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Protein

Ribonuclease alpha-sarcin

Gene

sar

Organism
Aspergillus giganteus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei77 – 771
Active sitei123 – 1231Proton acceptor
Active sitei164 – 1641Proton donor

GO - Molecular functioni

  1. RNA binding Source: InterPro
  2. rRNA endonuclease activity Source: UniProtKB-EC

GO - Biological processi

  1. negative regulation of translation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nuclease, Protein synthesis inhibitor

Enzyme and pathway databases

BRENDAi3.1.27.10. 510.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease alpha-sarcin (EC:3.1.27.10)
Alternative name(s):
rRNA endonuclease
Gene namesi
Name:sar
OrganismiAspergillus giganteus
Taxonomic identifieri5060 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Chaini28 – 177150Ribonuclease alpha-sarcinPRO_0000030836Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 ↔ 175
Disulfide bondi103 ↔ 159

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
177
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 3910Combined sources
Turni40 – 434Combined sources
Beta strandi44 – 5310Combined sources
Helixi54 – 607Combined sources
Turni61 – 633Combined sources
Beta strandi66 – 694Combined sources
Beta strandi71 – 733Combined sources
Beta strandi76 – 783Combined sources
Beta strandi85 – 873Combined sources
Turni101 – 1033Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi115 – 1173Combined sources
Beta strandi122 – 1243Combined sources
Beta strandi134 – 1363Combined sources
Beta strandi146 – 1516Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi158 – 1669Combined sources
Turni167 – 1693Combined sources
Beta strandi172 – 1743Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DE3NMR-A28-177[»]
1R4YNMR-A28-177[»]
SMRiP00655. Positions 28-177.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00655.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribonuclease U2 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.10.450.30. 1 hit.
InterProiIPR004025. Fun_ribotoxin.
IPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamiPF00545. Ribonuclease. 1 hit.
[Graphical view]
PIRSFiPIRSF037430. RNase_U2. 1 hit.
PRINTSiPR01704. FUNRIBOTOXIN.
SUPFAMiSSF53933. SSF53933. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00655-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAIKNLVLV ALTAVTALAV PSPLEARAVT WTCLNDQKNP KTNKYETKRL
60 70 80 90 100
LYNQNKAESN SHHAPLSDGK TGSSYPHWFT NGYDGDGKLP KGRTPIKFGK
110 120 130 140 150
SDCDRPPKHS KDGNGKTDHY LLEFPTFPDG HDYKFDSKKP KENPGPARVI
160 170
YTYPNKVFCG IIAHTKENQG ELKLCSH
Length:177
Mass (Da):19,724
Last modified:March 1, 1992 - v2
Checksum:i6C711D9482DC9DD1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13704 mRNA. Translation: BAA02863.1.
X60770 Genomic DNA. Translation: CAA43180.1.
PIRiJU0138. NRASSG.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13704 mRNA. Translation: BAA02863.1.
X60770 Genomic DNA. Translation: CAA43180.1.
PIRiJU0138. NRASSG.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DE3NMR-A28-177[»]
1R4YNMR-A28-177[»]
SMRiP00655. Positions 28-177.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.27.10. 510.

Miscellaneous databases

EvolutionaryTraceiP00655.

Family and domain databases

Gene3Di3.10.450.30. 1 hit.
InterProiIPR004025. Fun_ribotoxin.
IPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamiPF00545. Ribonuclease. 1 hit.
[Graphical view]
PIRSFiPIRSF037430. RNase_U2. 1 hit.
PRINTSiPR01704. FUNRIBOTOXIN.
SUPFAMiSSF53933. SSF53933. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiRNAS_ASPGI
AccessioniPrimary (citable) accession number: P00655
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 1, 1992
Last modified: April 1, 2015
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.