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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei36 – 361By similarity
Active sitei54 – 541Proton acceptorBy similarity
Active sitei87 – 871Proton donorBy similarity

GO - Molecular functioni

  1. endoribonuclease activity Source: InterPro
  2. ribonuclease T1 activity Source: UniProtKB-EC
  3. RNA binding Source: InterPro
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 101101Guanyl-specific ribonuclease Po1PRO_0000137374Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Pyrrolidone carboxylic acid
Disulfide bondi7 ↔ 84Sequence Analysis
Disulfide bondi9 ↔ 99By similarity
Disulfide bondi48 ↔ 82By similarity

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Structurei

Secondary structure

1
101
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93Combined sources
Beta strandi12 – 143Combined sources
Helixi16 – 2712Combined sources
Beta strandi34 – 385Combined sources
Beta strandi50 – 567Combined sources
Beta strandi70 – 767Combined sources
Beta strandi80 – 878Combined sources
Beta strandi91 – 944Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WHOX-ray1.85A/B/C1-101[»]
ProteinModelPortaliP81762.
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.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
3WHOX-ray1.85A/B/C1-101[»]
ProteinModelPortaliP81762.
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.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamiPF00545. Ribonuclease. 1 hit.
[Graphical view]
SUPFAMiSSF53933. SSF53933. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Purification and primary structure of a new guanylic acid specific ribonuclease from Pleurotus ostreatus."
    Nomura H., Inokuchi N., Kobayashi H., Koyama T., Iwama M., Ohgi K., Irie M.
    J. Biochem. 116:26-33(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, CHARACTERIZATION.

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 26, 2014
This is version 53 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

External Data

Dasty 3

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 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.