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Protein

Ribonuclease P protein component

Gene

rnpA

Organism
Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168)
Status
Reviewed-Annotation score: -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

GO - Biological processi

Keywordsi

Molecular functionEndonuclease, Hydrolase, Nuclease, RNA-binding
Biological processtRNA processing

Enzyme and pathway databases

BioCyciOANT439375:G1G9F-1445-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:Oant_1362
OrganismiOchrobactrum anthropi (strain ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168)
Taxonomic identifieri439375 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum
Proteomesi
  • UP000002301 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000214401 – 141Ribonuclease P protein componentAdd BLAST141

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi439375.Oant_1362

Structurei

3D structure databases

ProteinModelPortaliA6WYM5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RnpA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0594 LUCA
HOGENOMiHOG000266302
KOiK03536
OMAiGFTCSKK
OrthoDBiPOG091H01XK

Family and domain databases

Gene3Di3.30.230.10, 1 hit
HAMAPiMF_00227 RNase_P, 1 hit
InterProiView protein in InterPro
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR000100 RNase_P
IPR020539 RNase_P_CS
PANTHERiPTHR33992 PTHR33992, 1 hit
PfamiView protein in Pfam
PF00825 Ribonuclease_P, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD003629 Ribonuclease_P, 1 hit
SUPFAMiSSF54211 SSF54211, 1 hit
TIGRFAMsiTIGR00188 rnpA, 1 hit
PROSITEiView protein in PROSITE
PS00648 RIBONUCLEASE_P, 1 hit

Sequencei

Sequence statusi: Complete.

A6WYM5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKPKQILRL RKRAEFLALR NGEKRRGPLF LLEVRERTEE ESQTAKIGEK
60 70 80 90 100
PRAGFTVTKK NGNAVIRNRI RRRLREAVRC HAGRDMAPST DYVIVAREQA
110 120 130 140
LTAPFSRLTE ELSRRIKAKG ERRGDGKRRT ERPESGPVNG K
Length:141
Mass (Da):16,245
Last modified:August 21, 2007 - v1
Checksum:i3E106FCC969506B3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000758 Genomic DNA Translation: ABS14079.1
RefSeqiWP_010659430.1, NC_009667.1

Genome annotation databases

EnsemblBacteriaiABS14079; ABS14079; Oant_1362
GeneIDi5379556
KEGGioan:Oant_1362
PATRICifig|439375.7.peg.1428

Similar proteinsi

Entry informationi

Entry nameiRNPA_OCHA4
AccessioniPrimary (citable) accession number: A6WYM5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: May 23, 2018
This is version 65 of the entry and version 1 of the sequence. See 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
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Main funding by: National Institutes of Health