A7GVQ0 (RNPA_BACCN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 43.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended 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 |
| ||||
| Organism | Bacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 315749 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › ![]() |
Protein attributes
| Sequence length | 115 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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 process | tRNA processing |
| Ligand | RNA-binding |
| Molecular function | Endonuclease Hydrolase Nuclease |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC tRNA 5'-leader removalInferred 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 – 115 | 115 | Ribonuclease P protein component HAMAP-Rule MF_00227 | PRO_1000078188 | |||
Sequences
References
| [1] | "Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity." Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A. Chem. Biol. Interact. 171:236-249(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NVH 391-98. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000764 Genomic DNA. Translation: ABS24208.1. |
| RefSeq | YP_001377203.1. NC_009674.1. |
3D structure databases | |
| ProteinModelPortal | A7GVQ0. |
| SMR | A7GVQ0. Positions 1-110. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 315749.Bcer98_4027. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABS24208; ABS24208; Bcer98_4027. |
| GeneID | 5343745. |
| KEGG | bcy:Bcer98_4027. |
| PATRIC | 18936803. VBIBacCyt128034_4212. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0594. |
| HOGENOM | HOG000266301. |
| KO | K03536. |
| OMA | DEFQAVF. |
| ProtClustDB | PRK00499. |
Enzyme and pathway databases | |
| BioCyc | BCYT315749:GH2A-4164-MONOMER. |
Family and domain databases | |
| Gene3D | 3.30.230.10. 1 hit. |
| HAMAP | MF_00227. RNase_P. |
| InterPro | IPR020568. Ribosomal_S5_D2-typ_fold. IPR014721. Ribosomal_S5_D2-typ_fold_subgr. IPR000100. RNase_P. IPR020539. RNase_P_CS. [Graphical view] |
| Pfam | PF00825. Ribonuclease_P. 1 hit. [Graphical view] |
| ProDom | PD003629. Ribonuclease_P. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SUPFAM | SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit. |
| TIGRFAMs | TIGR00188. rnpA. 1 hit. |
| PROSITE | PS00648. RIBONUCLEASE_P. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | RNPA_BACCN | ||||||||
| Accession | Primary (citable) accession number: A7GVQ0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
