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Protein

Ribonuclease P protein component 2

Gene

rnp2

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 3 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

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

Enzyme and pathway databases

BRENDAi3.1.26.5. 5243.

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:PF1378
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 P complex Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 120120Ribonuclease P protein component 2PRO_0000140026Add
BLAST

Proteomic databases

PRIDEiQ8U151.

Interactioni

Subunit structurei

Consists of a catalytic RNA component and at least 4-5 protein subunits. Forms a subcomplex with Rnp3 which stimulates the catalytic RNA.UniRule annotation4 Publications

Protein-protein interaction databases

IntActiQ8U151. 1 interaction.
STRINGi186497.PF1378.

Structurei

Secondary structure

1
120
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 2712Combined sources
Helixi31 – 5424Combined sources
Beta strandi57 – 626Combined sources
Turni63 – 664Combined sources
Beta strandi67 – 737Combined sources
Helixi74 – 763Combined sources
Helixi77 – 859Combined sources
Beta strandi93 – 10513Combined sources
Helixi106 – 1127Combined sources
Turni113 – 1186Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AV5X-ray3.15A/B/C/D/E1-120[»]
ProteinModelPortaliQ8U151.
SMRiQ8U151. Positions 15-120.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8U151.

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.

Q8U151-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSERPKTLPP TLRDKKRYIA FKVISENQFN KDEIKEAIWN ACLRTLGELG
60 70 80 90 100
TAKAKPWLIK FDETTQTGII RCDRNHVYDV IFSLTLVSDI NGNKAIIKVL
110 120
GVSGTIKRLK RKFLSQFGWR
Length:120
Mass (Da):13,839
Last modified:May 31, 2002 - v1
Checksum:iB690DF4C26299915
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL81502.1.
RefSeqiNP_579107.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL81502; AAL81502; PF1378.
GeneIDi1469254.
KEGGipfu:PF1378.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL81502.1.
RefSeqiNP_579107.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AV5X-ray3.15A/B/C/D/E1-120[»]
ProteinModelPortaliQ8U151.
SMRiQ8U151. Positions 15-120.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8U151. 1 interaction.
STRINGi186497.PF1378.

Proteomic databases

PRIDEiQ8U151.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL81502; AAL81502; PF1378.
GeneIDi1469254.
KEGGipfu:PF1378.

Phylogenomic databases

eggNOGiCOG1369.
HOGENOMiHOG000286243.
KOiK03537.
OMAiNPWLIDY.

Enzyme and pathway databases

BRENDAi3.1.26.5. 5243.

Miscellaneous databases

EvolutionaryTraceiQ8U151.

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. "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. "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, 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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RNP3, SUBUNIT.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS), INTERACTION WITH RNP3, SUBUNIT.
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Entry informationi

Entry nameiRNP2_PYRFU
AccessioniPrimary (citable) accession number: Q8U151
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2004
Last sequence update: May 31, 2002
Last modified: March 31, 2015
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

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.