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Protein

Ribonuclease P protein component

Gene

rnpA

Organism
Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
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

BioCyciSYNEL:SYNPCC7942_1615-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:Synpcc7942_1615
OrganismiSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Taxonomic identifieri1140 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000002717 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 122122Ribonuclease P protein componentPRO_1000021484Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi1140.Synpcc7942_1615.

Structurei

3D structure databases

ProteinModelPortaliQ31MS4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RnpA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0594.
HOGENOMiHOG000266301.
KOiK03536.
OrthoDBiEOG6XWV8K.

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.
[Graphical view]
PfamiPF00825. Ribonuclease_P. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR00188. rnpA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q31MS4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALPRCHRLR QRDRFPALYR GGRKLSTPSL LLRWLPQAEI ESVNESRFAI
60 70 80 90 100
VISLKVHKRA VRRNRLRRRL QAALLRLRDR LRPGFDGLLT VKPGLDLDTS
110 120
TSQFLQELED LLTRAEIIHG RQ
Length:122
Mass (Da):14,286
Last modified:December 6, 2005 - v1
Checksum:iACB633774EA578F9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000100 Genomic DNA. Translation: ABB57645.1.
RefSeqiYP_400632.1. NC_007604.1.

Genome annotation databases

EnsemblBacteriaiABB57645; ABB57645; Synpcc7942_1615.
KEGGisyf:Synpcc7942_1615.
PATRICi23788629. VBISynElo51371_1838.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000100 Genomic DNA. Translation: ABB57645.1.
RefSeqiYP_400632.1. NC_007604.1.

3D structure databases

ProteinModelPortaliQ31MS4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1140.Synpcc7942_1615.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB57645; ABB57645; Synpcc7942_1615.
KEGGisyf:Synpcc7942_1615.
PATRICi23788629. VBISynElo51371_1838.

Phylogenomic databases

eggNOGiCOG0594.
HOGENOMiHOG000266301.
KOiK03536.
OrthoDBiEOG6XWV8K.

Enzyme and pathway databases

BioCyciSYNEL:SYNPCC7942_1615-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.
[Graphical view]
PfamiPF00825. Ribonuclease_P. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR00188. rnpA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7942.

Entry informationi

Entry nameiRNPA_SYNE7
AccessioniPrimary (citable) accession number: Q31MS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 6, 2005
Last modified: April 1, 2015
This is version 57 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.