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Q8U151 (RNP2_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 2

Short name=RNase P component 2
EC=3.1.26.5
Alternative name(s):
Pop5
Gene names
Name:rnp2
Ordered Locus Names:PF1378
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length120 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. The RNA is catalytic, but its KM for pre-tRNA is 170-fold decreased in the presence of the 4 known protein subunits (Rnp1-4). The protein subunits also decrease the amount of Mg2+ needed for activity. Ref.2 Ref.3 Ref.4

Catalytic activity

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. Ref.2

Subunit structure

Consists of a catalytic RNA component and at least 4-5 protein subunits. Forms a subcomplex with Rnp3 which stimulates the catalytic RNA. Ref.2 Ref.3 Ref.4 Ref.5

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00755.

Sequence similarities

Belongs to the eukaryotic/archaeal RNase P protein component 2 family.

Biophysicochemical properties

Kinetic parameters:

kcat is 9.5 min(-1). For enzyme reconstituted with RNA and 4 known subunits (Rnp1-4).

KM=0.18 µM for E.coli pre-tRNA(Tyr) Ref.2

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical term3D-structure
Complete proteome
Reference 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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 120120Ribonuclease P protein component 2 HAMAP-Rule MF_00755
PRO_0000140026

Secondary structure

............... 120
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8U151 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: B690DF4C26299915

FASTA12013,839
        10         20         30         40         50         60 
MSERPKTLPP TLRDKKRYIA FKVISENQFN KDEIKEAIWN ACLRTLGELG TAKAKPWLIK 

        70         80         90        100        110        120 
FDETTQTGII RCDRNHVYDV IFSLTLVSDI NGNKAIIKVL GVSGTIKRLK RKFLSQFGWR 

« Hide

References

« Hide 'large scale' references
[1]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]"Functional reconstitution and characterization of Pyrococcus furiosus RNase P."
Tsai H.Y., Pulukkunat D.K., Woznick W.K., Gopalan V.
Proc. Natl. Acad. Sci. U.S.A. 103:16147-16152(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[3]"Cooperative RNP assembly: complementary rescue of structural defects by protein and RNA subunits of archaeal RNase P."
Chen W.Y., Xu Y., Cho I.M., Oruganti S.V., Foster M.P., Gopalan V.
J. Mol. Biol. 411:368-383(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[4]"Fidelity of tRNA 5'-maturation: a possible basis for the functional dependence of archaeal and eukaryal RNase P on multiple protein cofactors."
Chen W.Y., Singh D., Lai L.B., Stiffler M.A., Lai H.D., Foster M.P., Gopalan V.
Nucleic Acids Res. 40:4666-4680(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RNP3, SUBUNIT.
[5]"Structure of Pfu Pop5, an archaeal RNase P protein."
Wilson R.C., Bohlen C.J., Foster M.P., Bell C.E.
Proc. Natl. Acad. Sci. U.S.A. 103:873-878(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS), INTERACTION WITH RNP3, SUBUNIT.
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009950 Genomic DNA. Translation: AAL81502.1.
RefSeqNP_579107.1. NC_003413.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AV5X-ray3.15A/B/C/D/E1-120[»]
ProteinModelPortalQ8U151.
SMRQ8U151. Positions 15-120.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8U151. 1 interaction.
STRING186497.PF1378.

Proteomic databases

PRIDEQ8U151.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL81502; AAL81502; PF1378.
GeneID1469254.
KEGGpfu:PF1378.

Phylogenomic databases

eggNOGCOG1369.
HOGENOMHOG000286243.
KOK03537.
OMANPWLIDY.

Family and domain databases

HAMAPMF_00755. RNase_P_2.
InterProIPR002759. RNase_P/MRP_subunit.
IPR016434. RNase_P_comp-2.
[Graphical view]
PfamPF01900. RNase_P_Rpp14. 1 hit.
[Graphical view]
PIRSFPIRSF004952. RNase_P_2. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ8U151.

Entry information

Entry nameRNP2_PYRFU
AccessionPrimary (citable) accession number: Q8U151
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2002
Last modified: July 9, 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references