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P00654

- RNU2_USTSP

UniProt

P00654 - RNU2_USTSP

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Protein

Ribonuclease U2

Gene

RNU2

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

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
Complete GO annotation...

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

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 – 95Combined sources
Beta strandi12 – 154Combined sources
Helixi16 – 3116Combined sources
Helixi36 – 383Combined sources
Beta strandi41 – 433Combined sources
Helixi47 – 493Combined sources
Beta strandi60 – 645Combined sources
Beta strandi75 – 773Combined sources
Beta strandi83 – 897Combined sources
Turni90 – 923Combined sources
Beta strandi95 – 1017Combined sources
Beta strandi105 – 1095Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
CDIPQSTNCG GNVYSNDDIN TAIQGALDDV ANGDRPDNYP HQYYDEASED
60 70 80 90 100
ITLCCGSGPW SEFPLVYNGP YYSSRDNYVS PGPDRVIYQT NTGEFCATVT
110
HTGAASYDGF TQCS
Length:114
Mass (Da):12,387
Last modified:December 15, 1998 - v4
Checksum:i96D32CB2E23AAB98
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ004827 Genomic DNA. Translation: CAC04098.1.
PIRiPC4081. NRUSU2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ004827 Genomic DNA. Translation: CAC04098.1 .
PIRi PC4081. NRUSU2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

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: November 26, 2014
This is version 88 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