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P00649 (RN_BACIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease

EC=3.1.27.-
Alternative name(s):
Binase
RNase Bi
OrganismBacillus intermedius
Taxonomic identifier1400 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length162 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is a purine-specific ribonuclease.

Subcellular location

Secreted.

Sequence similarities

Belongs to the ribonuclease N1/T1 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionEndonuclease
Hydrolase
Nuclease
   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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Propeptide30 – 5324
PRO_0000030824
Chain54 – 162109Ribonuclease
PRO_0000030825

Sites

Active site1251Proton acceptor
Active site1541Proton donor

Experimental info

Sequence conflict74 – 752DN → ND AA sequence Ref.3
Sequence conflict931N → D AA sequence Ref.3
Sequence conflict119 – 1202SG → GS AA sequence Ref.3

Secondary structure

........................ 162
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00649 [UniParc].

Last modified May 1, 1992. Version 3.
Checksum: CD6740EDFBCF5295

FASTA16217,956
        10         20         30         40         50         60 
MKKISSVFTM FALIAAILFS GFIPQQAYAE TPLTQTATNE TATIQLTSDV HTLAVINTFD 

        70         80         90        100        110        120 
GVADYLIRYK RLPDNYITKS QASALGWVAS KGNLAEVAPG KSIGGDVFSN REGRLPSASG 

       130        140        150        160 
RTWREADINY VSGFRNADRL VYSSDWLIYK TTDHYATFTR IR 

« Hide

References

[1]"Cloning of the gene encoding RNase binase from Bacillus intermedius 7P."
Schulga A.A., Nurkiyanova K.M., Zakharyev V.M., Kirpichnikov M.P., Skryabin K.G.
Nucleic Acids Res. 20:2375-2375(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 7P.
[2]"The cloning and determination of the nucleotide sequence of the RNase gene in Bacillus intermedius."
Nurkiyanova K.M., Shulga A.A., Zakharyev V.M., Kirpichnikov M.P., Skryabin K.G., Baev A.A.
Dokl. Akad. Nauk SSSR 309:1476-1479(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 7P.
[3]"Primary structure of ribonuclease from Bacillus intermedius 7P."
Aphanasenko G.A., Dudkin S.M., Kaminir L.B., Leshchinskaya I.B., Severin E.S.
FEBS Lett. 97:77-80(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 54-162.
Strain: 7P.
[4]"RNA cleavage without hydrolysis. Splitting the catalytic activities of binase with Asn101 and Thr101 mutations."
Okorokov A.L., Panov K.I., Offen W.A., Mukhortov V.G., Antson A.A., Karpeisky M.Y., Wilkinson A.J., Dodson G.G.
Protein Eng. 10:273-278(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) AND MUTAGENESIS OF HIS-154.
[5]"Three-dimensional structure of binase in solution."
Reibarkh M.Y.A., Nolde D.E., Vasilieva L.I., Bocharov E.V., Shulga A.A., Kirpichnikov M.P., Arseniev A.S.
FEBS Lett. 431:250-254(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[6]"The structure of substrate-free microbial ribonuclease binase and of its complexes with 3'GMP and sulfate ions."
Polyakov K.M., Lebedev A.A., Okorokov A.L., Panov K.I., Schulga A.A., Pavlovsky A.G., Karpeisky M.Y., Dodson G.G.
Acta Crystallogr. D 58:744-750(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 54-162.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53697 Genomic DNA. Translation: CAA37735.1.
PIRNRBSI. A00796.
S22653.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BUJNMR-A54-162[»]
1GOUX-ray1.65A/B54-162[»]
1GOVX-ray2.00A/B54-162[»]
1GOYX-ray2.00A/B54-162[»]
2RBIX-ray2.20A/B54-162[»]
4HAAX-ray1.90A/B/C/D54-162[»]
ProteinModelPortalP00649.
SMRP00649. Positions 54-162.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.10.450.30. 1 hit.
InterProIPR001887. Barnase.
IPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamPF00545. Ribonuclease. 1 hit.
[Graphical view]
PIRSFPIRSF001013. Barnase. 1 hit.
PRINTSPR00117. BARNASE.
SUPFAMSSF53933. SSF53933. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP00649.

Entry information

Entry nameRN_BACIN
AccessionPrimary (citable) accession number: P00649
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 1, 1992
Last modified: April 16, 2014
This is version 96 of the entry and version 3 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