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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei39 – 391
Active sitei57 – 571Proton acceptor
Active sitei91 – 911Proton donor

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 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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 105105Guanyl-specific ribonuclease MsPRO_0000137370Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi3 ↔ 11
Disulfide bondi7 ↔ 102

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
105
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Beta strandi10 – 123Combined sources
Helixi14 – 3017Combined sources
Beta strandi37 – 415Combined sources
Beta strandi55 – 606Combined sources
Beta strandi74 – 807Combined sources
Beta strandi85 – 917Combined sources
Beta strandi94 – 974Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RDSX-ray1.80A1-105[»]
1RMSX-ray1.90A1-105[»]
ProteinModelPortaliP00653.
SMRiP00653. Positions 1-105.
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.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1RDSX-ray1.80A1-105[»]
1RMSX-ray1.90A1-105[»]
ProteinModelPortaliP00653.
SMRiP00653. Positions 1-105.
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.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamiPF00545. Ribonuclease. 1 hit.
[Graphical view]
SUPFAMiSSF53933. SSF53933. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Primary structure of a minor ribonuclease from Aspergillus saitoi."
    Watanabe H., Ohgi K., Irie M.
    J. Biochem. 91:1495-1509(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "Three-dimensional structure of ribonuclease Ms*3'-guanylic acid complex at 2.5-A resolution."
    Nonaka T., Mitsui Y., Irie M., Nakamura K.T.
    FEBS Lett. 283:207-209(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SEQUENCE REVISION TO 52-54; 80 AND 95.

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 26, 2014
This is version 89 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

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.