Q10628 (RNPH_MYCTU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 82.
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 PH Short name=RNase PH EC=2.7.7.56 Alternative name(s): tRNA nucleotidyltransferase | ||||||||
| Gene names |
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| Organism | Mycobacterium tuberculosis [Reference proteome] [HAMAP] | ||||||||
| Taxonomic identifier | 1773 [NCBI] | ||||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex![]() |
Protein attributes
| Sequence length | 259 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Phosphorolytic exoribonuclease that removes nucleotide residues following the -CCA terminus of tRNA and adds nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates By similarity. HAMAP-Rule MF_00564 |
| Catalytic activity | tRNA(n+1) + phosphate = tRNA(n) + a nucleoside diphosphate. HAMAP-Rule MF_00564 |
| Sequence similarities | Belongs to the RNase PH family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | tRNA processing |
| Molecular function | Nucleotidyltransferase Transferase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | tRNA processing Inferred from electronic annotation. Source: HAMAP |
| Cellular_component | plasma membrane Inferred from direct assay PubMed 14532352. Source: MTBBASE |
| Molecular_function | tRNA binding Inferred from electronic annotation. Source: HAMAP tRNA nucleotidyltransferase activityInferred from electronic annotation. Source: HAMAP tRNA-specific ribonuclease activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 259 | 259 | Ribonuclease PH HAMAP-Rule MF_00564 | PRO_0000139912 | ||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 16 – 20 | 5 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 22 – 34 | 13 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 37 – 48 | 12 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 60 – 67 | 8 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 69 – 71 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 72 – 74 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 79 – 82 | 4 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 87 – 101 | 15 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 106 – 109 | 4 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 111 – 122 | 12 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 127 – 148 | 22 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 153 – 155 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 162 – 170 | 9 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 173 – 177 | 5 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 180 – 183 | 4 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 187 – 195 | 9 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 200 – 205 | 6 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 214 – 239 | 26 | ||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G.Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv. |
| [2] | "Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M.J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | BX842576 Genomic DNA. Translation: CAA99973.1. AE000516 Genomic DNA. Translation: AAK45646.1. AL123456 Genomic DNA. Translation: CCP44098.1. | ||||||||||||
| PIR | C70739. | ||||||||||||
| RefSeq | NP_215856.1. NC_000962.3. NP_335832.1. NC_002755.2. YP_006514718.1. NC_018143.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | Q10628. | ||||||||||||
| SMR | Q10628. Positions 3-248. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | 83332.Rv1340. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | Q10628. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | AAK45646; AAK45646; MT1381. | ||||||||||||
| GeneID | 13319926. 886864. 924657. | ||||||||||||
| KEGG | mtc:MT1381. mtu:Rv1340. mtv:RVBD_1340. | ||||||||||||
| PATRIC | 18124810. VBIMycTub22151_1520. | ||||||||||||
Organism-specific databases | |||||||||||||
| TubercuList | Rv1340. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0689. | ||||||||||||
| HOGENOM | HOG000229516. | ||||||||||||
| KO | K00989. | ||||||||||||
| OMA | MLPRATG. | ||||||||||||
| ProtClustDB | PRK00173. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_00564. RNase_PH. | ||||||||||||
| InterPro | IPR001247. ExoRNase_PH_dom1. IPR015847. ExoRNase_PH_dom2. IPR020568. Ribosomal_S5_D2-typ_fold. IPR002381. RNase_PH_bac-type. IPR018336. RNase_PH_CS. [Graphical view] | ||||||||||||
| Pfam | PF01138. RNase_PH. 1 hit. PF03725. RNase_PH_C. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF55666. 3_ExoRNase. 1 hit. SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit. | ||||||||||||
| TIGRFAMs | TIGR01966. RNasePH. 1 hit. | ||||||||||||
| PROSITE | PS01277. RIBONUCLEASE_PH. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | Q10628. | ||||||||||||
Entry information
| Entry name | RNPH_MYCTU | ||||||||
| Accession | Primary (citable) accession number: Q10628 Secondary accession number(s): L0T9C5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
