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Q8U151 (RNP2_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 52. 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 2
Short name=RNase P component 2
EC=3.1.26.5
Gene names
Name:rnp2
Ordered Locus Names:PF1378
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [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_00755

Catalytic activity

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

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 2 family.

Ontologies

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

Inferred from electronic annotation. Source: HAMAP

   Molecular_functionribonuclease P activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 120120Ribonuclease P protein component 2 HAMAP-Rule MF_00755
PRO_0000140026

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8U151 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: B690DF4C26299915

FASTA12013,839
        10         20         30         40         50         60 
MSERPKTLPP TLRDKKRYIA FKVISENQFN KDEIKEAIWN ACLRTLGELG TAKAKPWLIK 

        70         80         90        100        110        120 
FDETTQTGII RCDRNHVYDV IFSLTLVSDI NGNKAIIKVL GVSGTIKRLK RKFLSQFGWR

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References

[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(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE009950 Genomic DNA. Translation: AAL81502.1.
RefSeqNP_579107.1. NC_003413.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AV5X-ray3.15A/B/C/D/E1-120[»]
ProteinModelPortalQ8U151.
SMRQ8U151. Positions 15-120.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8U151. 1 interaction.
STRING186497.PF1378.

Proteomic databases

PRIDEQ8U151.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL81502; AAL81502; PF1378.
GeneID1469254.
KEGGpfu:PF1378.

Phylogenomic databases

eggNOGCOG1369.
HOGENOMHOG000286243.
KOK03537.
OMANPWLIDY.
ProtClustDBPRK03717.

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

EvolutionaryTraceQ8U151.

Entry information

Entry nameRNP2_PYRFU
AccessionPrimary (citable) accession number: Q8U151
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2002
Last modified: May 1, 2013
This is version 52 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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