Reviewed,
UniProtKB/Swiss-Prot B0CKY7 (RNC_BRUSI)
Last modified
November 3, 2009.
Version 12.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Ribonuclease 3 EC=3.1.26.3 Alternative name(s): Ribonuclease III Short name=RNase III | ||||
| Gene names |
| ||||
| Organism | Brucella suis (strain ATCC 23445 / NCTC 10510) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 470137 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella |
Protein attributes
| Sequence length | 245 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Digests double-stranded RNA. Involved in the processing of ribosomal RNA precursors and of some mRNAs By similarity. |
| Catalytic activity | Endonucleolytic cleavage to 5'-phosphomonoester. HAMAP MF_00104 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Contains 1 DRBM (double-stranded RNA-binding) domain. Contains 1 RNase III domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | RNA-binding |
| Molecular function | Endonuclease Hydrolase Nuclease |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | mRNA processing Inferred from electronic annotation. Source: HAMAP rRNA catabolic processInferred from electronic annotation. Source: InterPro rRNA processingInferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | double-stranded RNA binding Inferred from electronic annotation. Source: InterPro ribonuclease III 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 – 245 | 245 | Ribonuclease 3 HAMAP MF_00104 | PRO_1000075730 | |||||
Regions | |||||||||
| Domain | 19 – 144 | 126 | RNase III | ||||||
| Domain | 169 – 238 | 70 | DRBM | ||||||
Sequences
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References
| [1] | "Brucella suis ATCC 23445 whole genome shotgun sequencing project." Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M., Snyder E.E. Brettin T.S.Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000911 Genomic DNA. Translation: ABY37767.1. | |
| RefSeq | YP_001627337.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5838657. |
| GenomeReviews | Gene locus BSUIS_A0689 in contig CP000911_GR. |
| KEGG | bmt:BSUIS_A0689. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | ALTHKSF. |
Family and domain databases | |
| HAMAP | MF_00104. [Tree] |
| InterPro | IPR001159. Ds-RNA_bd. IPR014720. dsRNA-bd-like. IPR000999. RNase_III. IPR011907. RNase_III_bac. [Graphical view] |
| Gene3D | G3DSA:3.30.160.20. dsRNA-bd-like. 1 hit. G3DSA:1.10.1520.10. RNase_III. 1 hit. |
| Pfam | PF00035. dsrm. 1 hit. PF00636. Ribonuclease_3. 1 hit. [Graphical view] |
| SMART | SM00358. DSRM. 1 hit. SM00535. RIBOc. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR02191. RNaseIII. 1 hit. |
| PROSITE | PS50137. DS_RBD. 1 hit. PS00517. RNASE_3_1. 1 hit. PS50142. RNASE_3_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | RNC_BRUSI | ||||||||
| Accession | Primary (citable) accession number: B0CKY7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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