Reviewed,
UniProtKB/Swiss-Prot Q2YMC3 (RNH2_BRUA2)
Last modified
November 24, 2009.
Version 26.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Ribonuclease HII Short name=RNase HII EC=3.1.26.4 | ||||
| Gene names |
| ||||
| Organism | Brucella abortus (strain 2308) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 359391 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella |
Protein attributes
| Sequence length | 220 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Endonuclease that specifically degrades the RNA of RNA-DNA hybrids By similarity. |
| Catalytic activity | Endonucleolytic cleavage to 5'-phosphomonoester. HAMAP MF_00052 |
| Cofactor | Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding By similarity. |
| Subcellular location | Cytoplasm Potential. |
| Sequence similarities | Belongs to the RNase HII family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Manganese Metal-binding |
| Molecular function | Endonuclease Hydrolase Nuclease |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | RNA catabolic process Inferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | RNA binding Inferred from electronic annotation. Source: InterPro manganese ion bindingInferred from electronic annotation. Source: HAMAP ribonuclease H 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 – 220 | 220 | Ribonuclease HII HAMAP MF_00052 | PRO_0000235704 | |||||
Sites | |||||||||
| Metal binding | 38 | 1 | Divalent metal cation By similarity | ||||||
| Metal binding | 39 | 1 | Divalent metal cation By similarity | ||||||
| Metal binding | 130 | 1 | Divalent metal cation By similarity | ||||||
Sequences
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References
| [1] | "Whole-genome analyses of speciation events in pathogenic Brucellae." Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E. Infect. Immun. 73:8353-8361(2005) [PubMed: 16299333] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AM040264 Genomic DNA. Translation: CAJ10371.1. | |
| RefSeq | YP_413875.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q2YMC3. |
Genome annotation databases | |
| GeneID | 3788907. |
| GenomeReviews | Gene locus BAB1_0415 in contig AM040264_GR. |
| KEGG | bmf:BAB1_0415. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q2YMC3. |
| OMA | RLGPTPI |
Enzyme and pathway databases | |
| BioCyc | BMEL359391:BAB1_0415-MON. |
Family and domain databases | |
| HAMAP | MF_00052. [Tree] |
| InterPro | IPR012337. PolynucTfrase_RNaseH_fold. IPR001352. RNase_HII/HIII. [Graphical view] |
| PANTHER | PTHR10954. RNase_HII/HIII. 1 hit. |
| Pfam | PF01351. RNase_HII. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | RNH2_BRUA2 | ||||||||
| Accession | Primary (citable) accession number: Q2YMC3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Brucella abortus strain 2308 Brucella abortus (strain 2308): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

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