Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ribonuclease P protein component

Gene

rnpA

Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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-HAMAP
  2. tRNA binding Source: UniProtKB-HAMAP

GO - Biological processi

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

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciBPER257313:BP0493-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:BP0493
OrganismiBordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Taxonomic identifieri257313 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000002676: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 123123Ribonuclease P protein componentPRO_0000198432Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi257313.BP0493.

Structurei

3D structure databases

ProteinModelPortaliQ7VSD8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RnpA family.UniRule annotation

Phylogenomic databases

eggNOGiNOG127496.
HOGENOMiHOG000266301.
KOiK03536.
OMAiRNAIKRV.
OrthoDBiEOG6S52QN.

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.

Q7VSD8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPRATLPAEA RLHRPSEFAA ALKGRRLARG AFFIVSASPC APADDQPARA
60 70 80 90 100
RLGLVIAKRF AARAVTRNTL KRVIREAFRA RRLALPAQDY VVRLHSKLTP
110 120
ASLTALKRSA RAEVDAHFTR IAR
Length:123
Mass (Da):13,592
Last modified:October 1, 2003 - v1
Checksum:iE20149F58038F994
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640412 Genomic DNA. Translation: CAE44822.1.
RefSeqiNP_879346.1. NC_002929.2.

Genome annotation databases

EnsemblBacteriaiCAE44822; CAE44822; BP0493.
GeneIDi2664680.
KEGGibpe:BP0493.
PATRICi21154046. VBIBorPer7866_0530.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640412 Genomic DNA. Translation: CAE44822.1.
RefSeqiNP_879346.1. NC_002929.2.

3D structure databases

ProteinModelPortaliQ7VSD8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi257313.BP0493.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE44822; CAE44822; BP0493.
GeneIDi2664680.
KEGGibpe:BP0493.
PATRICi21154046. VBIBorPer7866_0530.

Phylogenomic databases

eggNOGiNOG127496.
HOGENOMiHOG000266301.
KOiK03536.
OMAiRNAIKRV.
OrthoDBiEOG6S52QN.

Enzyme and pathway databases

BioCyciBPER257313:BP0493-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica."
    Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S.
    , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.
    Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Tohama I / ATCC BAA-589 / NCTC 13251.

Entry informationi

Entry nameiRNPA_BORPE
AccessioniPrimary (citable) accession number: Q7VSD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: October 1, 2003
Last modified: February 4, 2015
This is version 64 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

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.