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Q9P9U0

- RNPA_XYLFA

UniProt

Q9P9U0 - RNPA_XYLFA

Protein

Ribonuclease P protein component

Gene

rnpA

Organism
Xylella fastidiosa (strain 9a5c)
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

    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:XF_2781
    OrganismiXylella fastidiosa (strain 9a5c)
    Taxonomic identifieri160492 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella
    ProteomesiUP000000812: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 135135Ribonuclease P protein componentPRO_0000198569Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi160492.XF2781.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9P9U0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RnpA family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0594.
    KOiK03536.
    OMAiGRRYSSV.
    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.

    Q9P9U0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNSCKRFPRS ARICLRSEYY VAFEQGRRYS SVLLRLHHLP TSGPVRLGLV    50
    VSRRVDIRAV NRNRIKRALR EVMRQIAYKL VPGDYVVVVR QTAKDVSNAE 100
    LSVALLSLLR RIGALPLAPI DNAMLPFFER NCSRK 135
    Length:135
    Mass (Da):15,492
    Last modified:June 16, 2003 - v2
    Checksum:i2C59AE7C6BACB89C
    GO

    Sequence cautioni

    The sequence AAF85566.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE003849 Genomic DNA. Translation: AAF85566.1. Different initiation.
    PIRiA82517.
    RefSeqiNP_300058.1. NC_002488.3.

    Genome annotation databases

    EnsemblBacteriaiAAF85566; AAF85566; XF_2781.
    GeneIDi1128347.
    KEGGixfa:XF2781.
    PATRICi24135891. VBIXylFas578_2953.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE003849 Genomic DNA. Translation: AAF85566.1 . Different initiation.
    PIRi A82517.
    RefSeqi NP_300058.1. NC_002488.3.

    3D structure databases

    ProteinModelPortali Q9P9U0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 160492.XF2781.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF85566 ; AAF85566 ; XF_2781 .
    GeneIDi 1128347.
    KEGGi xfa:XF2781.
    PATRICi 24135891. VBIXylFas578_2953.

    Phylogenomic databases

    eggNOGi COG0594.
    KOi K03536.
    OMAi GRRYSSV.
    OrthoDBi EOG6C01C6.

    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. "The genome sequence of the plant pathogen Xylella fastidiosa."
      Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A.
      , Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.
      Nature 406:151-159(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 9a5c.

    Entry informationi

    Entry nameiRNPA_XYLFA
    AccessioniPrimary (citable) accession number: Q9P9U0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: June 16, 2003
    Last modified: October 1, 2014
    This is version 83 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3