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Q8U007

- RNP1_PYRFU

UniProt

Q8U007 - RNP1_PYRFU

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Protein

Ribonuclease P protein component 1

Gene
rnp1, PF1816
Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed - 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.3 Publications

Catalytic activityi

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.1 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 1 (EC:3.1.26.5)
Short name:
RNase P component 1
Alternative name(s):
Rpp29
Gene namesi
Name:rnp1
Ordered Locus Names:PF1816
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000001013: Chromosome

Subcellular locationi

Cytoplasm By similarity 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. Add
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 127127Ribonuclease P protein component 1UniRule annotationPRO_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 – 223
Beta strandi23 – 253
Helixi27 – 315
Helixi40 – 434
Beta strandi52 – 598
Turni61 – 655
Beta strandi66 – 749
Beta strandi77 – 826
Beta strandi85 – 884
Beta strandi91 – 10010
Turni101 – 1033
Turni110 – 1134
Helixi117 – 1215

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KI7NMR-A1-127[»]
ProteinModelPortaliQ8U007.
SMRiQ8U007. Positions 36-127.

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

Phylogenomic databases

eggNOGiCOG1588.
HOGENOMiHOG000231353.
KOiK03538.
OMAiISTKGRV.

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

MWRNSEEREN RTSGRSQGSY QEIIGRTWIF RGAHRGRVNK KNIVWHELIG    50
LKVRVVNSTH PGYVGIEGYV IDETRNMLVI AGENKVWKVP KDVCIFEFET 100
WDGTKIKISG EKLVGRPEMR LKKRWRK 127
Length:127
Mass (Da):14,953
Last modified:June 1, 2002 - v1
Checksum:i3CBBA84DD7AE7E4C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE009950 Genomic DNA. Translation: AAL81940.1 .
RefSeqi NP_579545.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KI7 NMR - A 1-127 [» ]
ProteinModelPortali Q8U007.
SMRi Q8U007. Positions 36-127.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 186497.PF1816.

Proteomic databases

PRIDEi Q8U007.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL81940 ; AAL81940 ; PF1816 .
GeneIDi 1469695.
KEGGi pfu:PF1816.

Phylogenomic databases

eggNOGi COG1588.
HOGENOMi HOG000231353.
KOi K03538.
OMAi ISTKGRV.

Miscellaneous databases

EvolutionaryTracei Q8U007.

Family and domain databases

Gene3Di 2.30.30.210. 1 hit.
HAMAPi MF_00754. RNase_P_1.
InterProi IPR002730. RNase_P/MRP_p29.
IPR023538. RNase_P_comp-1.
IPR023534. Rof/RNase_P-like.
[Graphical view ]
Pfami PF01868. UPF0086. 1 hit.
[Graphical view ]
SMARTi SM00538. POP4. 1 hit.
[Graphical view ]
SUPFAMi SSF101744. SSF101744. 1 hit.
ProtoNeti Search...

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(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.

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: July 9, 2014
This is version 65 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

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