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P00654 (RNU2_USTSP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease U2

Short name=RNase U2
EC=3.1.27.4
Gene names
Name:RNU2
OrganismUstilago sphaerogena (Smut fungus)
Taxonomic identifier5271 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaeUstilago

Protein attributes

Sequence length114 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Miscellaneous

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

Sequence similarities

Belongs to the ribonuclease U2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 114114Ribonuclease U2
PRO_0000137379

Regions

Region39 – 4911Substrate binding
Region108 – 1103Substrate binding

Sites

Active site411 Ref.5
Active site621Proton acceptor Ref.5
Active site1011Proton donor Ref.5
Metal binding291Calcium 1
Metal binding291Calcium 2
Metal binding301Calcium 1; via carbonyl oxygen
Metal binding311Calcium 2; via carbonyl oxygen
Metal binding321Calcium 1
Metal binding321Calcium 2
Metal binding371Calcium 1
Metal binding391Calcium 2; via carbonyl oxygen
Binding site851Substrate
Site621Methylation inactivates enzyme Ref.6

Amino acid modifications

Disulfide bond1 ↔ 54 Ref.4 Ref.7
Disulfide bond9 ↔ 113 Ref.4 Ref.7
Disulfide bond55 ↔ 96 Ref.4 Ref.7

Secondary structure

....................... 114
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00654 [UniParc].

Last modified December 15, 1998. Version 4.
Checksum: 96D32CB2E23AAB98

FASTA11412,387
        10         20         30         40         50         60 
CDIPQSTNCG GNVYSNDDIN TAIQGALDDV ANGDRPDNYP HQYYDEASED ITLCCGSGPW 

        70         80         90        100        110 
SEFPLVYNGP YYSSRDNYVS PGPDRVIYQT NTGEFCATVT HTGAASYDGF TQCS 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ004827 Genomic DNA. Translation: CAC04098.1.
PIRNRUSU2. PC4081.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP00654.
SMRP00654. Positions 1-114.
ModBaseSearch...
MobiDBSearch...

Chemistry

DrugBankDB00128. L-Aspartic Acid.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.1.27.4. 6588.

Family and domain databases

Gene3D3.10.450.30. 1 hit.
InterProIPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamPF00545. Ribonuclease. 1 hit.
[Graphical view]
SUPFAMSSF53933. SSF53933. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP00654.
PROP00654.

Entry information

Entry nameRNU2_USTSP
AccessionPrimary (citable) accession number: P00654
Secondary accession number(s): Q9HGK7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 15, 1998
Last modified: April 16, 2014
This is version 84 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references