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Reviewed, UniProtKB/Swiss-Prot P29433 (RNPA_BUCAP)

Last modified November 24, 2009. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ribonuclease P protein component
      Short name=RNaseP protein
      Short name=RNase P protein
    EC=3.1.26.5
Alternative name(s):
    Protein C5
Gene names
Name: rnpA
Ordered Locus Names: BUsg_014
OrganismBuchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]
Taxonomic identifier98794 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length114 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme By similarity.

Catalytic activity

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. HAMAP MF_00227

Subunit structure

Consists of a catalytic RNA component (M1 or rnpB) and a protein subunit By similarity.

Sequence similarities

Belongs to the rnpA family.

Ontologies

Keywords
   Biological processtRNA processing
   LigandRNA-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical termComplete 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

tRNA binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 114114Ribonuclease P protein component HAMAP MF_00227
PRO_0000198436

Sequences

Sequence LengthMass (Da)Tools
P29433-1 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 3FFFFDA2262D95CA

FASTA11413,784
        10         20         30         40         50         60 
MLNYFFKKKS KLLKSTNFQY VFSNPCNKNT FHINILGRSN LLGHPRLGLS ISRKNIKHAY 

        70         80         90        100        110 
RRNKIKRLIR ETFRLLQHRL ISMDFVVIAK KNIVYLNNKK IVNILEYIWS NYQR 

« Hide

References

« Hide 'large scale' references
[1]"Genetic analysis of an aphid endosymbiont DNA fragment homologous to the rnpA-rpmH-dnaA-dnaN-gyrB region of eubacteria."
Lai C.-Y., Baumann P.
Gene 113:175-181(1992) [PubMed: 1572539] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence analysis of a 34.7-kb DNA segment from the genome of Buchnera aphidicola (endosymbiont of aphids) containing groEL, dnaA, the atp operon, gidA, and rho."
Clark M.A., Baumann L., Baumann P.
Curr. Microbiol. 36:158-163(1998) [PubMed: 9516544] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

M80817 Genomic DNA. Translation: AAA73147.1.
AF008210 Genomic DNA. Translation: AAC38104.1.
AE013218 Genomic DNA. Translation: AAM67586.1.
PIRJC1155.
RefSeqNP_660375.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1005830.
GenomeReviewsGene locus BUsg_014 in contig AE013218_GR.
KEGGbas:BUsg014.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP29433.
OMAPRIGLAI

Enzyme and pathway databases

BioCycBAPH198804:BUSG014-MON.

Family and domain databases

HAMAPMF_00227.
[Tree]
InterProIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000100. RNase_P.
IPR020539. RNase_P_CS.
[Graphical view]
Gene3DG3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.
PfamPF00825. Ribonuclease_P. 1 hit.
[Graphical view]
ProDomPD003629. Ribonuclease_P. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00188. rnpA. 1 hit.
PROSITEPS00648. RIBONUCLEASE_P. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRNPA_BUCAP
AccessionPrimary (citable) accession number: P29433
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: November 24, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents