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P00654

- RNU2_USTSP

UniProt

P00654 - RNU2_USTSP

Protein

Ribonuclease U2

Gene

RNU2

Organism
Ustilago sphaerogena (Smut fungus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Catalytic activityi

    Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in A-P or G-P with 2',3'-cyclic phosphate intermediates.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi29 – 291Calcium 11 Publication
    Metal bindingi29 – 291Calcium 21 Publication
    Metal bindingi30 – 301Calcium 1; via carbonyl oxygen1 Publication
    Metal bindingi31 – 311Calcium 2; via carbonyl oxygen1 Publication
    Metal bindingi32 – 321Calcium 11 Publication
    Metal bindingi32 – 321Calcium 21 Publication
    Metal bindingi37 – 371Calcium 11 Publication
    Metal bindingi39 – 391Calcium 2; via carbonyl oxygen1 Publication
    Active sitei41 – 4111 Publication
    Active sitei62 – 621Proton acceptor1 Publication
    Sitei62 – 621Methylation inactivates enzyme1 Publication
    Binding sitei85 – 851Substrate
    Active sitei101 – 1011Proton donor1 Publication

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. ribonuclease U2 activity Source: UniProtKB-EC
    3. RNA binding Source: InterPro

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.1.27.4. 6588.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonuclease U2 (EC:3.1.27.4)
    Short name:
    RNase U2
    Gene namesi
    Name:RNU2
    OrganismiUstilago sphaerogena (Smut fungus)
    Taxonomic identifieri5271 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaeUstilago

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 114114Ribonuclease U2PRO_0000137379Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi1 ↔ 541 Publication
    Disulfide bondi9 ↔ 1131 Publication
    Disulfide bondi55 ↔ 961 Publication

    Keywords - PTMi

    Disulfide bond

    Structurei

    Secondary structure

    1
    114
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 95
    Beta strandi12 – 154
    Helixi16 – 3116
    Helixi36 – 383
    Beta strandi41 – 433
    Helixi47 – 493
    Beta strandi60 – 645
    Beta strandi75 – 773
    Beta strandi83 – 897
    Turni90 – 923
    Beta strandi95 – 1017
    Beta strandi105 – 1095

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RTUX-ray1.80A1-114[»]
    3AGNX-ray0.96A1-114[»]
    3AGOX-ray0.99A1-114[»]
    3AHSX-ray1.32A/B/C1-114[»]
    3AHWX-ray1.03A1-114[»]
    ProteinModelPortaliP00654.
    SMRiP00654. Positions 1-114.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00654.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni39 – 4911Substrate bindingAdd
    BLAST
    Regioni108 – 1103Substrate binding

    Sequence similaritiesi

    Belongs to the ribonuclease U2 family.Curated

    Family and domain databases

    Gene3Di3.10.450.30. 1 hit.
    InterProiIPR000026. Gua-sp_ribonuclease_N1/T1.
    IPR016191. Ribonuclease/ribotoxin.
    [Graphical view]
    PfamiPF00545. Ribonuclease. 1 hit.
    [Graphical view]
    SUPFAMiSSF53933. SSF53933. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P00654-1 [UniParc]FASTAAdd to Basket

    « Hide

    CDIPQSTNCG GNVYSNDDIN TAIQGALDDV ANGDRPDNYP HQYYDEASED    50
    ITLCCGSGPW SEFPLVYNGP YYSSRDNYVS PGPDRVIYQT NTGEFCATVT 100
    HTGAASYDGF TQCS 114
    Length:114
    Mass (Da):12,387
    Last modified:December 15, 1998 - v4
    Checksum:i96D32CB2E23AAB98
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ004827 Genomic DNA. Translation: CAC04098.1.
    PIRiPC4081. NRUSU2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ004827 Genomic DNA. Translation: CAC04098.1 .
    PIRi PC4081. NRUSU2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RTU X-ray 1.80 A 1-114 [» ]
    3AGN X-ray 0.96 A 1-114 [» ]
    3AGO X-ray 0.99 A 1-114 [» ]
    3AHS X-ray 1.32 A/B/C 1-114 [» ]
    3AHW X-ray 1.03 A 1-114 [» ]
    ProteinModelPortali P00654.
    SMRi P00654. Positions 1-114.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    DrugBanki DB00128. L-Aspartic Acid.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 3.1.27.4. 6588.

    Miscellaneous databases

    EvolutionaryTracei P00654.
    PROi P00654.

    Family and domain databases

    Gene3Di 3.10.450.30. 1 hit.
    InterProi IPR000026. Gua-sp_ribonuclease_N1/T1.
    IPR016191. Ribonuclease/ribotoxin.
    [Graphical view ]
    Pfami PF00545. Ribonuclease. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53933. SSF53933. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The amino acid sequence of ribonuclease U2 from Ustilago sphaerogena."
      Sato S., Uchida T.
      Biochem. J. 145:353-360(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    2. "Ribonuclease U2: cloning, production in Pichia pastoris and affinity chromatography purification of the active recombinant protein."
      Martinez-Ruiz A., Garcia-Ortega L., Kao R., Onaderra M., Mancheno J.M., Davies J., Martinez del Pozo A., Gavilanes J.G.
      FEMS Microbiol. Lett. 189:165-169(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-106.
      Strain: ATCC 12421 / CBS 534.71 / IMI 61828 / 50-135.
    3. "Revised sequence of ribonuclease U2 in the substrate-binding region."
      Kanaya S., Uchida T.
      J. Biochem. 118:681-682(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 44-53, SEQUENCE REVISION.
    4. "The disulfide bridges of ribonuclease U2 from Ustilago sphaerogena."
      Sato S., Uchida T.
      J. Biochem. 77:1171-1176(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    5. Uchida T., Sato S.
      (In) Zelinka J., Balan J. (eds.); Ribosomes and RNA metabolism, pp.453-472, Publ. House Slovak Acad. Sci., Bratislava (1973)
      Cited for: ACTIVE SITE.
    6. "Crystal structure of Ustilago sphaerogena ribonuclease U2 at 1.8-A resolution."
      Noguchi S., Satow Y., Uchida T., Sasaki C., Matsuzaki T.
      Biochemistry 34:15583-15591(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SEQUENCE REVISION.
    7. "Isomerization mechanism of aspartate to isoaspartate implied by structures of Ustilago sphaerogena ribonuclease U2 complexed with adenosine 3'-monophosphate."
      Noguchi S.
      Acta Crystallogr. D 66:843-849(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (0.96 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS AND ADENOSINE 3'-MONOPHOSPHATE, FORMATION OF ISOASPARTATE, DISULFIDE BONDS.
    8. "Structural changes induced by the deamidation and isomerization of asparagine revealed by the crystal structure of Ustilago sphaerogena ribonuclease U2B."
      Noguchi S.
      Biopolymers 93:1003-1010(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS).
    9. "Conformational variation revealed by the crystal structure of RNase U2A complexed with Ca ion and 2'-adenylic acid at 1.03 A resolution."
      Noguchi S.
      Protein Pept. Lett. 17:1559-1561(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.03 ANGSTROMS) IN COMPLEX WITH CALCIUM AND ADENOSINE 2'-PHOSPHATE.

    Entry informationi

    Entry nameiRNU2_USTSP
    AccessioniPrimary (citable) accession number: P00654
    Secondary accession number(s): Q9HGK7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 86 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    After treatment by base Asn-32 and Asp-45 partially isomerise by succinimide rearrangement to form iosaspartyl peptides.

    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