCLNDQKNP KTNKYETKRL LYNQNKAESN 

        70         80         90        100        110        120 
SHHAPLSDGK TGSSYPHWFT NGYDGDGKLP KGRTPIKFGK SDCDRPPKHS KDGNGKTDHY 

       130        140        150        160        170 
LLEFPTFPDG HDYKFDSKKP KENPGPARVI YTYPNKVFCG IIAHTKENQG ELKLCSH 

« Hide

References

[1]"Complete nucleotide sequence of cDNA for the cytotoxin alpha sarcin."
Oka T., Natori Y., Tanaka S., Tsurugi K., Endo Y.
Nucleic Acids Res. 18:1897-1897(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: MDH 18894.
[2]Wnendt S., Felske H., Henze P.P., Ulbrich N., Stahl U.
Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MDH 18894.
[3]"The primary structure of the cytotoxin alpha-sarcin."
Sacco G., Drickamer K., Wool I.G.
J. Biol. Chem. 258:5811-5818(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-177.
[4]"The highly refined solution structure of the cytotoxic ribonuclease alpha-sarcin reveals the structural requirements for substrate recognition and ribonucleolytic activity."
Perez-Canadillas J.M., Santoro J., Campos-Olivas R., Lacadena J., Martinez del Pozo A., Gavilanes J.G., Rico M., Bruix M.
J. Mol. Biol. 299:1061-1073(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 28-177.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13704 mRNA. Translation: BAA02863.1.
X60770 Genomic DNA. Translation: CAA43180.1.
PIRNRASSG. JU0138.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DE3NMR-A28-177[»]
1R4YNMR-A50-177[»]
ProteinModelPortalP00655.
SMRP00655. Positions 28-177.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.10.450.30. 1 hit.
InterProIPR004025. Fun_ribotoxin.
IPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamPF00545. Ribonuclease. 1 hit.
[Graphical view]
PIRSFPIRSF037430. RNase_U2. 1 hit.
PRINTSPR01704. FUNRIBOTOXIN.
SUPFAMSSF53933. SSF53933. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP00655.

Entry information

Entry nameRNAS_ASPGI
AccessionPrimary (citable) accession number: P00655
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 1, 1992
Last modified: April 16, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references