Skip Header

Contribute Send feedback
Read comments (?) or add your own

P59413 (RNPA_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. 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

Short name=RNase P protein
Short name=RNaseP protein
EC=3.1.26.5
Alternative name(s):
Protein C5
Gene names
Name:rnpA
Ordered Locus Names:bbp_014
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length114 AA.
Sequence statusComplete.
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. HAMAP MF_00227

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 processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionribonuclease P activity

Inferred from electronic annotation. Source: EC

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 114114Ribonuclease P protein component HAMAP MF_00227
PRO_0000198437

Sequences

Sequence LengthMass (Da)Tools
P59413 [UniParc].

Last modified March 28, 2003. Version 1.
Checksum: 75EDAA043F1B1060

FASTA11413,761
        10         20         30         40         50         60 
MIEFYFNKKR RLITPNDFNY VFKSPNVIRC KEITILGRLN LLSFSRLGIS VSRKNVKYAY 

        70         80         90        100        110 
QRNKIKRLIR ENFRIIQHRL VSSDFVVIVN SSSMQISFKL LAKKLENLWS YYYQ 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO26758.1.
RefSeqNP_777653.1. NC_004545.1.

3D structure databases

ProteinModelPortalP59413.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBUCT00000002692; EBBUCP00000002516; EBBUCG00000002692.
GeneID1058533.
GenomeReviewsGene locus bbp_014 in contig AE016826_GR.
KEGGbab:bbp014.
PATRIC21244799. VBIBucAph80364_0015.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000008201.
HOGENOMHBG728160.
OMARKNIKHA.

Enzyme and pathway databases

BioCycBAPH224915:BBP_014-MONOMER.

Family and domain databases

HAMAPMF_00227. RNase_P.
[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.
KOK03536.
PfamPF00825. Ribonuclease_P. 1 hit.
[Graphical view]
ProDomPD003629. Ribonuclease_P. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
TIGRFAMsTIGR00188. RnpA. 1 hit.
PROSITEPS00648. RIBONUCLEASE_P. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRNPA_BUCBP
AccessionPrimary (citable) accession number: P59413
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: March 28, 2003
Last modified: January 25, 2012
This is version 55 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