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P0A0H5

- RNPA_STAAU

UniProt

P0A0H5 - RNPA_STAAU

Protein

Ribonuclease P protein component

Gene

rnpA

Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.

    Catalytic activityi

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

    GO - Molecular functioni

    1. ribonuclease P activity Source: UniProtKB-EC
    2. tRNA binding Source: InterPro

    GO - Biological processi

    1. tRNA processing Source: UniProtKB-KW

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    tRNA processing

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonuclease P protein componentUniRule annotation (EC:3.1.26.5UniRule annotation)
    Short name:
    RNase P proteinUniRule annotation
    Short name:
    RNaseP proteinUniRule annotation
    Alternative name(s):
    Protein C5UniRule annotation
    Gene namesi
    Name:rnpAUniRule annotation
    OrganismiStaphylococcus aureus
    Taxonomic identifieri1280 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 117117Ribonuclease P protein componentPRO_0000198530Add
    BLAST

    Interactioni

    Subunit structurei

    Consists of a catalytic RNA component (M1 or rnpB) and a protein subunit.

    Structurei

    Secondary structure

    1
    117
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 73
    Helixi13 – 219
    Beta strandi27 – 315
    Beta strandi45 – 484
    Beta strandi51 – 533
    Helixi58 – 7215
    Helixi73 – 753
    Beta strandi82 – 865
    Helixi89 – 924
    Helixi97 – 1026
    Helixi105 – 1095
    Beta strandi112 – 1143

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D6TNMR-A1-117[»]
    ProteinModelPortaliP0A0H5.
    SMRiP0A0H5. Positions 1-117.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A0H5.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RnpA family.UniRule annotation

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    HAMAPiMF_00227. RNase_P.
    InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR000100. RNase_P.
    IPR020539. RNase_P_CS.
    [Graphical view]
    PfamiPF00825. Ribonuclease_P. 1 hit.
    [Graphical view]
    ProDomiPD003629. Ribonuclease_P. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    TIGRFAMsiTIGR00188. rnpA. 1 hit.
    PROSITEiPS00648. RIBONUCLEASE_P. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A0H5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLEKAYRIK KNADFQRIYK KGHSVANRQF VVYTCNNKEI DHFRLGISVS    50
    KKLGNAVLRN KIKRAIRENF KVHKSHILAK DIIVIARQPA KDMTTLQIQN 100
    SLEHVLKIAK VFNKKIK 117
    Length:117
    Mass (Da):13,652
    Last modified:February 15, 2005 - v1
    Checksum:iAD5172C3654E01F0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF135268 Genomic DNA. Translation: AAF61418.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF135268 Genomic DNA. Translation: AAF61418.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D6T NMR - A 1-117 [» ]
    ProteinModelPortali P0A0H5.
    SMRi P0A0H5. Positions 1-117.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P0A0H5.

    Family and domain databases

    Gene3Di 3.30.230.10. 1 hit.
    HAMAPi MF_00227. RNase_P.
    InterProi IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR000100. RNase_P.
    IPR020539. RNase_P_CS.
    [Graphical view ]
    Pfami PF00825. Ribonuclease_P. 1 hit.
    [Graphical view ]
    ProDomi PD003629. Ribonuclease_P. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF54211. SSF54211. 1 hit.
    TIGRFAMsi TIGR00188. rnpA. 1 hit.
    PROSITEi PS00648. RIBONUCLEASE_P. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of Staphylococcus aureus ribonuclease P."
      Poppe S.M., Swaney S.M., Choi G.H., Hromockyj A., Shinabarger D.L.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ISP3.
    2. "The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA."
      Spitzfaden C., Nicholson N., Jones J.J., Guth S., Lehr R., Prescott C.D., Hegg L.A., Eggleston D.S.
      J. Mol. Biol. 295:105-115(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiRNPA_STAAU
    AccessioniPrimary (citable) accession number: P0A0H5
    Secondary accession number(s): P58031, Q9LAH9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 15, 2005
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 41 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

    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