Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q1IY22 (RNPA_DEIGD) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease P protein component

Short name=RNase P protein
Short name=RNaseP protein
EC=3.1.26.5
Alternative name(s):
Protein C5
Gene names
Name:rnpA
Ordered Locus Names:Dgeo_1567
OrganismDeinococcus geothermalis (strain DSM 11300) [Complete proteome] [HAMAP]
Taxonomic identifier319795 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length143 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_00227

Catalytic activity

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. HAMAP-Rule MF_00227

Subunit structure

Consists of a catalytic RNA component (M1 or rnpB) and a protein subunit By similarity.

Sequence similarities

Belongs to the RnpA family.

Ontologies

Keywords
   Biological processtRNA processing
   LigandRNA-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionribonuclease P activity

Inferred from electronic annotation. Source: UniProtKB-EC

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 143143Ribonuclease P protein component HAMAP-Rule MF_00227
PRO_1000194629

Sequences

Sequence LengthMass (Da)Tools
Q1IY22 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: A93656133A48EE5C

FASTA14315,870
        10         20         30         40         50         60 
MKGEREFRRV RQQGVALRDP LFTLRVTDYR PRHGEVWRPQ AIIGIVVSKK TLRRAVDRNR 

        70         80         90        100        110        120 
ARRRVREALR TLPGGLPPCR AILLPNPGVL TVPFPELQAA LVRVLAQVPG RVKRKGGGPG 

       130        140 
GNRRSAPPGS APLTDDGRLR GEP 

« Hide

References

[1]"Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J., Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 11300.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000359 Genomic DNA. Translation: ABF45862.1.
RefSeqYP_605031.1. NC_008025.1.

3D structure databases

ProteinModelPortalQ1IY22.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING319795.Dgeo_1567.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF45862; ABF45862; Dgeo_1567.
GeneID4057258.
KEGGdge:Dgeo_1567.
PATRIC21625067. VBIDeiGeo41128_2162.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0594.
HOGENOMHOG000124338.
KOK03536.
OMALPPCRAI.
OrthoDBEOG6B8XPX.
ProtClustDBCLSK445430.

Enzyme and pathway databases

BioCycDGEO319795:GHMU-1596-MONOMER.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
HAMAPMF_00227. RNase_P.
InterProIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000100. RNase_P.
IPR020539. RNase_P_CS.
[Graphical view]
PfamPF00825. Ribonuclease_P. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
TIGRFAMsTIGR00188. rnpA. 1 hit.
PROSITEPS00648. RIBONUCLEASE_P. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRNPA_DEIGD
AccessionPrimary (citable) accession number: Q1IY22
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 13, 2006
Last modified: April 16, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families