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O26783 (RNP2_METTH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 2

Short name=RNase P component 2
EC=3.1.26.5
Alternative name(s):
Pop5
Gene names
Name:rnp2
Ordered Locus Names:MTH_687
OrganismMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) [Reference proteome] [HAMAP]
Taxonomic identifier187420 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length124 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

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 4-5 protein subunits. Ref.2

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00755.

Induction

Constitutively expressed (at protein level). Ref.2

Sequence similarities

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

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtRNA 5'-leader removal

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

ribonuclease P complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionribonuclease P activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 124124Ribonuclease P protein component 2 HAMAP-Rule MF_00755
PRO_0000140024

Sequences

Sequence LengthMass (Da)Tools
O26783 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 5034454559C101A6

FASTA12414,568
        10         20         30         40         50         60 
MKILPPTLRV PRRYIAFEVI SERELSREEL VSLIWDSCLK LHGECETSNF RLWLMKLWRF 

        70         80         90        100        110        120 
DFPDAVRVRG ILQCQRGYER RVMMALTCAH HHSGVRVAIH ILGLSGTIRS ATQKFIKPSK 


KDKY 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
[2]"Archaeal RNase P has multiple protein subunits homologous to eukaryotic nuclear RNase P proteins."
Hall T.A., Brown J.W.
RNA 8:296-306(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INDUCTION.
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000666 Genomic DNA. Translation: AAB85192.1.
PIRE69191.
RefSeqNP_275830.1. NC_000916.1.

3D structure databases

ProteinModelPortalO26783.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO26783. 1 interaction.
STRING187420.MTH687.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB85192; AAB85192; MTH_687.
GeneID1470648.
KEGGmth:MTH687.

Phylogenomic databases

eggNOGCOG1369.
KOK03537.
OMANPWLIDY.

Enzyme and pathway databases

BioCycMTHE187420:GJNM-689-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...

Entry information

Entry nameRNP2_METTH
AccessionPrimary (citable) accession number: O26783
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 71 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