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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)DescriptionActionsGraphical viewLength
Active sitei120Proton acceptor1
Active sitei149Proton donor1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Enzyme and pathway databases

BRENDAi3.1.27.3. 630.

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

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)DescriptionActionsGraphical viewLength
Mutagenesisi149H → Q: Loss of activity. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 34Add BLAST34
PropeptideiPRO_000003082835 – 471 PublicationAdd BLAST13
ChainiPRO_000003082948 – 157Ribonuclease1 PublicationAdd BLAST110

Interactioni

Protein-protein interaction databases

DIPiDIP-544N.
IntActiP00648. 1 interactor.
STRINGi326423.RBAM_031940.

Structurei

Secondary structure

1157
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi54 – 64Combined sources11
Helixi74 – 79Combined sources6
Helixi84 – 86Combined sources3
Helixi89 – 92Combined sources4
Beta strandi97 – 103Combined sources7
Beta strandi118 – 122Combined sources5
Beta strandi127 – 129Combined sources3
Beta strandi134 – 138Combined sources5
Beta strandi143 – 148Combined sources6
Beta strandi154 – 157Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00648.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribonuclease N1/T1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105GGE. Bacteria.
ENOG4111TSC. LUCA.

Family and domain databases

Gene3Di3.10.450.30. 1 hit.
InterProiIPR001887. Barnase.
IPR000026. Gua-sp_ribonuclease_N1/T1/U2.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-544N.
IntActiP00648. 1 interactor.
STRINGi326423.RBAM_031940.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105GGE. Bacteria.
ENOG4111TSC. LUCA.

Enzyme and pathway databases

BRENDAi3.1.27.3. 630.

Miscellaneous databases

EvolutionaryTraceiP00648.

Family and domain databases

Gene3Di3.10.450.30. 1 hit.
InterProiIPR001887. Barnase.
IPR000026. Gua-sp_ribonuclease_N1/T1/U2.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamiPF00545. Ribonuclease. 1 hit.
[Graphical view]
PIRSFiPIRSF001013. Barnase. 1 hit.
PRINTSiPR00117. BARNASE.
SUPFAMiSSF53933. SSF53933. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 120 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

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.