Reviewed,
UniProtKB/Swiss-Prot Q9X0I6 (RNC_THEMA)
Last modified
November 3, 2009.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
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 | Thermotoga maritima [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 2336 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga |
Protein attributes
| Sequence length | 240 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
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 | 3D-structure 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 – 240 | 240 | Ribonuclease 3 HAMAP MF_00104 | PRO_0000180448 | ||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||
| Domain | 9 – 141 | 133 | RNase III | |||||||||||||||||||||||||||||||||||||
| Domain | 168 – 237 | 70 | DRBM | |||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||
| Helix | 3 – 16 | 14 | ||||||||||||||||||||||||||||||||||||||
| Helix | 23 – 30 | 8 | ||||||||||||||||||||||||||||||||||||||
| Helix | 33 – 41 | 9 | ||||||||||||||||||||||||||||||||||||||
| Helix | 51 – 72 | 22 | ||||||||||||||||||||||||||||||||||||||
| Helix | 78 – 88 | 11 | ||||||||||||||||||||||||||||||||||||||
| Helix | 91 – 100 | 10 | ||||||||||||||||||||||||||||||||||||||
| Helix | 103 – 106 | 4 | ||||||||||||||||||||||||||||||||||||||
| Helix | 111 – 115 | 5 | ||||||||||||||||||||||||||||||||||||||
| Helix | 118 – 120 | 3 | ||||||||||||||||||||||||||||||||||||||
| Helix | 122 – 140 | 19 | ||||||||||||||||||||||||||||||||||||||
| Helix | 142 – 161 | 20 | ||||||||||||||||||||||||||||||||||||||
| Helix | 169 – 181 | 13 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 186 – 193 | 8 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 200 – 207 | 8 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 210 – 219 | 10 | ||||||||||||||||||||||||||||||||||||||
| Helix | 220 – 235 | 16 | ||||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. Fraser C.M.Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AE000512 Genomic DNA. Translation: AAD36178.1. | |||||||||||||
| PIR | H72294. | ||||||||||||
| RefSeq | NP_228908.1. | ||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| ModBase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 898663. | ||||||||||||
| GenomeReviews | Gene locus TM_1102 in contig AE000512_GR. | ||||||||||||
| KEGG | tma:TM1102. | ||||||||||||
| NMPDR | fig|243274.1.peg.1092. | ||||||||||||
| TIGR | TM_1102. | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | Q9X0I6. | ||||||||||||
| OMA | ALTHKSF | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | TMAR243274:TM_1102-MON. | ||||||||||||
| BRENDA | 3.1.26.3. 16699. | ||||||||||||
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_THEMA | ||||||||
| Accession | Primary (citable) accession number: Q9X0I6 | ||||||||
| 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


