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

P48206 (RNPA_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. 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:SCO3881
ORF Names:STH24.03
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length123 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
Reference 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 – 123123Ribonuclease P protein component HAMAP-Rule MF_00227
PRO_0000198538

Sequences

Sequence LengthMass (Da)Tools
P48206 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 0D4D4E26A20B6C39

FASTA12313,320
        10         20         30         40         50         60 
MLPTENRLRR REDFATAVRR GRRVGRSTLV VHLRSGATDP HAPGESAPRT RAGFVVSKAV 

        70         80         90        100        110        120 
GVAVVRNKVK RRLRHLMRDR IDLLPPGSLV VVRALPGAGD ADHAQLARDL DAALARLLGG 


GAR 

« Hide

References

« Hide 'large scale' references
[1]"Conserved gene arrangement in the origin region of the Streptomyces coelicolor chromosome."
Calcutt M.J., Schmidt F.J.
J. Bacteriol. 174:3220-3226(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A3(2) / NRRL B-16638.
[2]"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)."
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. expand/collapse author list , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.
Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF187159 Genomic DNA. Translation: AAA26732.1.
AL939118 Genomic DNA. Translation: CAB42696.1.
PIRD41870.
RefSeqNP_628067.1. NC_003888.3.

3D structure databases

ProteinModelPortalP48206.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO3881.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB42696; CAB42696; CAB42696.
GeneID1099317.
KEGGsco:SCO3881.
PATRIC23737546. VBIStrCoe124346_3954.

Phylogenomic databases

HOGENOMHOG000266301.
KOK03536.
OMAMLPTENR.
OrthoDBEOG6XWV8K.
ProtClustDBCLSK902640.

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]
SUPFAMSSF54211. SSF54211. 1 hit.
TIGRFAMsTIGR00188. rnpA. 1 hit.
PROSITEPS00648. RIBONUCLEASE_P. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRNPA_STRCO
AccessionPrimary (citable) accession number: P48206
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 88 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