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P05798 (RNSA_STRAU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanyl-specific ribonuclease Sa

Short name=RNase Sa
EC=3.1.27.3
Gene names
Name:rnaSA
OrganismStreptomyces aureofaciens
Taxonomic identifier1894 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length96 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Subcellular location

Secreted.

Sequence similarities

Belongs to the ribonuclease N1/T1 family.

Ontologies

Keywords
   Cellular componentSecreted
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: InterPro

endoribonuclease activity

Inferred from electronic annotation. Source: InterPro

ribonuclease T1 activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P115401EBI-1027193,EBI-1027188From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9696Guanyl-specific ribonuclease Sa
PRO_0000137367

Sites

Active site541Proton acceptor
Active site851Proton donor

Amino acid modifications

Disulfide bond7 ↔ 96

Experimental info

Mutagenesis391N → A, D or S: Decreases protein stability. Ref.8
Sequence conflict721T → C AA sequence Ref.1
Sequence conflict721T → C AA sequence Ref.2

Secondary structure

...................... 96
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05798 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: FA4DB2FD0BA8A7E4

FASTA9610,576
        10         20         30         40         50         60 
DVSGTVCLSA LPPEATDTLN LIASDGPFPY SQDGVVFQNR ESVLPTQSYG YYHEYTVITP 

        70         80         90 
GARTRGTRRI ITGEATQEDY YTGDHYATFS LIDQTC 

« Hide

References

[1]"Amino acid sequence determination of guanyl-specific ribonuclease Sa from Streptomyces aureofaciens."
Shlyapnikov S.V., Both V., Kulikov V.A., Dementiev A.A., Sevcik J., Zelinka J.
FEBS Lett. 209:335-339(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Extracellular guanyl-specific ribonuclease Sa from the actinomycete Streptomyces aureofaciens. Primary structure and homology with ribonucleases from bacteria and fungi."
Shlyapnikov S.V., Both V., Kulikov V.A., Dementiev A.A., Zelinka J.
Bioorg. Khim. 13:760-772(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[3]"Determination and restrained least-squares refinement of the structures of ribonuclease Sa and its complex with 3'-guanylic acid at 1.8-A resolution."
Sevcik J., Dodson E.J., Dodson G.G.
Acta Crystallogr. B 47:240-253(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[4]"Complex of ribonuclease Sa with a cyclic nucleotide and a proposed model for the reaction intermediate."
Sevcik J., Zegers I., Wyns L., Dauter Z., Wilson K.S.
Eur. J. Biochem. 216:301-305(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[5]"Complex of ribonuclease from Streptomyces aureofaciens with 2'-GMP at 1.7-A resolution."
Sevcik J., Hill C.P., Dauter Z., Wilson K.S.
Acta Crystallogr. D 49:257-271(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[6]"Ribonuclease from Streptomyces aureofaciens at atomic resolution."
Sevcik J., Dauter Z., Lamzin V.S., Wilson K.S.
Acta Crystallogr. D 52:327-344(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS), SEQUENCE REVISION TO 72.
[7]"Recognition of RNase Sa by the inhibitor barstar: structure of the complex at 1.7 A resolution."
Sevcik J., Urbanikova L., Dauter Z., Wilson K.S.
Acta Crystallogr. D 54:954-963(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF COMPLEX WITH BARSTAR.
[8]"Contribution of a conserved asparagine to the conformational stability of ribonucleases Sa, Ba, and T1."
Hebert E.J., Giletto A., Sevcik J., Urbanikova L., Wilson K.S., Dauter Z., Pace C.N.
Biochemistry 37:16192-16200(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) AND MUTAGENESIS OF ASN-39.
[9]"Solution structure and dynamics of ribonuclease Sa."
Laurents D., Perez-Canadillas J.M., Santoro J., Rico M., Schell D., Pace C.N., Bruix M.
Proteins 44:200-211(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRNRSM. A25655.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AY7X-ray1.70A1-96[»]
1BOXX-ray1.60A1-96[»]
1C54NMR-A1-96[»]
1GMPX-ray1.70A/B1-96[»]
1GMQX-ray1.80A/B1-96[»]
1GMRX-ray1.77A/B1-96[»]
1I70X-ray1.70A/B1-96[»]
1I8VX-ray1.25A/B1-96[»]
1LNIX-ray1.00A/B1-96[»]
1RGEX-ray1.15A/B1-96[»]
1RGFX-ray1.20A/B1-96[»]
1RGGX-ray1.20A/B1-96[»]
1RGHX-ray1.20A/B1-96[»]
1RSNX-ray2.00A/B1-96[»]
1SARX-ray1.80A/B1-96[»]
1T2HX-ray1.00A/B1-96[»]
1T2IX-ray1.10A1-96[»]
1UCIX-ray1.80A/B1-96[»]
1UCJX-ray1.81A/B1-96[»]
1UCKX-ray1.80A/B1-96[»]
1UCLX-ray1.82A/B1-96[»]
1YNVX-ray1.20X1-96[»]
1ZGXX-ray1.13A1-63[»]
B64-96[»]
2SARX-ray1.80A/B1-96[»]
3A5EX-ray1.60A1-96[»]
4GHOX-ray1.10A/B1-96[»]
ProteinModelPortalP05798.
SMRP05798. Positions 1-96.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP05798. 1 interaction.
MINTMINT-1539638.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.10.450.30. 1 hit.
InterProIPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamPF00545. Ribonuclease. 1 hit.
[Graphical view]
SUPFAMSSF53933. SSF53933. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP05798.

Entry information

Entry nameRNSA_STRAU
AccessionPrimary (citable) accession number: P05798
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: April 27, 2001
Last modified: April 16, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references