Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q821V0 (RNPA_CHLCV) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 62. 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:CCA_00835
OrganismChlamydophila caviae (strain GPIC) [Complete proteome] [HAMAP]
Taxonomic identifier227941 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

Protein attributes

Sequence length139 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-Rule MF_00227

Catalytic activity

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. HAMAP-Rule 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: UniProtKB-EC

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 139139Ribonuclease P protein component HAMAP-Rule MF_00227
PRO_0000198444

Sequences

Sequence LengthMass (Da)Tools
Q821V0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: F4A28E28FE4C992D

FASTA13915,948
        10         20         30         40         50         60 
MHRSTLPKYA RVLKRKQFLY ISRAGSHCQG SQVIFHVAPS RYSGCCKLGI TVSKKFGKAH 

        70         80         90        100        110        120 
KRNYFKRIVR EAFRKKRHSL PACQIVVMPK NKQQPKFEDL LQDFAQQIPE ALSSKLAKNK 

       130 
PTTGVEYSPK NEKCESVLP 

« Hide

References

[1]"Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae."
Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G. expand/collapse author list , Rank R.G., Bavoil P.M., Fraser C.M.
Nucleic Acids Res. 31:2134-2147(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GPIC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015925 Genomic DNA. Translation: AAP05576.1.
RefSeqNP_829698.1. NC_003361.3.

3D structure databases

ProteinModelPortalQ821V0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227941.CCA00835.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP05576; AAP05576; CCA_00835.
GeneID1218520.
KEGGcca:CCA00835.
PATRIC20270807. VBIChlCav107360_0883.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0594.
KOK03536.
OMAQFLYISR.
OrthoDBEOG6XWV8K.
ProtClustDBPRK00730.

Enzyme and pathway databases

BioCycCCAV227941:GH8L-868-MONOMER.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
HAMAPMF_00227. RNase_P.
InterProIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000100. RNase_P.
IPR020539. RNase_P_CS.
[Graphical view]
PfamPF00825. Ribonuclease_P. 1 hit.
[Graphical view]
ProDomPD003629. Ribonuclease_P. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF54211. SSF54211. 1 hit.
TIGRFAMsTIGR00188. rnpA. 1 hit.
PROSITEPS00648. RIBONUCLEASE_P. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRNPA_CHLCV
AccessionPrimary (citable) accession number: Q821V0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 62 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