Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O59150 (RNP2_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease P protein component 2

Short name=RNase P component 2
EC=3.1.26.5
Alternative name(s):
Pop5
Gene names
Name:rnp2
Ordered Locus Names:PH1481
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length120 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Ref.2 Ref.3 Ref.4

Catalytic activity

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. HAMAP-Rule MF_00755

Subunit structure

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. Ref.2 Ref.3 Ref.4 Ref.5

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00755.

Sequence similarities

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

Biophysicochemical properties

Temperature dependence:

Optimum temperature is 70 degrees Celsius. Ref.2 Ref.3

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 120120Ribonuclease P protein component 2 HAMAP-Rule MF_00755
PRO_0000140027

Experimental info

Mutagenesis43 – 486Missing: Froms heterodimer with Rnp3, but not heterotetramer. Does not reconstitute RNase P activity. Ref.5
Mutagenesis721C → S: Fully reconstitutes RNase P activity. Ref.5

Secondary structure

.................. 120
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O59150 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: C78C9EF6C5380E53

FASTA12014,044
        10         20         30         40         50         60 
MMRKLKTLPP TLRDKNRYIA FEIISDGDFT KDEVKELIWK SSLEVLGETG TAIVKPWLIK 

        70         80         90        100        110        120 
FDPNTKTGIV RCDREYVEYL RFALMLVSEF NGKRLIIRTL GVSGTIKRLK RKFLAKYGWK 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3."
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. expand/collapse author list , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.
DNA Res. 5:55-76(1998) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000001 Genomic DNA. Translation: BAA30588.1.
PIRD71023.
RefSeqNP_143344.1. NC_000961.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CZVX-ray2.00C/D1-120[»]
ProteinModelPortalO59150.
SMRO59150. Positions 2-120.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO59150. 2 interactions.
STRING70601.PH1481.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA30588; BAA30588; BAA30588.
GeneID1443798.
KEGGpho:PH1481.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1369.
HOGENOMHOG000286243.
KOK03537.
OMANPWLIDY.

Enzyme and pathway databases

BioCycPHOR70601:GJWR-1479-MONOMER.

Family and domain databases

HAMAPMF_00755. RNase_P_2.
InterProIPR002759. RNase_P/MRP_subunit.
IPR016434. RNase_P_comp-2.
[Graphical view]
PfamPF01900. RNase_P_Rpp14. 1 hit.
[Graphical view]
PIRSFPIRSF004952. RNase_P_2. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO59150.

Entry information

Entry nameRNP2_PYRHO
AccessionPrimary (citable) accession number: O59150
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references