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Protein

Ribonuclease P protein component 2

Gene

rnp2

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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.UniRule annotation3 Publications

Catalytic activityi

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.UniRule annotation1 Publication

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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    tRNA processing

    Enzyme and pathway databases

    BRENDAi3.1.26.5. 5243.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonuclease P protein component 2UniRule annotation (EC:3.1.26.5UniRule annotation)
    Short name:
    RNase P component 2UniRule annotation
    Alternative name(s):
    Pop5UniRule annotation
    Gene namesi
    Name:rnp2UniRule annotation
    Ordered Locus Names:PF1378
    OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
    Taxonomic identifieri186497 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    ProteomesiUP000001013 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 120120Ribonuclease P protein component 2PRO_0000140026Add
    BLAST

    Proteomic databases

    PRIDEiQ8U151.

    Interactioni

    Subunit structurei

    Consists of a catalytic RNA component and at least 4-5 protein subunits. Forms a subcomplex with Rnp3 which stimulates the catalytic RNA.UniRule annotation4 Publications

    Protein-protein interaction databases

    IntActiQ8U151. 1 interaction.
    STRINGi186497.PF1378.

    Structurei

    Secondary structure

    1
    120
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 2712Combined sources
    Helixi31 – 5424Combined sources
    Beta strandi57 – 626Combined sources
    Turni63 – 664Combined sources
    Beta strandi67 – 737Combined sources
    Helixi74 – 763Combined sources
    Helixi77 – 859Combined sources
    Beta strandi93 – 10513Combined sources
    Helixi106 – 1127Combined sources
    Turni113 – 1186Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AV5X-ray3.15A/B/C/D/E1-120[»]
    ProteinModelPortaliQ8U151.
    SMRiQ8U151. Positions 15-120.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8U151.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the eukaryotic/archaeal RNase P protein component 2 family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1369.
    HOGENOMiHOG000286243.
    KOiK03537.
    OMAiNPWLIDY.

    Family and domain databases

    HAMAPiMF_00755. RNase_P_2.
    InterProiIPR002759. RNase_P/MRP_subunit.
    IPR016434. RNase_P_comp-2.
    [Graphical view]
    PfamiPF01900. RNase_P_Rpp14. 1 hit.
    [Graphical view]
    PIRSFiPIRSF004952. RNase_P_2. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8U151-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSERPKTLPP TLRDKKRYIA FKVISENQFN KDEIKEAIWN ACLRTLGELG
    60 70 80 90 100
    TAKAKPWLIK FDETTQTGII RCDRNHVYDV IFSLTLVSDI NGNKAIIKVL
    110 120
    GVSGTIKRLK RKFLSQFGWR
    Length:120
    Mass (Da):13,839
    Last modified:June 1, 2002 - v1
    Checksum:iB690DF4C26299915
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE009950 Genomic DNA. Translation: AAL81502.1.
    RefSeqiNP_579107.1. NC_003413.1.
    WP_011012525.1. NC_003413.1.

    Genome annotation databases

    EnsemblBacteriaiAAL81502; AAL81502; PF1378.
    GeneIDi1469254.
    KEGGipfu:PF1378.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE009950 Genomic DNA. Translation: AAL81502.1.
    RefSeqiNP_579107.1. NC_003413.1.
    WP_011012525.1. NC_003413.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AV5X-ray3.15A/B/C/D/E1-120[»]
    ProteinModelPortaliQ8U151.
    SMRiQ8U151. Positions 15-120.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ8U151. 1 interaction.
    STRINGi186497.PF1378.

    Proteomic databases

    PRIDEiQ8U151.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAL81502; AAL81502; PF1378.
    GeneIDi1469254.
    KEGGipfu:PF1378.

    Phylogenomic databases

    eggNOGiCOG1369.
    HOGENOMiHOG000286243.
    KOiK03537.
    OMAiNPWLIDY.

    Enzyme and pathway databases

    BRENDAi3.1.26.5. 5243.

    Miscellaneous databases

    EvolutionaryTraceiQ8U151.

    Family and domain databases

    HAMAPiMF_00755. RNase_P_2.
    InterProiIPR002759. RNase_P/MRP_subunit.
    IPR016434. RNase_P_comp-2.
    [Graphical view]
    PfamiPF01900. RNase_P_Rpp14. 1 hit.
    [Graphical view]
    PIRSFiPIRSF004952. RNase_P_2. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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. "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.
    3. "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.
    4. "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 RNP3, SUBUNIT.
    5. Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS), INTERACTION WITH RNP3, SUBUNIT.
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

    Entry informationi

    Entry nameiRNP2_PYRFU
    AccessioniPrimary (citable) accession number: Q8U151
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: June 1, 2002
    Last modified: May 27, 2015
    This is version 66 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    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.