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A9KBT3

- RNPA_COXBN

UniProt

A9KBT3 - RNPA_COXBN

Protein

Ribonuclease P protein component

Gene

rnpA

Organism
Coxiella burnetii (strain Dugway 5J108-111)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
  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.UniRule annotation

    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

    Enzyme and pathway databases

    BioCyciCBUR434922:GJTP-219-MONOMER.

    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
    Ordered Locus Names:CBUD_0203
    OrganismiCoxiella burnetii (strain Dugway 5J108-111)
    Taxonomic identifieri434922 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
    ProteomesiUP000008555: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 121121Ribonuclease P protein componentPRO_1000078195Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi434922.CBUD_0203.

    Structurei

    3D structure databases

    ProteinModelPortaliA9KBT3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RnpA family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0594.
    HOGENOMiHOG000266301.
    KOiK03536.
    OMAiFTQLERQ.
    OrthoDBiEOG6C01C6.

    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.

    A9KBT3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKGFSVGWR IRTTAEFRRI YAARQRIIGR YYLLYYRENE IKHSRLGVVA    50
    SKRNVRKAVW RNRVRRVVKE TFRIRKKDLP AFDIVVVAKA SSVEADNKEL 100
    YECINKLFTQ LERQSKRSSS V 121
    Length:121
    Mass (Da):14,456
    Last modified:February 5, 2008 - v1
    Checksum:iF67D36E3D63ADEFE
    GO

    Sequence cautioni

    The sequence ABS77389.2 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000733 Genomic DNA. Translation: ABS77389.2. Different initiation.
    RefSeqiYP_001423628.2. NC_009727.1.

    Genome annotation databases

    EnsemblBacteriaiABS77389; ABS77389; CBUD_0203.
    GeneIDi5458885.
    KEGGicbd:CBUD_0203.
    PATRICi17920257. VBICoxBur32972_0252.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000733 Genomic DNA. Translation: ABS77389.2 . Different initiation.
    RefSeqi YP_001423628.2. NC_009727.1.

    3D structure databases

    ProteinModelPortali A9KBT3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 434922.CBUD_0203.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABS77389 ; ABS77389 ; CBUD_0203 .
    GeneIDi 5458885.
    KEGGi cbd:CBUD_0203.
    PATRICi 17920257. VBICoxBur32972_0252.

    Phylogenomic databases

    eggNOGi COG0594.
    HOGENOMi HOG000266301.
    KOi K03536.
    OMAi FTQLERQ.
    OrthoDBi EOG6C01C6.

    Enzyme and pathway databases

    BioCyci CBUR434922:GJTP-219-MONOMER.

    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. "Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
      Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A.
      Infect. Immun. 77:642-656(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Dugway 5J108-111.

    Entry informationi

    Entry nameiRNPA_COXBN
    AccessioniPrimary (citable) accession number: A9KBT3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 50 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3