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P67876

- RNMG_ASPRE

UniProt

P67876 - RNMG_ASPRE

Protein

Ribonuclease mitogillin

Gene

ret

Organism
Aspergillus restrictus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      Previous versions | rss
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    Functioni

    This purine-specific ribonuclease cleaves 28S RNA in eukaryotic ribosomes, inhibits protein synthesis, and shows antitumor activity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei76 – 761
    Active sitei122 – 1221Proton acceptor
    Active sitei163 – 1631Proton donor

    GO - Molecular functioni

    1. endoribonuclease activity Source: InterPro
    2. RNA binding Source: InterPro

    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 mitogillin (EC:3.1.27.-)
    Alternative name(s):
    Restrictocin
    Gene namesi
    Name:ret
    OrganismiAspergillus restrictus
    Taxonomic identifieri5064 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Protein family/group databases

    Allergomei3050. Asp r 1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 27271 PublicationAdd
    BLAST
    Chaini28 – 176149Ribonuclease mitogillinPRO_0000030838Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi32 ↔ 174
    Disulfide bondi102 ↔ 158

    Keywords - PTMi

    Disulfide bond

    Structurei

    Secondary structure

    1
    176
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 357
    Turni39 – 424
    Beta strandi46 – 527
    Helixi53 – 6210
    Beta strandi65 – 684
    Beta strandi70 – 723
    Beta strandi75 – 784
    Beta strandi84 – 863
    Helixi100 – 1034
    Beta strandi118 – 1247
    Turni137 – 1404
    Beta strandi145 – 1528
    Beta strandi157 – 1659
    Beta strandi171 – 1733

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AQZX-ray1.70A/B28-176[»]
    1JBRX-ray2.15A/B28-176[»]
    1JBSX-ray1.97A/B28-176[»]
    1JBTX-ray2.70A/B28-176[»]
    ProteinModelPortaliP67876.
    SMRiP67876. Positions 28-176.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP67876.

    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.

    P67876-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVAIKNLFLL AATAVSVLAA PSPLDARATW TCINQQLNPK TNKWEDKRLL    50
    YSQAKAESNS HHAPLSDGKT GSSYPHWFTN GYDGNGKLIK GRTPIKFGKA 100
    DCDRPPKHSQ NGMGKDDHYL LEFPTFPDGH DYKFDSKKPK EDPGPARVIY 150
    TYPNKVFCGI VAHQRGNQGD LRLCSH 176
    Length:176
    Mass (Da):19,595
    Last modified:October 11, 2004 - v1
    Checksum:iAAD431C57939E42C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti52 – 521S → N in AAA32707. 1 PublicationCurated
    Sequence conflicti142 – 1421D → N AA sequence (PubMed:3994994)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56176 Genomic DNA. Translation: CAA39637.1.
    M55508 mRNA. Translation: AAA32706.1.
    M65257 Genomic DNA. Translation: AAA32707.1.
    PIRiS22294. NRASMR.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56176 Genomic DNA. Translation: CAA39637.1 .
    M55508 mRNA. Translation: AAA32706.1 .
    M65257 Genomic DNA. Translation: AAA32707.1 .
    PIRi S22294. NRASMR.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AQZ X-ray 1.70 A/B 28-176 [» ]
    1JBR X-ray 2.15 A/B 28-176 [» ]
    1JBS X-ray 1.97 A/B 28-176 [» ]
    1JBT X-ray 2.70 A/B 28-176 [» ]
    ProteinModelPortali P67876.
    SMRi P67876. Positions 28-176.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    Allergomei 3050. Asp r 1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P67876.

    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. "Isolation and nucleotide sequence of the Aspergillus restrictus gene coding for the ribonucleolytic toxin restrictocin and its expression in Aspergillus nidulans: the leader sequence protects producing strains from suicide."
      Lamy B., Davies J.
      Nucleic Acids Res. 19:1001-1006(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 34475 / NRRL 2869.
    2. "Secretion of a potential virulence factor, a fungal ribonucleotoxin, during human aspergillosis infections."
      Lamy B., Moutaouakil M., Latge J.P., Davies J.
      Mol. Microbiol. 5:1811-1815(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 34475 / NRRL 2869.
    3. "Regulation and sequence of the restrictocin gene of Aspergillus restrictus."
      Yang R., Kenealy W.R.
      Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: ATCC 34475 / NRRL 2869.
    4. "Complete amino acid sequence of the Aspergillus cytotoxin mitogillin."
      Fernandez-Luna J.L., Lopez-Otin C., Soriano F., Mendez E.
      Biochemistry 24:861-867(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-176.
    5. "Insights into specificity of cleavage and mechanism of cell entry from the crystal structure of the highly specific Aspergillus ribotoxin, restrictocin."
      Yang X., Moffat K.
      Structure 4:837-852(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 28-176.
    6. "Crystal structures of restrictocin-inhibitor complexes with implications for RNA recognition and base flipping."
      Yang X., Gerczei T., Glover L.T., Correll C.C.
      Nat. Struct. Biol. 8:968-973(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 28-176.

    Entry informationi

    Entry nameiRNMG_ASPRE
    AccessioniPrimary (citable) accession number: P67876
    Secondary accession number(s): P04389, P19792
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 52 of the entry and version 1 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