Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ribonuclease U2

Gene

RNU2

Organism
Ustilago sphaerogena (Smut fungus)
Status
Reviewed-Annotation score: 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

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/U2.
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.
PIRiPC4081. NRUSU2.

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...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.27.4. 6588.

Miscellaneous databases

EvolutionaryTraceiP00654.
PROiP00654.

Family and domain databases

Gene3Di3.10.450.30. 1 hit.
InterProiIPR000026. Gua-sp_ribonuclease_N1/T1/U2.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamiPF00545. Ribonuclease. 1 hit.
[Graphical view]
SUPFAMiSSF53933. SSF53933. 1 hit.
ProtoNetiSearch...

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: September 7, 2016
This is version 92 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.