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Reviewed, UniProtKB/Swiss-Prot P51833 (RNC_BACSU)

Last modified November 3, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Ribonuclease 3
    EC=3.1.26.3
Alternative name(s):
    Ribonuclease III
      Short name=RNase III
Gene names
Name: rnc
Synonyms: rncS
Ordered Locus Names: BSU15930
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Digests double-stranded RNA. Involved in the processing of ribosomal RNA precursors and of some mRNAs By similarity.

Catalytic activity

Endonucleolytic cleavage to 5'-phosphomonoester. HAMAP MF_00104

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Contains 1 DRBM (double-stranded RNA-binding) domain.

Contains 1 RNase III domain.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandRNA-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processmRNA processing

Inferred from electronic annotation. Source: HAMAP

rRNA catabolic process

Inferred from electronic annotation. Source: InterPro

rRNA processing

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondouble-stranded RNA binding

Inferred from electronic annotation. Source: InterPro

ribonuclease III activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 249249Ribonuclease 3 HAMAP MF_00104
PRO_0000180375

Regions

Domain20 – 149130RNase III
Domain175 – 24470DRBM

Experimental info

Sequence conflict791A → P in BAA10976. Ref.1
Sequence conflict1711S → P in BAA10976. Ref.1
Sequence conflict2431Q → E in BAA10976. Ref.1
Sequence conflict2491Q → QLNPPYDSGGFQYVCRLI in BAA10976. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P51833-1 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 304F3B0BF5B7CCDC

FASTA24928,425
        10         20         30         40         50         60 
MSKHSHYKDK KKFYKKVEQF KEFQERISVH FQNEKLLYQA FTHSSYVNEH RKKPYEDNER 

        70         80         90        100        110        120 
LEFLGDAVLE LTISRFLFAK YPAMSEGDLT KLRAAIVCEP SLVSLAHELS FGDLVLLGKG 

       130        140        150        160        170        180 
EEMTGGRKRP ALLADVFEAF IGALYLDQGL EPVESFLKVY VFPKINDGAF SHVMDFKSQL 

       190        200        210        220        230        240 
QEYVQRDGKG SLEYKISNEK GPAHNREFEA IVSLKGEPLG VGNGRSKKEA EQHAAQEALA 


KLQKHHTKQ

« Hide

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References

« Hide 'large scale' references
[1]"The effect of Srb, a homologue of the mammalian SRP receptor alpha-subunit, on Bacillus subtilis growth and protein translocation."
Oguro A., Kakeshita H., Takamatsu H., Nakamura K., Yamane K.
Gene 172:17-24(1996) [PubMed: 8654983] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

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Cross-references

Sequence databases

D64116 Genomic DNA. Translation: BAA10976.1.
AL009126 Genomic DNA. Translation: CAB13466.1.
PIRB69693.
RefSeqNP_389475.1.

3D structure databases

HSSPHSSP built from PDB template 1O0W based on UniProtKB Q9X0I6.
ModBaseSearch...

Genome annotation databases

GeneID936169.
GenomeReviewsGene locus BSU15930 in contig AL009126_GR.
KEGGbsu:BSU15930.
NMPDRfig|224308.1.peg.1595.

Organism-specific databases

SubtiListBG11537. rnc. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP51833.
OMAALTHKSF.

Enzyme and pathway databases

BioCycBSUB224308:BSU1594-MON.
BRENDA3.1.26.3. 150.

Family and domain databases

HAMAPMF_00104.
[Tree]
InterProIPR001159. Ds-RNA_bd.
IPR014720. dsRNA-bd-like.
IPR000999. RNase_III.
IPR011907. RNase_III_bac.
[Graphical view]
Gene3DG3DSA:3.30.160.20. dsRNA-bd-like. 1 hit.
G3DSA:1.10.1520.10. RNase_III. 1 hit.
PfamPF00035. dsrm. 1 hit.
PF00636. Ribonuclease_3. 1 hit.
[Graphical view]
SMARTSM00358. DSRM. 1 hit.
SM00535. RIBOc. 1 hit.
[Graphical view]
TIGRFAMsTIGR02191. RNaseIII. 1 hit.
PROSITEPS50137. DS_RBD. 1 hit.
PS00517. RNASE_3_1. 1 hit.
PS50142. RNASE_3_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameRNC_BACSU
AccessionPrimary (citable) accession number: P51833
Secondary accession number(s): O31734
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2000
Last modified: November 3, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents