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P51833 (RNC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. 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 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 (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Digests double-stranded RNA. Involved in the processing of ribosomal RNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Also processes pre-scRNA (the precursor of the signal recognition particle RNA). Probably also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Ref.3 Ref.4

Catalytic activity

Endonucleolytic cleavage to 5'-phosphomonoester. HAMAP-Rule MF_00104

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00104

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00104.

Disruption phenotype

Essential. Depletion leads to the accumulation of 30S precursor rRNA. Ref.3 Ref.4

Sequence similarities

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

Contains 1 RNase III domain.

Ontologies

Keywords
   Biological processmRNA processing
rRNA processing
tRNA processing
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
RNA-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmRNA processing

Inferred from electronic annotation. Source: UniProtKB-HAMAP

rRNA catabolic process

Inferred from electronic annotation. Source: InterPro

rRNA processing

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribonuclease III activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 249249Ribonuclease 3 HAMAP-Rule MF_00104
PRO_0000180375

Regions

Domain20 – 149130RNase III
Domain175 – 24470DRBM

Sites

Active site661 By similarity
Active site1381 By similarity
Metal binding621Magnesium By similarity
Metal binding1351Magnesium By similarity
Metal binding1381Magnesium By similarity

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

Sequences

Sequence LengthMass (Da)Tools
P51833 [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

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Endoribonuclease RNase III is essential in Bacillus subtilis."
Herskovitz M.A., Bechhofer D.H.
Mol. Microbiol. 38:1027-1033(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RRNA PRECURSOR PROCESSING, FUNCTION IN PRE-SCRNA PROCESSING, FUNCTION AS AN RNASE, DISRUPTION PHENOTYPE.
[4]"Mini-III, an unusual member of the RNase III family of enzymes, catalyses 23S ribosomal RNA maturation in B. subtilis."
Redko Y., Bechhofer D.H., Condon C.
Mol. Microbiol. 68:1096-1106(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RRNA PRECURSOR PROCESSING, RNASE ACTIVITY, DISRUPTION PHENOTYPE.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D64116 Genomic DNA. Translation: BAA10976.1.
AL009126 Genomic DNA. Translation: CAB13466.1.
PIRB69693.
RefSeqNP_389475.1. NC_000964.3.

3D structure databases

ProteinModelPortalP51833.
SMRP51833. Positions 17-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU15930.

Proteomic databases

PaxDbP51833.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13466; CAB13466; BSU15930.
GeneID936169.
KEGGbsu:BSU15930.
PATRIC18974991. VBIBacSub10457_1687.

Organism-specific databases

GenoListBSU15930. [Micado]

Phylogenomic databases

eggNOGCOG0571.
HOGENOMHOG000246808.
KOK03685.
OMALTHKSCK.
OrthoDBEOG6T1WVS.
ProtClustDBPRK00102.

Enzyme and pathway databases

BioCycBSUB:BSU15930-MONOMER.

Family and domain databases

Gene3D1.10.1520.10. 1 hit.
3.30.160.20. 1 hit.
HAMAPMF_00104. RNase_III.
InterProIPR014720. dsRNA-bd_dom.
IPR011907. RNase_III.
IPR000999. RNase_III_dom.
[Graphical view]
PANTHERPTHR11207. PTHR11207. 1 hit.
PfamPF00035. dsrm. 1 hit.
PF14622. Ribonucleas_3_3. 1 hit.
[Graphical view]
SMARTSM00358. DSRM. 1 hit.
SM00535. RIBOc. 1 hit.
[Graphical view]
SUPFAMSSF69065. SSF69065. 1 hit.
TIGRFAMsTIGR02191. RNaseIII. 1 hit.
PROSITEPS50137. DS_RBD. 1 hit.
PS00517. RNASE_3_1. 1 hit.
PS50142. RNASE_3_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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: April 16, 2014
This is version 101 of the entry and version 2 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

Bacillus subtilis

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