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P60780 (RNP2_METMP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. 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:MMP0878
OrganismMethanococcus maripaludis (strain S2 / LL) [Complete proteome] [HAMAP]
Taxonomic identifier267377 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

Protein attributes

Sequence length130 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 5 protein subunits. Ref.2

Subcellular location

Cytoplasm Ref.2.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

kcat 10 min(-1) in absence of L7Ae, 63 min(-1) in presence of L7Ae. Kinetic parameters determined at 37 degrees Celsius.

KM=2.6 µM for pre-tRNA-Tyr in the absence of L7Ae Ref.2

KM=0.044 µM for pre-tRNA-Tyr in the presence of L7Ae

Temperature dependence:

Optimum temperature is 36-38 degrees Celsius in the absence of L7Ae, 48-50 degrees Celsius in presence of L7Ae.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processRNA phosphodiester bond hydrolysis

Inferred from direct assay Ref.2. Source: GOC

RNA phosphodiester bond hydrolysis, endonucleolytic

Inferred from direct assay Ref.2. Source: GOC

tRNA 5'-leader removal

Inferred from direct assay Ref.2. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.2. Source: UniProtKB

ribonuclease P complex

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionribonuclease P activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 130130Ribonuclease P protein component 2 HAMAP-Rule MF_00755
PRO_0000140023

Sequences

Sequence LengthMass (Da)Tools
P60780 [UniParc].

Last modified April 13, 2004. Version 1.
Checksum: F886926B406FCA75

FASTA13015,149
        10         20         30         40         50         60 
MLKTLPPTLR EKKRYVALEI IYEMELSQKD VISVVRNALL NYSGVLGCSR TNPWLIDYGH 

        70         80         90        100        110        120 
PYGILRISRE EVDTLRSSLS LMGEHKKKPI NIRIIGISNS VKHIREKFLH VPHEPYYKVI 

       130 
QKLKRKGPKK 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis."
Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J., Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M., Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A., Moore B.C. expand/collapse author list , Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D., Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W., Olson M.V., Leigh J.A.
J. Bacteriol. 186:6956-6969(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S2 / LL.
[2]"Ribosomal protein L7Ae is a subunit of archaeal RNase P."
Cho I.M., Lai L.B., Susanti D., Mukhopadhyay B., Gopalan V.
Proc. Natl. Acad. Sci. U.S.A. 107:14573-14578(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.
Strain: S2 / LL.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX950229 Genomic DNA. Translation: CAF30434.1.
RefSeqNP_987998.1. NC_005791.1.

3D structure databases

ProteinModelPortalP60780.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59368N.
STRING267377.MMP0878.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF30434; CAF30434; MMP0878.
GeneID2762695.
KEGGmmp:MMP0878.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1369.
HOGENOMHOG000286243.
KOK03537.
OMANPWLIDY.

Enzyme and pathway databases

BioCycMMAR267377:GJ77-908-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_METMP
AccessionPrimary (citable) accession number: P60780
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: May 14, 2014
This is version 49 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