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Q8U0H6

- RNP4_PYRFU

UniProt

Q8U0H6 - RNP4_PYRFU

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Protein

Ribonuclease P protein component 4

Gene

rnp4

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 PublicationsUniRule annotation

Catalytic activityi

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.1 PublicationUniRule annotation

Cofactori

Binds 1 zinc ion per subunit.2 PublicationsUniRule annotation

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631Zinc2 PublicationsUniRule annotation
Metal bindingi66 – 661Zinc2 PublicationsUniRule annotation
Metal bindingi92 – 921Zinc2 PublicationsUniRule annotation
Metal bindingi95 – 951Zinc2 PublicationsUniRule annotation

GO - Molecular functioni

  1. ribonuclease P activity Source: UniProtKB-HAMAP
  2. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. tRNA 5'-leader removal Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease P protein component 4UniRule annotation (EC:3.1.26.5UniRule annotation)
Short name:
RNase P component 4UniRule annotation
Alternative name(s):
Rpp21UniRule annotation
Gene namesi
Name:rnp4UniRule annotation
Ordered Locus Names:PF1613
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000001013: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
  2. ribonuclease P complex Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141A → V: 3-fold reduced binding to Rnp1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 117117Ribonuclease P protein component 4PRO_0000153859Add
BLAST

Proteomic databases

PRIDEiQ8U0H6.

Interactioni

Subunit structurei

Consists of a catalytic RNA component and at least 4 protein subunits. Forms a subcomplex with Rnp1 which stimulates the catalytic RNA.5 Publications

Protein-protein interaction databases

STRINGi186497.PF1613.

Structurei

Secondary structure

1
117
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 3116
Helixi33 – 5018
Turni57 – 604
Turni64 – 663
Turni72 – 743
Beta strandi75 – 817
Beta strandi83 – 853
Beta strandi87 – 926
Turni93 – 953
Beta strandi98 – 1025

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K3RNMR-A1-117[»]
2KI7NMR-B1-117[»]
ProteinModelPortaliQ8U0H6.
SMRiQ8U0H6. Positions 13-104.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8U0H6.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG2023.
HOGENOMiHOG000230709.
KOiK03540.
OMAiPRKWKRR.

Family and domain databases

HAMAPiMF_00757. RNase_P_4.
InterProiIPR016432. RNase_P_comp-4.
IPR007175. Rpr2.
[Graphical view]
PANTHERiPTHR14742. PTHR14742. 1 hit.
PfamiPF04032. Rpr2. 1 hit.
[Graphical view]
PIRSFiPIRSF004878. RNase_P_4. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8U0H6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKYNEKKEK KRIAKERIDI LFSLAERVFP YSPELAKRYV ELALLVQQKA
60 70 80 90 100
KVKIPRKWKR RYCKKCHAFL VPGINARVRL RQKRMPHIVV KCLECGHIMR
110
YPYIKEIKKR RKEKMEY
Length:117
Mass (Da):14,303
Last modified:June 1, 2002 - v1
Checksum:i876CD8CC664F3F38
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE009950 Genomic DNA. Translation: AAL81737.1.
RefSeqiNP_579342.1. NC_003413.1.
WP_011012760.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL81737; AAL81737; PF1613.
GeneIDi1469490.
KEGGipfu:PF1613.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE009950 Genomic DNA. Translation: AAL81737.1 .
RefSeqi NP_579342.1. NC_003413.1.
WP_011012760.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2K3R NMR - A 1-117 [» ]
2KI7 NMR - B 1-117 [» ]
ProteinModelPortali Q8U0H6.
SMRi Q8U0H6. Positions 13-104.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 186497.PF1613.

Proteomic databases

PRIDEi Q8U0H6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL81737 ; AAL81737 ; PF1613 .
GeneIDi 1469490.
KEGGi pfu:PF1613.

Phylogenomic databases

eggNOGi COG2023.
HOGENOMi HOG000230709.
KOi K03540.
OMAi PRKWKRR.

Miscellaneous databases

EvolutionaryTracei Q8U0H6.

Family and domain databases

HAMAPi MF_00757. RNase_P_4.
InterProi IPR016432. RNase_P_comp-4.
IPR007175. Rpr2.
[Graphical view ]
PANTHERi PTHR14742. PTHR14742. 1 hit.
Pfami PF04032. Rpr2. 1 hit.
[Graphical view ]
PIRSFi PIRSF004878. RNase_P_4. 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. "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 RNP1, 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 RNP1, SUBUNIT.
  5. "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: STRUCTURE BY NMR IN COMPLEX WITH ZINC, INTERACTION WITH RNP1, SUBUNIT, COFACTOR.
  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 IN COMPLEX WITH RNP1 AND ZINC, COFACTOR, SUBUNIT, MUTAGENESIS OF ALA-14.

Entry informationi

Entry nameiRNP4_PYRFU
AccessioniPrimary (citable) accession number: Q8U0H6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: June 1, 2002
Last modified: October 29, 2014
This is version 64 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