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O26784 (RNP3_METTH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. 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 3

Short name=RNase P component 3
EC=3.1.26.5
Alternative name(s):
Rpp30
Gene names
Name:rnp3
Ordered Locus Names:MTH_688
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 length245 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_00756

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_00756.

Induction

Constitutively expressed (at protein level). Ref.2

Sequence similarities

Belongs to the eukaryotic/archaeal RNase P protein component 3 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 – 245245Ribonuclease P protein component 3 HAMAP-Rule MF_00756
PRO_0000140043

Sequences

Sequence LengthMass (Da)Tools
O26784 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: B86C15C0495F957E

FASTA24527,680
        10         20         30         40         50         60 
MIPQRILMKF FDFHIQGRDH DSSLRLLLEA SRLGYQGGVL VYPSERYPDL KSDLESLREN 

        70         80         90        100        110        120 
PELQDFEIAR GVMINASDPR DMRRSVNKFR KKADVIYVSG GNLKVNRAAC ESRRVDVLSA 

       130        140        150        160        170        180 
PYTSRRDPGI NHVLAREAAR NNVAVELPLA DVIGSWLKVR ARVLEQFREI LKLHRKFGFP 

       190        200        210        220        230        240 
LLLTSRASSI YDLRTPGDIM NLAECFGMES SEAEESLTST PASILEDSGN RHLLIAEGVR 


LLPES 

« 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: AAB85193.1.
PIRF69191.
RefSeqNP_275831.1. NC_000916.1.

3D structure databases

ProteinModelPortalO26784.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO26784. 1 interaction.
STRING187420.MTH688.

Proteomic databases

PRIDEO26784.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB85193; AAB85193; MTH_688.
GeneID1470649.
KEGGmth:MTH688.

Phylogenomic databases

eggNOGCOG1603.
KOK03539.
OMASSRQMKF.

Enzyme and pathway databases

BioCycMTHE187420:GJNM-690-MONOMER.

Family and domain databases

HAMAPMF_00756. RNase_P_3.
InterProIPR016195. Pol/histidinol_Pase-like.
IPR023539. RNase_P_comp-3_arc.
IPR002738. RNase_P_p30.
[Graphical view]
PANTHERPTHR13031. PTHR13031. 1 hit.
PfamPF01876. RNase_P_p30. 1 hit.
[Graphical view]
SUPFAMSSF89550. SSF89550. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRNP3_METTH
AccessionPrimary (citable) accession number: O26784
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 79 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