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O59248 (RNP4_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribonuclease P protein component 4
Short name=RNase P component 4
EC=3.1.26.5
Gene names
Name:rnp4
Ordered Locus Names:PH1601
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus ›

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 By similarity. HAMAP-Rule MF_00757

Catalytic activity

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. HAMAP-Rule MF_00757

Subunit structure

Consists of a catalytic RNA component and at least 4 protein subunits Potential.

Sequence similarities

Belongs to the eukaryotic/archaeal RNase P protein component 4 family.

Ontologies

Keywords
   Biological processtRNA processing
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processtRNA 5'-leader removal

Inferred from electronic annotation. Source: InterPro

   Molecular_functionribonuclease P activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

rnp2O591503EBI-2641275,EBI-2603177

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 120120Ribonuclease P protein component 4 HAMAP-Rule MF_00757
PRO_0000153860

Secondary structure

1 ................... 120
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O59248 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 2AC453B35C964AE6

FASTA12014,589
        10         20         30         40         50         60 
MVDIVKRRDW EKKEKKKIAI ERIDTLFTLA ERVARYSPDL AKRYVELALE IQKKAKVKIP 

        70         80         90        100        110        120 
RKWKRRYCKR CHTFLIPGVN ARVRLRTKRM PHVVITCLEC GYIMRYPYLR EVKQKRKKAT

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000001 Genomic DNA. Translation: BAA30713.1.
PIRA71039.
RefSeqNP_143456.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X0TX-ray1.60A1-120[»]
2ZAEX-ray2.21B/D1-120[»]
ProteinModelPortalO59248.
SMRO59248. Positions 4-109.
ModBaseSearch...

Protein-protein interaction databases

IntActO59248. 2 interactions.
STRING70601.PH1601.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA30713; BAA30713; BAA30713.
GeneID1442455.
KEGGpho:PH1601.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2023.
HOGENOMHOG000230709.
KOK03540.
OMAPRKWKRR.
ProtClustDBPRK03954.

Enzyme and pathway databases

BioCycPHOR70601:GJWR-1604-MONOMER.

Family and domain databases

HAMAPMF_00757. RNase_P_4.
InterProIPR016432. RNase_P_comp-4.
IPR007175. Rpr2.
[Graphical view]
PANTHERPTHR14742. PTHR14742. 1 hit.
PfamPF04032. Rpr2. 1 hit.
[Graphical view]
PIRSFPIRSF004878. RNase_P_4. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO59248.

Entry information

Entry nameRNP4_PYRHO
AccessionPrimary (citable) accession number: O59248
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: August 1, 1998
Last modified: May 29, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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