Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ribonuclease

Gene
N/A
Organism
Bacillus amyloliquefaciens (Bacillus velezensis)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei120 – 1201Proton acceptor
Active sitei149 – 1491Proton donor

GO - Molecular functioni

  1. endoribonuclease activity Source: InterPro
  2. RNA binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease (EC:3.1.27.-)
Alternative name(s):
Barnase
RNase Ba
OrganismiBacillus amyloliquefaciens (Bacillus velezensis)
Taxonomic identifieri1390 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Biotechnological usei

Introduced by genetic manipulation and expressed in male sterile maize and rape by Plant Genetic Systems and in radicchio rosso by Bejo Zaden. Barnase expressed in transgenic plants will specifically destroy the tissue(s) where it is expressed. After cell transformation, protein expression and plant regeneration, the active nuclease destroys the pollen producing organs thus rendering the plant sterile.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi149 – 1491H → Q: Loss of activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434Add
BLAST
Propeptidei35 – 47131 PublicationPRO_0000030828Add
BLAST
Chaini48 – 157110Ribonuclease1 PublicationPRO_0000030829Add
BLAST

Interactioni

Protein-protein interaction databases

DIPiDIP-544N.
IntActiP00648. 1 interaction.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi54 – 6411Combined sources
Helixi74 – 796Combined sources
Helixi84 – 863Combined sources
Helixi89 – 924Combined sources
Beta strandi97 – 1037Combined sources
Beta strandi118 – 1225Combined sources
Beta strandi127 – 1293Combined sources
Beta strandi134 – 1385Combined sources
Beta strandi143 – 1486Combined sources
Beta strandi154 – 1574Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2PX-ray1.50A/B/C48-157[»]
1B20X-ray1.70A/B/C48-157[»]
1B21X-ray2.00A/B/C48-157[»]
1B27X-ray2.10A/B/C48-157[»]
1B2SX-ray1.82A/B/C48-157[»]
1B2UX-ray2.10A/B/C48-157[»]
1B2XX-ray1.80A/B/C48-157[»]
1B2ZX-ray2.03A/B/C48-157[»]
1B3SX-ray2.39A/B/C48-157[»]
1BANX-ray2.20A/B/C48-157[»]
1BAOX-ray2.20A/B/C48-157[»]
1BGSX-ray2.60A/B/C48-157[»]
1BNEX-ray2.10A/B/C48-157[»]
1BNFX-ray2.00A/B/C48-157[»]
1BNGX-ray2.10A/B/C48-157[»]
1BNIX-ray2.10A/B/C48-157[»]
1BNJX-ray2.10A/B/C48-157[»]
1BNRNMR-A48-157[»]
1BNSX-ray2.05A/B/C48-157[»]
1BRGX-ray2.20A/B/C50-157[»]
1BRHX-ray2.00A/B/C48-157[»]
1BRIX-ray1.90A/B/C48-157[»]
1BRJX-ray2.00A/B/C48-157[»]
1BRKX-ray2.00A/B/C48-157[»]
1BRNX-ray1.76L/M48-157[»]
1BRSX-ray2.00A/B/C48-157[»]
1BSAX-ray2.00A/B/C48-157[»]
1BSBX-ray2.00A/B/C48-157[»]
1BSCX-ray2.00A/B/C48-157[»]
1BSDX-ray2.30A/B/C48-157[»]
1BSEX-ray2.00A/B/C48-157[»]
1FW7NMR-A48-157[»]
1RNBX-ray1.90A48-157[»]
1X1UX-ray2.30A/B/C48-157[»]
1X1WX-ray2.10A/B/C48-157[»]
1X1XX-ray2.30A/B/C48-157[»]
1X1YX-ray1.90A/B/C48-157[»]
1YVSX-ray2.20A48-157[»]
2C4BX-ray1.30A/B49-157[»]
2F4YX-ray2.15A/B/C50-157[»]
2F56X-ray1.96A/B/C50-157[»]
2F5MX-ray1.95A/B/C50-157[»]
2F5WX-ray2.00A/B/C50-157[»]
2KF3NMR-A48-157[»]
2KF4NMR-A48-157[»]
2KF5NMR-A48-157[»]
2KF6NMR-A48-157[»]
2ZA4X-ray1.58A/C48-157[»]
3DA7X-ray2.25A/B/E/G48-113[»]
3KCHX-ray1.94A/B/C48-157[»]
3Q3FX-ray2.17A48-157[»]
ProteinModelPortaliP00648.
SMRiP00648. Positions 48-157.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00648.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribonuclease N1/T1 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.10.450.30. 1 hit.
InterProiIPR001887. Barnase.
IPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamiPF00545. Ribonuclease. 1 hit.
[Graphical view]
PIRSFiPIRSF001013. Barnase. 1 hit.
PRINTSiPR00117. BARNASE.
SUPFAMiSSF53933. SSF53933. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00648-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMKMEGIALK KRLSWISVCL LVLVSAAGML FSTAAKTETS SHKAHTEAQV
60 70 80 90 100
INTFDGVADY LQTYHKLPDN YITKSEAQAL GWVASKGNLA DVAPGKSIGG
110 120 130 140 150
DIFSNREGKL PGKSGRTWRE ADINYTSGFR NSDRILYSSD WLIYKTTDHY

