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P00655

- RNAS_ASPGI

UniProt

P00655 - RNAS_ASPGI

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Protein

Ribonuclease alpha-sarcin

Gene

sar

Organism
Aspergillus giganteus
Status
Reviewed - 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

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-KW
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 – 3910
Turni40 – 434
Beta strandi44 – 5310
Helixi54 – 607
Turni61 – 633
Beta strandi66 – 694
Beta strandi71 – 733
Beta strandi76 – 783
Beta strandi85 – 873
Turni101 – 1033
Beta strandi111 – 1133
Beta strandi115 – 1173
Beta strandi122 – 1243
Beta strandi134 – 1363
Beta strandi146 – 1516
Beta strandi153 – 1553
Beta strandi158 – 1669
Turni167 – 1693
Beta strandi172 – 1743

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DE3NMR-A28-177[»]
1R4YNMR-A28-177[»]
ProteinModelPortaliP00655.
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 [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:
EMBL
GenBank
DDBJ
Links Updated
D13704 mRNA. Translation: BAA02863.1.
X60770 Genomic DNA. Translation: CAA43180.1.
PIRiJU0138. NRASSG.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D13704 mRNA. Translation: BAA02863.1 .
X60770 Genomic DNA. Translation: CAA43180.1 .
PIRi JU0138. NRASSG.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DE3 NMR - A 28-177 [» ]
1R4Y NMR - A 28-177 [» ]
ProteinModelPortali P00655.
SMRi P00655. Positions 28-177.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P00655.

Family and domain databases

Gene3Di 3.10.450.30. 1 hit.
InterProi IPR004025. Fun_ribotoxin.
IPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view ]
Pfami PF00545. Ribonuclease. 1 hit.
[Graphical view ]
PIRSFi PIRSF037430. RNase_U2. 1 hit.
PRINTSi PR01704. FUNRIBOTOXIN.
SUPFAMi SSF53933. SSF53933. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 94 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