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Q8TZS0

- RNP3_PYRFU

UniProt

Q8TZS0 - RNP3_PYRFU

Protein

Ribonuclease P protein component 3

Gene

rnp3

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. The RNA is catalytic, but its KM for pre-tRNA is 170-fold decreased in the presence of the 4 known protein subunits (Rnp1-4). The protein subunits also decrease the amount of Mg2+ needed for activity.3 PublicationsUniRule annotation

    Catalytic activityi

    Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.1 PublicationUniRule annotation

    Kineticsi

    kcat is 9.5 min(-1). For enzyme reconstituted with RNA and 4 known subunits (Rnp1-4).

    1. KM=0.18 µM for E.coli pre-tRNA(Tyr)1 Publication

    GO - Molecular functioni

    1. ribonuclease P activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. tRNA 5'-leader removal Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    tRNA processing

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonuclease P protein component 3UniRule annotation (EC:3.1.26.5UniRule annotation)
    Short name:
    RNase P component 3UniRule annotation
    Alternative name(s):
    Rpp30UniRule annotation
    Gene namesi
    Name:rnp3UniRule annotation
    Ordered Locus Names:PF1914
    OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
    Taxonomic identifieri186497 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    ProteomesiUP000001013: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. ribonuclease P complex Source: UniProtKB-HAMAP

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 214214Ribonuclease P protein component 3PRO_0000140045Add
    BLAST

    Proteomic databases

    PRIDEiQ8TZS0.

    Interactioni

    Subunit structurei

    Consists of a catalytic RNA component and at least 4-5 protein subunits. Forms a subcomplex with Rnp2 which stimulates the catalytic RNA.3 PublicationsUniRule annotation

    Protein-protein interaction databases

    IntActiQ8TZS0. 1 interaction.
    STRINGi186497.PF1914.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8TZS0.
    SMRiQ8TZS0. Positions 7-214.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the eukaryotic/archaeal RNase P protein component 3 family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1603.
    HOGENOMiHOG000073988.
    KOiK03539.
    OMAiDALISPW.

    Family and domain databases

    HAMAPiMF_00756. RNase_P_3.
    InterProiIPR016195. Pol/histidinol_Pase-like.
    IPR023539. RNase_P_comp-3_arc.
    IPR002738. RNase_P_p30.
    [Graphical view]
    PfamiPF01876. RNase_P_p30. 1 hit.
    [Graphical view]
    SUPFAMiSSF89550. SSF89550. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8TZS0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGGRNGVKF VEMDIRSREA YELAEEWFDD VVFSYEIPPG VLDKERLKEI    50
    KKEYGNVAIT LINPKPSLVK EAVQRFKQNY LIYVESSDLR VVRYSIERGV 100
    DAVISPWANR KDQGIDHVLA RMMNKRGVAL GFSLRPLLHQ NPYERANALK 150
    FMRKAWTLVN KYKVPRFISS SAKGKFQVRG VKELISLGIA IGMEEVQAKA 200
    SLSFYPLGIL ERLK 214
    Length:214
    Mass (Da):24,495
    Last modified:June 1, 2002 - v1
    Checksum:iA915506635C02CFB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE009950 Genomic DNA. Translation: AAL82038.1.
    RefSeqiNP_579643.1. NC_003413.1.
    WP_011013054.1. NC_003413.1.

    Genome annotation databases

    EnsemblBacteriaiAAL82038; AAL82038; PF1914.
    GeneIDi1469794.
    KEGGipfu:PF1914.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE009950 Genomic DNA. Translation: AAL82038.1 .
    RefSeqi NP_579643.1. NC_003413.1.
    WP_011013054.1. NC_003413.1.

    3D structure databases

    ProteinModelPortali Q8TZS0.
    SMRi Q8TZS0. Positions 7-214.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8TZS0. 1 interaction.
    STRINGi 186497.PF1914.

    Proteomic databases

    PRIDEi Q8TZS0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL82038 ; AAL82038 ; PF1914 .
    GeneIDi 1469794.
    KEGGi pfu:PF1914.

    Phylogenomic databases

    eggNOGi COG1603.
    HOGENOMi HOG000073988.
    KOi K03539.
    OMAi DALISPW.

    Family and domain databases

    HAMAPi MF_00756. RNase_P_3.
    InterProi IPR016195. Pol/histidinol_Pase-like.
    IPR023539. RNase_P_comp-3_arc.
    IPR002738. RNase_P_p30.
    [Graphical view ]
    Pfami PF01876. RNase_P_p30. 1 hit.
    [Graphical view ]
    SUPFAMi SSF89550. SSF89550. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
      Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
      Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    2. Cited for: INTERACTION WITH RNP2.
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    3. "Functional reconstitution and characterization of Pyrococcus furiosus RNase P."
      Tsai H.Y., Pulukkunat D.K., Woznick W.K., Gopalan V.
      Proc. Natl. Acad. Sci. U.S.A. 103:16147-16152(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    4. "Cooperative RNP assembly: complementary rescue of structural defects by protein and RNA subunits of archaeal RNase P."
      Chen W.Y., Xu Y., Cho I.M., Oruganti S.V., Foster M.P., Gopalan V.
      J. Mol. Biol. 411:368-383(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    5. "Fidelity of tRNA 5'-maturation: a possible basis for the functional dependence of archaeal and eukaryal RNase P on multiple protein cofactors."
      Chen W.Y., Singh D., Lai L.B., Stiffler M.A., Lai H.D., Foster M.P., Gopalan V.
      Nucleic Acids Res. 40:4666-4680(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RNP2, SUBUNIT.

    Entry informationi

    Entry nameiRNP3_PYRFU
    AccessioniPrimary (citable) accession number: Q8TZS0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 63 of the entry and version 1 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3