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Protein

Guanyl-specific ribonuclease Sa

Gene

rnaSA

Organism
Streptomyces aureofaciens
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 sitei54 – 541Proton acceptor
Active sitei85 – 851Proton 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

Enzyme and pathway databases

BRENDAi3.1.27.3. 5978.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanyl-specific ribonuclease Sa (EC:3.1.27.3)
Short name:
RNase Sa
Gene namesi
Name:rnaSA
OrganismiStreptomyces aureofaciens
Taxonomic identifieri1894 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391N → A, D or S: Decreases protein stability.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9696Guanyl-specific ribonuclease SaPRO_0000137367Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi7 ↔ 96

Keywords - PTMi

Disulfide bond

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
P115401EBI-1027193,EBI-1027188From a different organism.

Protein-protein interaction databases

IntActiP05798. 1 interaction.
MINTiMINT-1539638.

Structurei

Secondary structure

1
96
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Helixi8 – 103Combined sources
Helixi13 – 2311Combined sources
Turni31 – 344Combined sources
Beta strandi35 – 373Combined sources
Beta strandi42 – 443Combined sources
Beta strandi48 – 503Combined sources
Beta strandi51 – 566Combined sources
Beta strandi63 – 653Combined sources
Beta strandi69 – 757Combined sources
Beta strandi79 – 846Combined sources
Beta strandi90 – 934Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4J5GX-ray1.31A/B1-94[»]
4J5KX-ray1.23A/B1-96[»]
SMRiP05798. Positions 1-96.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05798.

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.

P05798-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
DVSGTVCLSA LPPEATDTLN LIASDGPFPY SQDGVVFQNR ESVLPTQSYG
60 70 80 90
YYHEYTVITP GARTRGTRRI ITGEATQEDY YTGDHYATFS LIDQTC
Length:96
Mass (Da):10,576
Last modified:April 27, 2001 - v2
Checksum:iFA4DB2FD0BA8A7E4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721T → C AA sequence (PubMed:3098582).Curated
Sequence conflicti72 – 721T → C AA sequence (PubMed:3118883).Curated

Sequence databases

PIRiA25655. NRSM.

Cross-referencesi

Sequence databases

PIRiA25655. NRSM.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4J5GX-ray1.31A/B1-94[»]
4J5KX-ray1.23A/B1-96[»]
SMRiP05798. Positions 1-96.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP05798. 1 interaction.
MINTiMINT-1539638.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.27.3. 5978.

Miscellaneous databases

EvolutionaryTraceiP05798.

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. "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(1985) [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(1986) [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(1990) [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(1992) [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(1992) [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(1995) [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(1997) [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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) AND MUTAGENESIS OF ASN-39.
  9. Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiRNSA_STRAU
AccessioniPrimary (citable) accession number: P05798
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: April 27, 2001
Last modified: April 1, 2015
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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.