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
Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024)
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

BioCyciSDEG203122:G1G67-4232-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:Sde_4016
OrganismiSaccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024)
Taxonomic identifieri203122 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaCellvibrionalesCellvibrionaceaeSaccharophagus
Proteomesi
  • UP000001947 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000214541 – 135Ribonuclease P protein componentAdd BLAST135

Proteomic databases

PRIDEiQ21DF8

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi203122.Sde_4016

Structurei

3D structure databases

ProteinModelPortaliQ21DF8
SMRiQ21DF8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RnpA family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105NVJ Bacteria
COG0594 LUCA
HOGENOMiHOG000266301
KOiK03536
OMAiLHQHELP
OrthoDBiPOG091H011Y

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.

Q21DF8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSASPKERCF SFGKDQRLLN SSDFTPVFND APIRASNSEI LILCKLSTTG
60 70 80 90 100
KARLGLVVAK KNIKHANKRN QFKRIARESF RLKQHKLPPI DAIVLARRGA
110 120 130
DSLSKVELRR MFDGLWKRVV KKAEKLTATQ PEKTG
Length:135
Mass (Da):15,262
Last modified:April 18, 2006 - v1
Checksum:i648BE6B19AD58BC1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000282 Genomic DNA Translation: ABD83271.1
RefSeqiWP_011470486.1, NC_007912.1

Genome annotation databases

EnsemblBacteriaiABD83271; ABD83271; Sde_4016
KEGGisde:Sde_4016

Entry informationi

Entry nameiRNPA_SACD2
AccessioniPrimary (citable) accession number: Q21DF8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 18, 2006
Last modified: May 23, 2018
This is version 74 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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health