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P00655

- RNAS_ASPGI

UniProt

P00655 - RNAS_ASPGI

Protein

Ribonuclease alpha-sarcin

Gene

sar

Organism
Aspergillus giganteus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (01 Mar 1992)
      Previous versions | rss
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    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

    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-SubCell

    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.

    P00655-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVAIKNLVLV ALTAVTALAV PSPLEARAVT WTCLNDQKNP KTNKYETKRL    50
    LYNQNKAESN SHHAPLSDGK TGSSYPHWFT NGYDGDGKLP KGRTPIKFGK 100
    SDCDRPPKHS KDGNGKTDHY LLEFPTFPDG HDYKFDSKKP KENPGPARVI 150
    YTYPNKVFCG IIAHTKENQG ELKLCSH 177
    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 1, 2014
    This is version 93 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