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O59425 (RNP1_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease P protein component 1

Short name=RNase P component 1
EC=3.1.26.5
Alternative name(s):
Rpp29
Gene names
Name:rnp1
Ordered Locus Names:PH1771
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length127 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of ribonuclease P (RNase P), a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Binds RNase P RNA. Ref.2 Ref.3 Ref.4 Ref.6

Catalytic activity

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. HAMAP-Rule MF_00754

Subunit structure

Consists of a catalytic RNA component and at least 5 protein subunits. Forms a heterodimeric subcomplex with Rnp4. 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_00754.

Sequence similarities

Belongs to the eukaryotic/archaeal RNase P protein component 1 family.

Biophysicochemical properties

Temperature dependence:

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 127127Ribonuclease P protein component 1 HAMAP-Rule MF_00754
PRO_0000128437

Experimental info

Mutagenesis1 – 3131Missing: Does not reconstitute RNase P activity, no longer interacts with Rnp4. Ref.6
Mutagenesis471E → A: Fully reconstitutes RNase P activity. Ref.6
Mutagenesis731E → A: 40% reconstituted RNase P activity. Ref.6
Mutagenesis751R → A: 40% reconstituted RNase P activity. Ref.6
Mutagenesis901K → A: 10% reconstituted RNase P activity. Ref.6
Mutagenesis951F → A: 75% reconstituted RNase P activity. Ref.6
Mutagenesis1151R → A: 75% reconstituted RNase P activity. Ref.6
Mutagenesis118 – 12710Missing: Does not reconstitute RNase P activity. Ref.6
Mutagenesis121 – 1222KK → AA: 60% reconstituted RNase P activity. Ref.6
Mutagenesis1211K → A: 90% reconstituted RNase P activity. Ref.6
Mutagenesis1221K → A: Fully reconstitutes RNase P activity. Ref.6
Mutagenesis124 – 1274Missing: Fully reconstitutes RNase P activity. Ref.6

Secondary structure

....................... 127
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O59425 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 840FE2A1234FF0AD

FASTA12715,054
        10         20         30         40         50         60 
MRRNSKERKN RATRRSQGSY QEIIGRTWIF RGAHRGRVTR RNIIWHELIG LRVRIVGSTH 

        70         80         90        100        110        120 
PAFVGIEGYV IDETRNMLVI AGDRIWKVPK DVCIFEFEAD DGTKIKIPGE RLVGRPEMRL 


KKRWKKW 

« 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 archaeal ribonuclease P protein Ph1771p from Pyrococcus horikoshii OT3: an archaeal homolog of eukaryotic ribonuclease P protein Rpp29."
Numata T., Ishimatsu I., Kakuta Y., Tanaka I., Kimura M.
RNA 10:1423-1432(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 32-127.
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
[6]"Structure of an archaeal homolog of the human protein complex Rpp21-Rpp29 that is a key core component for the assembly of active ribonuclease P."
Honda T., Kakuta Y., Kimura K., Saho J., Kimura M.
J. Mol. Biol. 384:652-662(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) IN COMPLEX WITH RNP4, FUNCTION, SUBUNIT, MUTAGENESIS OF 1-MET--ARG-31; GLU-47; GLU-73; ARG-75; LYS-90; PHE-95; ARG-115; 118-MET--TRP-127; LYS-121; 121-LYS-LYS-122; LYS-122 AND 124-TRP--TRP-127.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000001 Genomic DNA. Translation: BAA30886.1.
PIRG71186.
RefSeqNP_143607.1. NC_000961.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1V76X-ray2.00A/B32-127[»]
2ZAEX-ray2.21A/C1-127[»]
ProteinModelPortalO59425.
SMRO59425. Positions 36-127.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO59425. 1 interaction.
STRING70601.PH1771.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA30886; BAA30886; BAA30886.
GeneID1442614.
KEGGpho:PH1771.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1588.
HOGENOMHOG000231353.
KOK03538.
OMAISTKGRV.

Enzyme and pathway databases

BioCycPHOR70601:GJWR-1769-MONOMER.

Family and domain databases

Gene3D2.30.30.210. 1 hit.
HAMAPMF_00754. RNase_P_1.
InterProIPR002730. RNase_P/MRP_p29.
IPR023538. RNase_P_comp-1.
IPR023534. Rof/RNase_P-like.
[Graphical view]
PfamPF01868. UPF0086. 1 hit.
[Graphical view]
SMARTSM00538. POP4. 1 hit.
[Graphical view]
SUPFAMSSF101744. SSF101744. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO59425.

Entry information

Entry nameRNP1_PYRHO
AccessionPrimary (citable) accession number: O59425
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 87 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