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Protein

Ribonuclease P protein component 1

Gene

rnp1

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation3 Publications

Catalytic activityi

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.UniRule annotation1 Publication

Kineticsi

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

  1. KM=0.18 µM for E.coli pre-tRNA(Tyr)1 Publication

GO - Molecular functioni

  1. ribonuclease P activity Source: UniProtKB-HAMAP
  2. RNA binding Source: InterPro

GO - Biological processi

  1. mRNA cleavage Source: InterPro
  2. rRNA processing Source: InterPro
  3. tRNA 5'-leader removal Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

tRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease P protein component 1UniRule annotation (EC:3.1.26.5UniRule annotation)
Short name:
RNase P component 1UniRule annotation
Alternative name(s):
Rpp29UniRule annotation
Gene namesi
Name:rnp1UniRule annotation
Ordered Locus Names:PF1816
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000001013 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. ribonuclease MRP complex Source: InterPro
  3. ribonuclease P complex Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 3131Missing : No interaction with Rnp4, does not reconstitute RNase P activity. 1 PublicationAdd
BLAST
Mutagenesisi1 – 2424Missing : No interaction with Rnp4, reconstitutes RNase P activity. 1 PublicationAdd
BLAST
Mutagenesisi1 – 1717Missing : Interacts normally with Rnp4, reconstitutes RNase P activity. 1 PublicationAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 127127Ribonuclease P protein component 1PRO_0000128436Add
BLAST

Proteomic databases

PRIDEiQ8U007.

Interactioni

Subunit structurei

Consists of a catalytic RNA component and at least 4 protein subunits. Forms a subcomplex with Rnp4 which stimulates the catalytic RNA.5 Publications

Protein-protein interaction databases

STRINGi186497.PF1816.

Structurei

Secondary structure

1
127
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni20 – 223Combined sources
Beta strandi23 – 253Combined sources
Helixi27 – 315Combined sources
Helixi40 – 434Combined sources
Beta strandi52 – 598Combined sources
Turni61 – 655Combined sources
Beta strandi66 – 749Combined sources
Beta strandi77 – 826Combined sources
Beta strandi85 – 884Combined sources
Beta strandi91 – 10010Combined sources
Turni101 – 1033Combined sources
Turni110 – 1134Combined sources
Helixi117 – 1215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KI7NMR-A1-127[»]
ProteinModelPortaliQ8U007.
SMRiQ8U007. Positions 36-127.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8U007.

Family & Domainsi

Domaini

Interaction with Rnp4 is mediated by the N-terminus; short deletion mutants are still able to reconstitute RNase P activity.1 Publication

Sequence similaritiesi

Belongs to the eukaryotic/archaeal RNase P protein component 1 family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1588.
HOGENOMiHOG000231353.
KOiK03538.
OMAiWHELIGL.

Family and domain databases

Gene3Di2.30.30.210. 1 hit.
HAMAPiMF_00754. RNase_P_1.
InterProiIPR002730. RNase_P/MRP_p29.
IPR023538. RNase_P_comp-1.
IPR023534. Rof/RNase_P-like.
[Graphical view]
PfamiPF01868. UPF0086. 1 hit.
[Graphical view]
SMARTiSM00538. POP4. 1 hit.
[Graphical view]
SUPFAMiSSF101744. SSF101744. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8U007-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWRNSEEREN RTSGRSQGSY QEIIGRTWIF RGAHRGRVNK KNIVWHELIG
60 70 80 90 100
LKVRVVNSTH PGYVGIEGYV IDETRNMLVI AGENKVWKVP KDVCIFEFET
110 120
WDGTKIKISG EKLVGRPEMR LKKRWRK
Length:127
Mass (Da):14,953
Last modified:June 1, 2002 - v1
Checksum:i3CBBA84DD7AE7E4C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL81940.1.
RefSeqiNP_579545.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL81940; AAL81940; PF1816.
GeneIDi1469695.
KEGGipfu:PF1816.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL81940.1.
RefSeqiNP_579545.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KI7NMR-A1-127[»]
ProteinModelPortaliQ8U007.
SMRiQ8U007. Positions 36-127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF1816.

Proteomic databases

PRIDEiQ8U007.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL81940; AAL81940; PF1816.
GeneIDi1469695.
KEGGipfu:PF1816.

Phylogenomic databases

eggNOGiCOG1588.
HOGENOMiHOG000231353.
KOiK03538.
OMAiWHELIGL.

Miscellaneous databases

EvolutionaryTraceiQ8U007.

Family and domain databases

Gene3Di2.30.30.210. 1 hit.
HAMAPiMF_00754. RNase_P_1.
InterProiIPR002730. RNase_P/MRP_p29.
IPR023538. RNase_P_comp-1.
IPR023534. Rof/RNase_P-like.
[Graphical view]
PfamiPF01868. UPF0086. 1 hit.
[Graphical view]
SMARTiSM00538. POP4. 1 hit.
[Graphical view]
SUPFAMiSSF101744. SSF101744. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1998) [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(2005) [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(2007) [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(2010) [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(2011) [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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, INTERACTION WITH RNP4, SUBUNIT.

Entry informationi

Entry nameiRNP1_PYRFU
AccessioniPrimary (citable) accession number: Q8U007
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: June 1, 2002
Last modified: April 1, 2015
This is version 71 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.