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

O59543 (RNP3_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. 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 3

Short name=RNase P component 3
EC=3.1.26.5
Alternative name(s):
Rpp30
Gene names
Name:rnp3
Ordered Locus Names:PH1877
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length212 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. Not absolutely essential for activity in vitro, however it strongly stimulates activity. Binds RNase P RNA. Ref.2 Ref.3 Ref.4

Catalytic activity

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. HAMAP-Rule MF_00756

Subunit structure

Consists of a catalytic RNA component and at least 5 protein subunits. Forms a heterotetrameric subcomplex with Rnp2. Reconstituted enzyme missing individual protein subunits is suboptimally active, showing each subunit contributes to optimization of activity. Ref.2 Ref.3 Ref.4 Ref.6

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00756.

Sequence similarities

Belongs to the eukaryotic/archaeal RNase P protein component 3 family.

Biophysicochemical properties

Temperature dependence:

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

rnp2O591502EBI-2603192,EBI-2603177

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 212212Ribonuclease P protein component 3 HAMAP-Rule MF_00756
PRO_0000140046

Experimental info

Mutagenesis421K → A: Fully reconstitutes RNase P activity. Ref.5
Mutagenesis681R → A: 75% reconstituted RNase P activity. Ref.5
Mutagenesis871R → A: Fully reconstitutes RNase P activity. Ref.5
Mutagenesis901R → A: 45% reconstituted RNase P activity. Ref.5
Mutagenesis981D → A: 80% reconstituted RNase P activity. Ref.5
Mutagenesis1071R → A: 45% reconstituted RNase P activity. Ref.5
Mutagenesis1141H → A: 75% reconstituted RNase P activity. Ref.5
Mutagenesis1231K → A: 45% reconstituted RNase P activity. Ref.5
Mutagenesis1581K → A: 75% reconstituted RNase P activity. Ref.5
Mutagenesis1761R → A: 45% reconstituted RNase P activity. Ref.5
Mutagenesis1801D → A: 50% reconstituted RNase P activity. Ref.5
Mutagenesis1961K → A: 45% reconstituted RNase P activity. Ref.5

Secondary structure

......................................... 212
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O59543 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 321490D4A2859C24

FASTA21224,694
        10         20         30         40         50         60 
MVGGGGVKFI EMDIRDKEAY ELAKEWFDEV VVSIKFNEEV DKEKLREARK EYGKVAILLS 

        70         80         90        100        110        120 
NPKPSLVRDT VQKFKSYLIY VESNDLRVIR YSIEKGVDAI ISPWVNRKDP GIDHVLAKLM 

       130        140        150        160        170        180 
VKKNVALGFS LRPLLYSNPY ERANLLRFMM KAWKLVEKYK VRRFLTSSAQ EKWDVRYPRD 

       190        200        210 
LISLGVVIGM EIPQAKASIS MYPEIILKRL KY 

« 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, RNA-BINDING.
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 the ribonuclease P protein Ph1877p from hyperthermophilic archaeon Pyrococcus horikoshii OT3."
Takagi H., Watanabe M., Kakuta Y., Kamachi R., Numata T., Tanaka I., Kimura M.
Biochem. Biophys. Res. Commun. 319:787-794(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), MUTAGENESIS OF LYS-42; ARG-68; ARG-87; ARG-90; ASP-98; ARG-107; HIS-114; LYS-123; LYS-158; ARG-176; ASP-180 AND LYS-196.
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
[6]"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 RNP2, SUBUNIT.
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000001 Genomic DNA. Translation: BAA30999.1.
PIRH71200.
RefSeqNP_143706.1. NC_000961.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1V77X-ray1.80A1-212[»]
2CZVX-ray2.00A/B1-212[»]
ProteinModelPortalO59543.
SMRO59543. Positions 2-209.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO59543. 1 interaction.
STRING70601.PH1877.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA30999; BAA30999; BAA30999.
GeneID1442721.
KEGGpho:PH1877.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1603.
HOGENOMHOG000073988.
KOK03539.
OMADALISPW.

Enzyme and pathway databases

BioCycPHOR70601:GJWR-1877-MONOMER.

Family and domain databases

HAMAPMF_00756. RNase_P_3.
InterProIPR016195. Pol/histidinol_Pase-like.
IPR023539. RNase_P_comp-3_arc.
IPR002738. RNase_P_p30.
[Graphical view]
PANTHERPTHR13031. PTHR13031. 1 hit.
PfamPF01876. RNase_P_p30. 1 hit.
[Graphical view]
SUPFAMSSF89550. SSF89550. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO59543.

Entry information

Entry nameRNP3_PYRHO
AccessionPrimary (citable) accession number: O59543
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 85 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