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Q8U007 (RNP1_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 65. 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 1

Short name=RNase P component 1
EC=3.1.26.5
Alternative name(s):
Rpp29
Gene names
Name:rnp1
Ordered Locus Names:PF1816
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length127 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.4 Ref.5

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 protein subunits. Forms a subcomplex with Rnp4 which stimulates the catalytic RNA. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00754.

Domain

Interaction with Rnp4 is mediated by the N-terminus; short deletion mutants are still able to reconstitute RNase P activity. Ref.4

Sequence similarities

Belongs to the eukaryotic/archaeal RNase P protein component 1 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_processmRNA cleavage

Inferred from electronic annotation. Source: InterPro

rRNA processing

Inferred from electronic annotation. Source: InterPro

tRNA 5'-leader removal

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

ribonuclease MRP complex

Inferred from electronic annotation. Source: InterPro

ribonuclease P complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: InterPro

ribonuclease P activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 127127Ribonuclease P protein component 1 HAMAP-Rule MF_00754
PRO_0000128436

Experimental info

Mutagenesis1 – 3131Missing: No interaction with Rnp4, does not reconstitute RNase P activity. Ref.4
Mutagenesis1 – 2424Missing: No interaction with Rnp4, reconstitutes RNase P activity. Ref.4
Mutagenesis1 – 1717Missing: Interacts normally with Rnp4, reconstitutes RNase P activity.

Secondary structure

........................ 127
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8U007 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 3CBBA84DD7AE7E4C

FASTA12714,953
        10         20         30         40         50         60 
MWRNSEEREN RTSGRSQGSY QEIIGRTWIF RGAHRGRVNK KNIVWHELIG LKVRVVNSTH 

        70         80         90        100        110        120 
PGYVGIEGYV IDETRNMLVI AGENKVWKVP KDVCIFEFET WDGTKIKISG EKLVGRPEMR 


LKKRWRK 

« 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]"Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with its RPP29 protein partner."
Amero C.D., Boomershine W.P., Xu Y., Foster M.
Biochemistry 47:11704-11710(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNP1, SUBUNIT.
[4]"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, INTERACTION WITH RNP4, SUBUNIT, DOMAIN, MUTAGENESIS OF 1-MET--GLN-17; 1-MET--ILE-24 AND 1-MET--ARG-31.
[5]"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 RNP4, SUBUNIT.
[6]"Solution structure of an archaeal RNase P binary protein complex: formation of the 30-kDa complex between Pyrococcus furiosus RPP21 and RPP29 is accompanied by coupled protein folding and highlights critical features for protein-protein and protein-RNA interactions."
Xu Y., Amero C.D., Pulukkunat D.K., Gopalan V., Foster M.P.
J. Mol. Biol. 393:1043-1055(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, INTERACTION WITH RNP4, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009950 Genomic DNA. Translation: AAL81940.1.
RefSeqNP_579545.1. NC_003413.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KI7NMR-A1-127[»]
ProteinModelPortalQ8U007.
SMRQ8U007. Positions 36-127.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186497.PF1816.

Proteomic databases

PRIDEQ8U007.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL81940; AAL81940; PF1816.
GeneID1469695.
KEGGpfu:PF1816.

Phylogenomic databases

eggNOGCOG1588.
HOGENOMHOG000231353.
KOK03538.
OMAISTKGRV.

Family and domain databases

Gene3D2.30.30.210. 1 hit.
HAMAPMF_00754. RNase_P_1.
InterProIPR002730. RNase_P/MRP_p29.
IPR023538. RNase_P_comp-1.
IPR023534. Rof/RNase_P-like.
[Graphical view]
PfamPF01868. UPF0086. 1 hit.
[Graphical view]
SMARTSM00538. POP4. 1 hit.
[Graphical view]
SUPFAMSSF101744. SSF101744. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ8U007.

Entry information

Entry nameRNP1_PYRFU
AccessionPrimary (citable) accession number: Q8U007
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 65 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