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Protein

Ribonuclease P protein component 2

Gene

rnp2

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 5 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.UniRule annotation3 Publications

Catalytic activityi

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

Temperature dependencei

Optimum temperature is 70 degrees Celsius.2 Publications

GO - Molecular functioni

  • ribonuclease P activity Source: UniProtKB

GO - Biological processi

  • RNA phosphodiester bond hydrolysis Source: GOC
  • RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  • tRNA 5'-leader removal Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

tRNA processing

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1479-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease P protein component 2UniRule annotation (EC:3.1.26.5UniRule annotation)
Short name:
RNase P component 2UniRule annotation
Alternative name(s):
Pop5UniRule annotation
Gene namesi
Name:rnp2UniRule annotation
Ordered Locus Names:PH1481
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000000752 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • ribonuclease P complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi43 – 486Missing : Froms heterodimer with Rnp3, but not heterotetramer. Does not reconstitute RNase P activity. 1 Publication
Mutagenesisi72 – 721C → S: Fully reconstitutes RNase P activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 120120Ribonuclease P protein component 2PRO_0000140027Add
BLAST

Interactioni

Subunit structurei

Homodimer in solution. Component of RNase P which consists of a catalytic RNA component and at least 5 protein subunits. Forms a heterotetrameric subcomplex with Rnp3. Reconstituted enzyme missing individual protein subunits is suboptimally active, showing each subunit contributes to optimization of activity.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
rnp3O595432EBI-2603177,EBI-2603192
rnp4O592483EBI-2603177,EBI-2641275

Protein-protein interaction databases

IntActiO59150. 2 interactions.
STRINGi70601.PH1481.

Structurei

Secondary structure

1
120
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni10 – 123Combined sources
Beta strandi16 – 249Combined sources
Helixi31 – 5424Combined sources
Beta strandi57 – 626Combined sources
Turni63 – 664Combined sources
Beta strandi67 – 737Combined sources
Helixi74 – 763Combined sources
Helixi77 – 859Combined sources
Beta strandi96 – 10510Combined sources
Helixi106 – 1138Combined sources
Helixi115 – 1173Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CZVX-ray2.00C/D1-120[»]
ProteinModelPortaliO59150.
SMRiO59150. Positions 2-120.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO59150.

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic/archaeal RNase P protein component 2 family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1369.
HOGENOMiHOG000286243.
KOiK03537.
OMAiNPWLIDY.

Family and domain databases

HAMAPiMF_00755. RNase_P_2.
InterProiIPR002759. RNase_P/MRP_subunit.
IPR016434. RNase_P_comp-2.
[Graphical view]
PfamiPF01900. RNase_P_Rpp14. 1 hit.
[Graphical view]
PIRSFiPIRSF004952. RNase_P_2. 1 hit.

Sequencei

Sequence statusi: Complete.

O59150-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMRKLKTLPP TLRDKNRYIA FEIISDGDFT KDEVKELIWK SSLEVLGETG
60 70 80 90 100
TAIVKPWLIK FDPNTKTGIV RCDREYVEYL RFALMLVSEF NGKRLIIRTL
110 120
GVSGTIKRLK RKFLAKYGWK
Length:120
Mass (Da):14,044
Last modified:August 1, 1998 - v1
Checksum:iC78C9EF6C5380E53
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30588.1.
PIRiD71023.
RefSeqiNP_143344.1. NC_000961.1.
WP_010885560.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA30588; BAA30588; BAA30588.
GeneIDi1443798.
KEGGipho:PH1481.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30588.1.
PIRiD71023.
RefSeqiNP_143344.1. NC_000961.1.
WP_010885560.1. NC_000961.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CZVX-ray2.00C/D1-120[»]
ProteinModelPortaliO59150.
SMRiO59150. Positions 2-120.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO59150. 2 interactions.
STRINGi70601.PH1481.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA30588; BAA30588; BAA30588.
GeneIDi1443798.
KEGGipho:PH1481.

Phylogenomic databases

eggNOGiCOG1369.
HOGENOMiHOG000286243.
KOiK03537.
OMAiNPWLIDY.

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1479-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO59150.

Family and domain databases

HAMAPiMF_00755. RNase_P_2.
InterProiIPR002759. RNase_P/MRP_subunit.
IPR016434. RNase_P_comp-2.
[Graphical view]
PfamiPF01900. RNase_P_Rpp14. 1 hit.
[Graphical view]
PIRSFiPIRSF004952. RNase_P_2. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  2. "Reconstitution of archaeal ribonuclease P from RNA and four protein components."
    Kouzuma Y., Mizoguchi M., Takagi H., Fukuhara H., Tsukamoto M., Numata T., Kimura M.
    Biochem. Biophys. Res. Commun. 306:666-673(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  3. "A fifth protein subunit Ph1496p elevates the optimum temperature for the ribonuclease P activity from Pyrococcus horikoshii OT3."
    Fukuhara H., Kifusa M., Watanabe M., Terada A., Honda T., Numata T., Kakuta Y., Kimura M.
    Biochem. Biophys. Res. Commun. 343:956-964(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  4. "Characterization of the archaeal ribonuclease P proteins from Pyrococcus horikoshii OT3."
    Terada A., Honda T., Fukuhara H., Hada K., Kimura M.
    J. Biochem. 140:293-298(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  5. "Crystal structure of protein Ph1481p in complex with protein Ph1877p of archaeal RNase P from Pyrococcus horikoshii OT3: implication of dimer formation of the holoenzyme."
    Kawano S., Nakashima T., Kakuta Y., Tanaka I., Kimura M.
    J. Mol. Biol. 357:583-591(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH RNP3, SUBUNIT, MUTAGENESIS OF 43-LEU--GLU-48 AND CYS-72.
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Entry informationi

Entry nameiRNP2_PYRHO
AccessioniPrimary (citable) accession number: O59150
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: August 1, 1998
Last modified: May 27, 2015
This is version 84 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

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.