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
Escherichia coli (strain UTI89 / UPEC)
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

BioCyciECOL364106:GHPQ-4217-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:UTI89_C4255
OrganismiEscherichia coli (strain UTI89 / UPEC)
Taxonomic identifieri364106 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001952: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 119119Ribonuclease P protein componentPRO_1000021406Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi364106.UTI89_C4255.

Structurei

3D structure databases

ProteinModelPortaliQ1R4N2.
SMRiQ1R4N2. Positions 1-119.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RnpA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0594.
HOGENOMiHOG000266301.
KOiK03536.
OMAiPPMDFVV.
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.

Q1R4N2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKLAFPREL RLLTPSQFTF VFQQPQRAGT PQITILGRLN SLGHPRIGLT
60 70 80 90 100
VAKKNVRRAH ERNRIKRLTR ESFRLRQHEL PAMDFVVVAK KGVADLDNRA
110
LSEALEKLWR RHCRLARGS
Length:119
Mass (Da):13,789
Last modified:May 16, 2006 - v1
Checksum:i449D9EDACA1C6240
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000243 Genomic DNA. Translation: ABE09682.1.
RefSeqiYP_543213.1. NC_007946.1.

Genome annotation databases

EnsemblBacteriaiABE09682; ABE09682; UTI89_C4255.
GeneIDi3992809.
KEGGieci:UTI89_C4255.
PATRICi18457938. VBIEscCol42261_4165.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000243 Genomic DNA. Translation: ABE09682.1.
RefSeqiYP_543213.1. NC_007946.1.

3D structure databases

ProteinModelPortaliQ1R4N2.
SMRiQ1R4N2. Positions 1-119.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi364106.UTI89_C4255.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE09682; ABE09682; UTI89_C4255.
GeneIDi3992809.
KEGGieci:UTI89_C4255.
PATRICi18457938. VBIEscCol42261_4165.

Phylogenomic databases

eggNOGiCOG0594.
HOGENOMiHOG000266301.
KOiK03536.
OMAiPPMDFVV.
OrthoDBiEOG6C01C6.

Enzyme and pathway databases

BioCyciECOL364106:GHPQ-4217-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. "Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach."
    Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.
    Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: UTI89 / UPEC.

Entry informationi

Entry nameiRNPA_ECOUT
AccessioniPrimary (citable) accession number: Q1R4N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 16, 2006
Last modified: February 4, 2015
This is version 61 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

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.