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P51833

- RNC_BACSU

UniProt

P51833 - RNC_BACSU

Protein

Ribonuclease 3

Gene

rnc

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    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

    1. metal ion binding Source: UniProtKB-KW
    2. ribonuclease III activity Source: UniProtKB-HAMAP
    3. RNA binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. mRNA processing Source: UniProtKB-HAMAP
    2. rRNA catabolic process Source: InterPro
    3. rRNA processing Source: UniProtKB-HAMAP
    4. tRNA processing Source: UniProtKB-KW

    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: Chromosome

    Organism-specific databases

    GenoListiBSU15930. [Micado]

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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.BSU15930.

    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.
    KOiK03685.
    OMAiAQKDPKT.
    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]
    PANTHERiPTHR11207. PTHR11207. 1 hit.
    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

    MSKHSHYKDK KKFYKKVEQF KEFQERISVH FQNEKLLYQA FTHSSYVNEH    50
    RKKPYEDNER LEFLGDAVLE LTISRFLFAK YPAMSEGDLT KLRAAIVCEP 100
    SLVSLAHELS FGDLVLLGKG EEMTGGRKRP ALLADVFEAF IGALYLDQGL 150
    EPVESFLKVY VFPKINDGAF SHVMDFKSQL QEYVQRDGKG SLEYKISNEK 200
    GPAHNREFEA IVSLKGEPLG VGNGRSKKEA EQHAAQEALA KLQKHHTKQ 249
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D64116 Genomic DNA. Translation: BAA10976.1.
    AL009126 Genomic DNA. Translation: CAB13466.1.
    PIRiB69693.
    RefSeqiNP_389475.1. NC_000964.3.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D64116 Genomic DNA. Translation: BAA10976.1 .
    AL009126 Genomic DNA. Translation: CAB13466.1 .
    PIRi B69693.
    RefSeqi NP_389475.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P51833.
    SMRi P51833. Positions 17-244.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU15930.

    Proteomic databases

    PaxDbi P51833.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13466 ; CAB13466 ; BSU15930 .
    GeneIDi 936169.
    KEGGi bsu:BSU15930.
    PATRICi 18974991. VBIBacSub10457_1687.

    Organism-specific databases

    GenoListi BSU15930. [Micado ]

    Phylogenomic databases

    eggNOGi COG0571.
    HOGENOMi HOG000246808.
    KOi K03685.
    OMAi AQKDPKT.
    OrthoDBi EOG6T1WVS.
    PhylomeDBi P51833.

    Enzyme and pathway databases

    BioCyci BSUB:BSU15930-MONOMER.

    Family and domain databases

    Gene3Di 1.10.1520.10. 1 hit.
    3.30.160.20. 1 hit.
    HAMAPi MF_00104. RNase_III.
    InterProi IPR014720. dsRNA-bd_dom.
    IPR011907. RNase_III.
    IPR000999. RNase_III_dom.
    [Graphical view ]
    PANTHERi PTHR11207. PTHR11207. 1 hit.
    Pfami PF00035. dsrm. 1 hit.
    PF14622. Ribonucleas_3_3. 1 hit.
    [Graphical view ]
    SMARTi SM00358. DSRM. 1 hit.
    SM00535. RIBOc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69065. SSF69065. 1 hit.
    TIGRFAMsi TIGR02191. RNaseIII. 1 hit.
    PROSITEi PS50137. DS_RBD. 1 hit.
    PS00517. RNASE_3_1. 1 hit.
    PS50142. RNASE_3_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 105 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