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Protein

Ribonuclease 3

Gene

rnc

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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. Probably processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.4 Publications

Catalytic activityi

Endonucleolytic cleavage to 5'-phosphomonoester.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi62 – 621MagnesiumBy similarity
Active sitei66 – 661By similarity
Metal bindingi135 – 1351MagnesiumBy similarity
Active sitei138 – 1381By similarity
Metal bindingi138 – 1381MagnesiumBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

mRNA processing, rRNA processing, tRNA processing

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Enzyme and pathway databases

BioCyciBSUB:BSU15930-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease 3 (EC:3.1.26.3)
Alternative name(s):
Ribonuclease III
Short name:
RNase III
Gene namesi
Name:rnc
Synonyms:rncS
Ordered Locus Names:BSU15930
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU15930. [Micado]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Essential. Depletion leads to the accumulation of 30S precursor rRNA (PubMed:11123676), and alteration of levels of about 11% of total transcripts (PubMed:22412379).3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249Ribonuclease 3PRO_0000180375Add
BLAST

Proteomic databases

PaxDbiP51833.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100008786.

Structurei

3D structure databases

ProteinModelPortaliP51833.
SMRiP51833. Positions 17-244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 149130RNase IIIAdd
BLAST
Domaini175 – 24470DRBMAdd
BLAST

Sequence similaritiesi

Contains 1 RNase III domain.Curated

Phylogenomic databases

eggNOGiCOG0571.
HOGENOMiHOG000246808.
InParanoidiP51833.
KOiK03685.
OMAiNSYANER.
OrthoDBiEOG6T1WVS.
PhylomeDBiP51833.

Family and domain databases

Gene3Di1.10.1520.10. 1 hit.
3.30.160.20. 1 hit.
HAMAPiMF_00104. RNase_III.
InterProiIPR014720. dsRNA-bd_dom.
IPR011907. RNase_III.
IPR000999. RNase_III_dom.
[Graphical view]
PfamiPF00035. dsrm. 1 hit.
PF14622. Ribonucleas_3_3. 1 hit.
[Graphical view]
SMARTiSM00358. DSRM. 1 hit.
SM00535. RIBOc. 1 hit.
[Graphical view]
SUPFAMiSSF69065. SSF69065. 1 hit.
TIGRFAMsiTIGR02191. RNaseIII. 1 hit.
PROSITEiPS50137. DS_RBD. 1 hit.
PS00517. RNASE_3_1. 1 hit.
PS50142. RNASE_3_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51833-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKHSHYKDK KKFYKKVEQF KEFQERISVH FQNEKLLYQA FTHSSYVNEH
60 70 80 90 100
RKKPYEDNER LEFLGDAVLE LTISRFLFAK YPAMSEGDLT KLRAAIVCEP
110 120 130 140 150
SLVSLAHELS FGDLVLLGKG EEMTGGRKRP ALLADVFEAF IGALYLDQGL
160 170 180 190 200
EPVESFLKVY VFPKINDGAF SHVMDFKSQL QEYVQRDGKG SLEYKISNEK
210 220 230 240
GPAHNREFEA IVSLKGEPLG VGNGRSKKEA EQHAAQEALA KLQKHHTKQ
Length:249
Mass (Da):28,425
Last modified:May 30, 2000 - v2
Checksum:i304F3B0BF5B7CCDC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791A → P in BAA10976 (PubMed:8654983).Curated
Sequence conflicti171 – 1711S → P in BAA10976 (PubMed:8654983).Curated
Sequence conflicti243 – 2431Q → E in BAA10976 (PubMed:8654983).Curated
Sequence conflicti249 – 2491Q → QLNPPYDSGGFQYVCRLI in BAA10976 (PubMed:8654983).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D64116 Genomic DNA. Translation: BAA10976.1.
AL009126 Genomic DNA. Translation: CAB13466.1.
PIRiB69693.
RefSeqiNP_389475.1. NC_000964.3.
WP_003232030.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13466; CAB13466; BSU15930.
GeneIDi936169.
KEGGibsu:BSU15930.
PATRICi18974991. VBIBacSub10457_1687.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D64116 Genomic DNA. Translation: BAA10976.1.
AL009126 Genomic DNA. Translation: CAB13466.1.
PIRiB69693.
RefSeqiNP_389475.1. NC_000964.3.
WP_003232030.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliP51833.
SMRiP51833. Positions 17-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100008786.

Proteomic databases

PaxDbiP51833.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13466; CAB13466; BSU15930.
GeneIDi936169.
KEGGibsu:BSU15930.
PATRICi18974991. VBIBacSub10457_1687.

Organism-specific databases

GenoListiBSU15930. [Micado]

Phylogenomic databases

eggNOGiCOG0571.
HOGENOMiHOG000246808.
InParanoidiP51833.
KOiK03685.
OMAiNSYANER.
OrthoDBiEOG6T1WVS.
PhylomeDBiP51833.

Enzyme and pathway databases

BioCyciBSUB:BSU15930-MONOMER.

Family and domain databases

Gene3Di1.10.1520.10. 1 hit.
3.30.160.20. 1 hit.
HAMAPiMF_00104. RNase_III.
InterProiIPR014720. dsRNA-bd_dom.
IPR011907. RNase_III.
IPR000999. RNase_III_dom.
[Graphical view]
PfamiPF00035. dsrm. 1 hit.
PF14622. Ribonucleas_3_3. 1 hit.
[Graphical view]
SMARTiSM00358. DSRM. 1 hit.
SM00535. RIBOc. 1 hit.
[Graphical view]
SUPFAMiSSF69065. SSF69065. 1 hit.
TIGRFAMsiTIGR02191. RNaseIII. 1 hit.
PROSITEiPS50137. DS_RBD. 1 hit.
PS00517. RNASE_3_1. 1 hit.
PS50142. RNASE_3_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. "Processing of Bacillus subtilis small cytoplasmic RNA: evidence for an additional endonuclease cleavage site."
    Yao S., Blaustein J.B., Bechhofer D.H.
    Nucleic Acids Res. 35:4464-4473(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "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.
  6. "Three essential ribonucleases-RNase Y, J1, and III-control the abundance of a majority of Bacillus subtilis mRNAs."
    Durand S., Gilet L., Bessieres P., Nicolas P., Condon C.
    PLoS Genet. 8:E1002520-E1002520(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: 168.

Entry informationi

Entry nameiRNC_BACSU
AccessioniPrimary (citable) accession number: P51833
Secondary accession number(s): O31734
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2000
Last modified: June 24, 2015
This is version 109 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

Complete proteome, Reference proteome

Documents

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