Q8U007 (RNP1_PYRFU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 58.
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 1 Short name=RNase P component 1 EC=3.1.26.5 | ||||
| Gene names |
| ||||
| Organism | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 186497 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus › ![]() |
Protein attributes
| Sequence length | 127 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends By similarity. HAMAP-Rule MF_00754 |
| Catalytic activity | Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. HAMAP-Rule MF_00754 |
| Subunit structure | Consists of a catalytic RNA component and at least 4 protein subunits Potential. |
| Sequence similarities | Belongs to the eukaryotic/archaeal RNase P protein component 1 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | tRNA processing |
| Molecular function | Hydrolase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | mRNA cleavage Inferred from electronic annotation. Source: InterPro rRNA processingInferred from electronic annotation. Source: InterPro tRNA 5'-leader removalInferred from electronic annotation. Source: HAMAP |
| Cellular_component | ribonuclease MRP complex Inferred from electronic annotation. Source: InterPro ribonuclease P complexInferred from electronic annotation. Source: InterPro |
| Molecular_function | RNA binding Inferred from electronic annotation. Source: InterPro ribonuclease P activityInferred 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 – 127 | 127 | Ribonuclease P protein component 1 HAMAP-Rule MF_00754 | PRO_0000128436 | ||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||
| Turn | 20 – 22 | 3 | ||||||||||||||||||||||||||||||
| Beta strand | 23 – 25 | 3 | ||||||||||||||||||||||||||||||
| Helix | 27 – 31 | 5 | ||||||||||||||||||||||||||||||
| Helix | 40 – 43 | 4 | ||||||||||||||||||||||||||||||
| Beta strand | 52 – 59 | 8 | ||||||||||||||||||||||||||||||
| Turn | 61 – 65 | 5 | ||||||||||||||||||||||||||||||
| Beta strand | 66 – 74 | 9 | ||||||||||||||||||||||||||||||
| Beta strand | 77 – 82 | 6 | ||||||||||||||||||||||||||||||
| Beta strand | 85 – 88 | 4 | ||||||||||||||||||||||||||||||
| Beta strand | 91 – 100 | 10 | ||||||||||||||||||||||||||||||
| Turn | 101 – 103 | 3 | ||||||||||||||||||||||||||||||
| Turn | 110 – 113 | 4 | ||||||||||||||||||||||||||||||
| Helix | 117 – 121 | 5 | ||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences." Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T. Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AE009950 Genomic DNA. Translation: AAL81940.1. | ||||||||||||
| RefSeq | NP_579545.1. NC_003413.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q8U007. | ||||||||||||
| SMR | Q8U007. Positions 36-127. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | 186497.PF1816. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | Q8U007. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | AAL81940; AAL81940; PF1816. | ||||||||||||
| GeneID | 1469695. | ||||||||||||
| KEGG | pfu:PF1816. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG1588. | ||||||||||||
| HOGENOM | HOG000231353. | ||||||||||||
| KO | K03538. | ||||||||||||
| OMA | PEMRLKK. | ||||||||||||
| ProtClustDB | PRK03879. | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 2.30.30.210. 1 hit. | ||||||||||||
| HAMAP | MF_00754. RNase_P_1. | ||||||||||||
| InterPro | IPR002730. RNase_P/MRP_p29. IPR023538. RNase_P_comp-1. IPR023534. Rof/RNase_P-like. [Graphical view] | ||||||||||||
| Pfam | PF01868. UPF0086. 1 hit. [Graphical view] | ||||||||||||
| SMART | SM00538. POP4. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF101744. RNase_P_Rpp29. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | Q8U007. | ||||||||||||
Entry information
| Entry name | RNP1_PYRFU | ||||||||
| Accession | Primary (citable) accession number: Q8U007 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