QTFTKIR
Length:157
Mass (Da):17,473
Last modified:July 1, 1989 - v2
Checksum:i42B6669F9B0D7FBA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14442 Genomic DNA. Translation: AAA86441.1.
X12871 Genomic DNA. Translation: CAA31365.1.
PIRiA24038. NRBSN.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14442 Genomic DNA. Translation: AAA86441.1.
X12871 Genomic DNA. Translation: CAA31365.1.
PIRiA24038. NRBSN.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2PX-ray1.50A/B/C48-157[»]
1B20X-ray1.70A/B/C48-157[»]
1B21X-ray2.00A/B/C48-157[»]
1B27X-ray2.10A/B/C48-157[»]
1B2SX-ray1.82A/B/C48-157[»]
1B2UX-ray2.10A/B/C48-157[»]
1B2XX-ray1.80A/B/C48-157[»]
1B2ZX-ray2.03A/B/C48-157[»]
1B3SX-ray2.39A/B/C48-157[»]
1BANX-ray2.20A/B/C48-157[»]
1BAOX-ray2.20A/B/C48-157[»]
1BGSX-ray2.60A/B/C48-157[»]
1BNEX-ray2.10A/B/C48-157[»]
1BNFX-ray2.00A/B/C48-157[»]
1BNGX-ray2.10A/B/C48-157[»]
1BNIX-ray2.10A/B/C48-157[»]
1BNJX-ray2.10A/B/C48-157[»]
1BNRNMR-A48-157[»]
1BNSX-ray2.05A/B/C48-157[»]
1BRGX-ray2.20A/B/C50-157[»]
1BRHX-ray2.00A/B/C48-157[»]
1BRIX-ray1.90A/B/C48-157[»]
1BRJX-ray2.00A/B/C48-157[»]
1BRKX-ray2.00A/B/C48-157[»]
1BRNX-ray1.76L/M48-157[»]
1BRSX-ray2.00A/B/C48-157[»]
1BSAX-ray2.00A/B/C48-157[»]
1BSBX-ray2.00A/B/C48-157[»]
1BSCX-ray2.00A/B/C48-157[»]
1BSDX-ray2.30A/B/C48-157[»]
1BSEX-ray2.00A/B/C48-157[»]
1FW7NMR-A48-157[»]
1RNBX-ray1.90A48-157[»]
1X1UX-ray2.30A/B/C48-157[»]
1X1WX-ray2.10A/B/C48-157[»]
1X1XX-ray2.30A/B/C48-157[»]
1X1YX-ray1.90A/B/C48-157[»]
1YVSX-ray2.20A48-157[»]
2C4BX-ray1.30A/B49-157[»]
2F4YX-ray2.15A/B/C50-157[»]
2F56X-ray1.96A/B/C50-157[»]
2F5MX-ray1.95A/B/C50-157[»]
2F5WX-ray2.00A/B/C50-157[»]
2KF3NMR-A48-157[»]
2KF4NMR-A48-157[»]
2KF5NMR-A48-157[»]
2KF6NMR-A48-157[»]
2ZA4X-ray1.58A/C48-157[»]
3DA7X-ray2.25A/B/E/G48-113[»]
3KCHX-ray1.94A/B/C48-157[»]
3Q3FX-ray2.17A48-157[»]
ProteinModelPortaliP00648.
SMRiP00648. Positions 48-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-544N.
IntActiP00648. 1 interaction.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00648.

Family and domain databases

Gene3Di3.10.450.30. 1 hit.
InterProiIPR001887. Barnase.
IPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamiPF00545. Ribonuclease. 1 hit.
[Graphical view]
PIRSFiPIRSF001013. Barnase. 1 hit.
PRINTSiPR00117. BARNASE.
SUPFAMiSSF53933. SSF53933. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequencing and transcription of an inactivated copy of Bacillus amyloliquefaciens extracellular ribonuclease (barnase)."
    Paddon C.J., Hartley R.W.
    Gene 40:231-239(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Barnase and barstar. Expression of its cloned inhibitor permits expression of a cloned ribonuclease."
    Hartley R.W.
    J. Mol. Biol. 202:913-915(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-157.
  3. "Amino-acid sequence of extracellular ribonuclease (barnase) of Bacillus amyloliquefaciens."
    Hartley R.W., Barker E.A.
    Nature New Biol. 235:15-16(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 48-157.
  4. "Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy."
    Bycroft M., Ludvigsen S., Fersht A.R., Poulsen F.M.
    Biochemistry 30:8697-8701(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  5. "An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate."
    Sancho J., Neira J.L., Fersht A.R.
    J. Mol. Biol. 224:749-758(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 48-83.
  6. Cited for: STRUCTURE BY NMR OF 48-157.
  7. "Crystal structure of a barnase-d(GpC) complex at 1.9-A resolution."
    Baudet S., Janin J.
    J. Mol. Biol. 219:123-132(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  8. "Recognition between a bacterial ribonuclease, barnase, and its natural inhibitor, barstar."
    Guillet V., Lapthorn A., Hartley R.W., Mauguen Y.
    Structure 1:165-177(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH BARNASE.
  9. "A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase."
    Vaughan C.K., Harryson P., Buckle A.M., Fersht A.R.
    Acta Crystallogr. D 58:591-600(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  10. "Barnase and barstar: two small proteins to fold and fit together."
    Hartley R.W.
    Trends Biochem. Sci. 14:450-454(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiRNBR_BACAM
AccessioniPrimary (citable) accession number: P00648
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: February 4, 2015
This is version 110 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, Genetically modified food

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.