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

Q9V166 (RNP4_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 63. 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 4

Short name=RNase P component 4
EC=3.1.26.5
Alternative name(s):
Rpp21
Gene names
Name:rnp4
Ordered Locus Names:PYRAB05620
ORF Names:PAB0385
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length117 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends By similarity. HAMAP-Rule MF_00757

Catalytic activity

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. HAMAP-Rule MF_00757

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00757

Subunit structure

Consists of a catalytic RNA component and at least 4-5 protein subunits Potential.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00757.

Sequence similarities

Belongs to the eukaryotic/archaeal RNase P protein component 4 family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtRNA 5'-leader removal

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

ribonuclease P complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionribonuclease P activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 117117Ribonuclease P protein component 4 HAMAP-Rule MF_00757
PRO_0000153858

Sites

Metal binding641Zinc By similarity
Metal binding671Zinc By similarity
Metal binding931Zinc By similarity
Metal binding961Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9V166 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 673E27AADA398A8B

FASTA11714,272
        10         20         30         40         50         60 
MKKVSWEKRE KKKVAIERID TLFTLAEKVV KYSPDLARRY VELALEIQKK SKVKLPRKWK 

        70         80         90        100        110 
RRYCKRCHAF LVPGFNARVR LRTDRMPHVV ITCLECGHIM RYPYLREVKE KRKRKKD 

« Hide

References

« Hide 'large scale' references
[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
[2]"Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
Gao J., Wang J.
Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248284 Genomic DNA. Translation: CAB49484.1.
HE613800 Genomic DNA. Translation: CCE69952.1.
PIRE75175.
RefSeqNP_126253.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9V166.
SMRQ9V166. Positions 1-105.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272844.PAB0385.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB49484; CAB49484; PAB0385.
GeneID1495465.
KEGGpab:PAB0385.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2023.
HOGENOMHOG000230709.
KOK03540.
OMAPRKWKRR.

Family and domain databases

HAMAPMF_00757. RNase_P_4.
InterProIPR016432. RNase_P_comp-4.
IPR007175. Rpr2.
[Graphical view]
PANTHERPTHR14742. PTHR14742. 1 hit.
PfamPF04032. Rpr2. 1 hit.
[Graphical view]
PIRSFPIRSF004878. RNase_P_4. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRNP4_PYRAB
AccessionPrimary (citable) accession number: Q9V166
Secondary accession number(s): G8ZJ25
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 63 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