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Protein

Guanyl-specific ribonuclease Po1

Gene
N/A
Organism
Pleurotus ostreatus (Oyster mushroom) (White-rot fungus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Enzyme regulationi

Inhibited by divalent cations. Inhibition decreases in the order zinc, lead, cadmium, nickel, mercury.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei36By similarity1
Active sitei54Proton acceptorBy similarity1
Active sitei87Proton donorBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Names & Taxonomyi

Protein namesi
Recommended name:
Guanyl-specific ribonuclease Po1 (EC:3.1.27.3)
Short name:
RNase Po1
OrganismiPleurotus ostreatus (Oyster mushroom) (White-rot fungus)
Taxonomic identifieri5322 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesPleurotaceaePleurotus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001373741 – 101Guanyl-specific ribonuclease Po1Add BLAST101

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1Pyrrolidone carboxylic acid1
Disulfide bondi7 ↔ 84Sequence analysis
Disulfide bondi9 ↔ 99By similarity
Disulfide bondi48 ↔ 82By similarity

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Structurei

Secondary structure

1101
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 9Combined sources3
Beta strandi12 – 14Combined sources3
Helixi16 – 27Combined sources12
Beta strandi34 – 38Combined sources5
Beta strandi50 – 56Combined sources7
Beta strandi59 – 61Combined sources3
Beta strandi70 – 76Combined sources7
Beta strandi80 – 87Combined sources8
Beta strandi91 – 94Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WHOX-ray1.85A/B/C1-101[»]
3WR2X-ray1.75A/B/C/D/E/F1-101[»]
ProteinModelPortaliP81762.
SMRiP81762.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribonuclease N1/T1 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.

P81762-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
QTGVRSCNCA GRSFTGTDVT NAIRSARAGG SGNYPHVYNN FEGFSFSCTP
60 70 80 90 100
TFFEFPVFRG SVYSGGSPGA DRVIYDQSGR FCACLTHTGA PSTNGFVECR

F
Length:101
Mass (Da):10,789
Last modified:June 1, 2001 - v1
Checksum:iFF30477497990D00
GO

Sequence databases

PIRiJX0333.

Cross-referencesi

Sequence databases

PIRiJX0333.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WHOX-ray1.85A/B/C1-101[»]
3WR2X-ray1.75A/B/C/D/E/F1-101[»]
ProteinModelPortaliP81762.
SMRiP81762.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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 nameiRNPO_PLEOS
AccessioniPrimary (citable) accession number: P81762
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 57 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

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.