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Protein

Ribonuclease P protein component 4

Gene

rnp4

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Binds RNase P RNA.UniRule annotation5 Publications

Catalytic activityi

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

Cofactori

Zn2+UniRule annotation2 PublicationsNote: Binds 1 zinc ion per subunit.UniRule annotation2 Publications

Temperature dependencei

Optimum temperature is 70 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi68Zinc1
Metal bindingi71Zinc1
Metal bindingi97Zinc1
Metal bindingi100Zinc1

GO - Molecular functioni

  • ribonuclease P activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • tRNA 5'-leader removal Source: UniProtKB

Keywordsi

Molecular functionEndonuclease, Hydrolase, Nuclease
Biological processtRNA processing
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciPHOR70601:G1G39-1555-MONOMER

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:PH1601
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • ribonuclease P complex Source: UniProtKB

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi22R → A: 40% reconstituted RNase P activity. 1 Publication1
Mutagenesisi44Y → A: 40% reconstituted RNase P activity. 1 Publication1
Mutagenesisi65R → A: 70% reconstituted RNase P activity. 1 Publication1
Mutagenesisi68 – 71CKRC → SKRS: Does not reconstitute RNase P activity. Protein destabilized. 1 Publication4
Mutagenesisi69K → A: 10% reconstituted RNase P activity. 1 Publication1
Mutagenesisi84R → A: 50% reconstituted RNase P activity. 1 Publication1
Mutagenesisi86R → A: 20% reconstituted RNase P activity. 1 Publication1
Mutagenesisi97 – 100CLEC → SLES: Does not reconstitute RNase P activity. Protein destabilized. 1 Publication4
Mutagenesisi105R → A: Does not reconstitute RNase P activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001538601 – 120Ribonuclease P protein component 4Add BLAST120

Proteomic databases

PRIDEiO59248

Interactioni

Subunit structurei

Consists of a catalytic RNA component and at least 5 protein subunits. Forms a heterodimeric subcomplex with Rnp1. Reconstituted enzyme missing individual protein subunits is suboptimally active, showing each subunit contributes to optimization of activity.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
rnp2O591503EBI-2641275,EBI-2603177

Protein-protein interaction databases

IntActiO59248, 2 interactors
STRINGi70601.PH1601

Structurei

Secondary structure

1120
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 34Combined sources30
Helixi38 – 55Combined sources18
Turni61 – 65Combined sources5
Turni69 – 71Combined sources3
Turni77 – 79Combined sources3
Beta strandi80 – 86Combined sources7
Beta strandi88 – 90Combined sources3
Beta strandi92 – 97Combined sources6
Turni98 – 100Combined sources3
Beta strandi103 – 107Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X0TX-ray1.60A1-120[»]
2ZAEX-ray2.21B/D1-120[»]
ProteinModelPortaliO59248
SMRiO59248
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO59248

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiarCOG04345 Archaea
COG2023 LUCA
HOGENOMiHOG000230709
KOiK03540
OMAiHVVITCL
OrthoDBiPOG093Z0K3G

Family and domain databases

HAMAPiMF_00757 RNase_P_4, 1 hit
InterProiView protein in InterPro
IPR016432 RNase_P_comp-4
IPR007175 Rpr2
PfamiView protein in Pfam
PF04032 Rpr2, 1 hit
PIRSFiPIRSF004878 RNase_P_4, 1 hit

Sequencei

Sequence statusi: Complete.

O59248-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDIVKRRDW EKKEKKKIAI ERIDTLFTLA ERVARYSPDL AKRYVELALE
60 70 80 90 100
IQKKAKVKIP RKWKRRYCKR CHTFLIPGVN ARVRLRTKRM PHVVITCLEC
110 120
GYIMRYPYLR EVKQKRKKAT
Length:120
Mass (Da):14,589
Last modified:August 1, 1998 - v1
Checksum:i2AC453B35C964AE6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA Translation: BAA30713.1
PIRiA71039
RefSeqiWP_010885676.1, NC_000961.1

Genome annotation databases

EnsemblBacteriaiBAA30713; BAA30713; BAA30713
GeneIDi1442455
KEGGipho:PH1601

Similar proteinsi

Entry informationi

Entry nameiRNP4_PYRHO
AccessioniPrimary (citable) accession number: O59248
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: August 1, 1998
Last modified: May 23, 2018
This is version 96 of the entry and version 1 of the sequence. See 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

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