Reviewed,
UniProtKB/Swiss-Prot P0A0H5 (RNPA_STAAU)
Last modified
September 22, 2009.
Version 19.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended 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 |
| ||
| Organism | Staphylococcus aureus | ||
| Taxonomic identifier | 1280 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 117 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
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. 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. HAMAP MF_00227 |
| Sequence similarities | Belongs to the rnpA family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | tRNA processing |
| Ligand | RNA-binding |
| Molecular function | Endonuclease Hydrolase Nuclease |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | tRNA 5'-leader removal Inferred from electronic annotation. Source: HAMAP |
| Molecular function | ribonuclease P activity Inferred from electronic annotation. Source: HAMAP tRNA bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 117 | 117 | Ribonuclease P protein component HAMAP MF_00227 | PRO_0000198530 | ||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||
| Helix | 5 – 7 | 3 | ||||||||||||||||||||||||||||||
| Helix | 13 – 21 | 9 | ||||||||||||||||||||||||||||||
| Beta strand | 27 – 31 | 5 | ||||||||||||||||||||||||||||||
| Beta strand | 45 – 48 | 4 | ||||||||||||||||||||||||||||||
| Beta strand | 51 – 53 | 3 | ||||||||||||||||||||||||||||||
| Helix | 58 – 72 | 15 | ||||||||||||||||||||||||||||||
| Helix | 73 – 75 | 3 | ||||||||||||||||||||||||||||||
| Beta strand | 82 – 86 | 5 | ||||||||||||||||||||||||||||||
| Helix | 89 – 92 | 4 | ||||||||||||||||||||||||||||||
| Helix | 97 – 102 | 6 | ||||||||||||||||||||||||||||||
| Helix | 105 – 109 | 5 | ||||||||||||||||||||||||||||||
| Beta strand | 112 – 114 | 3 | ||||||||||||||||||||||||||||||
Sequences
References
| [1] | "Cloning and characterization of Staphylococcus aureus ribonuclease P." Poppe S.M., Swaney S.M., Choi G.H., Hromockyj A., Shinabarger D.L. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ISP3. |
| [2] | "The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA." Spitzfaden C., Nicholson N., Jones J.J., Guth S., Lehr R., Prescott C.D., Hegg L.A., Eggleston D.S. J. Mol. Biol. 295:105-115(2000) [PubMed: 10623511] [Abstract] Cited for: STRUCTURE BY NMR. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AF135268 Genomic DNA. Translation: AAF61418.1. | |||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 3.1.26.5. 95. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_00227. [Tree] | ||||||||||||
| InterPro | IPR014721. Ribosomal_S5_D2-typ_fold_subgr. IPR000100. RNase_P. IPR020539. RNase_P_CS. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit. | ||||||||||||
| Pfam | PF00825. Ribonuclease_P. 1 hit. [Graphical view] | ||||||||||||
| ProDom | PD003629. Ribonuclease_P. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| TIGRFAMs | TIGR00188. rnpA. 1 hit. | ||||||||||||
| PROSITE | PS00648. RIBONUCLEASE_P. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | RNPA_STAAU | ||||||||
| Accession | Primary (citable) accession number: P0A0H5 Secondary accession number(s): P58031, Q9LAH9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


