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Protein

Guanyl-specific ribonuclease Ms

Gene
N/A
Organism
Aspergillus phoenicis (Aspergillus saitoi)
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei391
Active sitei57Proton acceptor1
Active sitei91Proton donor1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Names & Taxonomyi

Protein namesi
Recommended name:
Guanyl-specific ribonuclease Ms (EC:3.1.27.3)
Short name:
RNase Ms
OrganismiAspergillus phoenicis (Aspergillus saitoi)
Taxonomic identifieri5063 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001373701 – 105Guanyl-specific ribonuclease MsAdd BLAST105

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi3 ↔ 11
Disulfide bondi7 ↔ 102

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1105
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Beta strandi10 – 12Combined sources3
Helixi14 – 30Combined sources17
Beta strandi37 – 41Combined sources5
Beta strandi55 – 60Combined sources6
Beta strandi74 – 80Combined sources7
Beta strandi85 – 91Combined sources7
Beta strandi94 – 97Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RDSX-ray1.80A1-105[»]
1RMSX-ray1.90A1-105[»]
ProteinModelPortaliP00653.
SMRiP00653.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00653.

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.

P00653-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ESCEYTCGST CYWSSDVSAA KAKGYSLYES GDTIDDYPHG YHDYEGFDFP
60 70 80 90 100
VSGTYYEYPI MSDYDVYTGG SPGADRVIFN GDDELAGVIT HTGASGDDFV

ACSSS
Length:105
Mass (Da):11,332
Last modified:August 1, 1991 - v2
Checksum:i94CF56D109242EFD
GO

Sequence databases

PIRiA00800. NRASTP.

Cross-referencesi

Sequence databases

PIRiA00800. NRASTP.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RDSX-ray1.80A1-105[»]
1RMSX-ray1.90A1-105[»]
ProteinModelPortaliP00653.
SMRiP00653.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00653.

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 nameiRNMS_ASPPH
AccessioniPrimary (citable) accession number: P00653
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1991
Last modified: November 2, 2016
This is version 93 of the entry and version 2 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.