Q7W912 (SYT_BORPA) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 63.
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: Threonine--tRNA ligase EC=6.1.1.3 Alternative name(s): Threonyl-tRNA synthetase Short name=ThrRS | ||||
| Gene names |
| ||||
| Organism | Bordetella parapertussis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 519 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella |
Protein attributes
| Sequence length | 649 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). HAMAP MF_00184 |
| Cofactor | Binds 1 zinc ion per subunit By similarity. HAMAP MF_00184 |
| Subunit structure | Homodimer By similarity. HAMAP MF_00184 |
| Subcellular location | |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Metal-binding Nucleotide-binding Zinc |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | threonyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW threonine-tRNA ligase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 649 | 649 | Threonine--tRNA ligase HAMAP MF_00184 | PRO_1000020348 | |||||
Regions | |||||||||
| Region | 247 – 538 | 292 | Catalytic HAMAP MF_00184 | ||||||
Sites | |||||||||
| Metal binding | 338 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 389 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 515 | 1 | Zinc; catalytic By similarity | ||||||
Sequences
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References
| [1] | "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. Maskell D.J.Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 12822 / ATCC BAA-587 / NCTC 13253. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX640429 Genomic DNA. Translation: CAE37262.1. |
| RefSeq | NP_884223.1. NC_002928.3. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1EVL based on UniProtKB P0A8M3. |
| ProteinModelPortal | Q7W912. |
| SMR | Q7W912. Positions 246-640. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1667920. |
| GenomeReviews | Gene locus BPP1963 in contig BX470249_GR. |
| KEGG | bpa:BPP1963. |
| PATRIC | 21147740. VBIBorPar43418_2068. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG352811. |
| OMA | MIIRNIL. |
| PhylomeDB | Q7W912. |
| ProtClustDB | PRK00413. |
Enzyme and pathway databases | |
| BioCyc | BPAR257311:BPP1963-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00184. Thr_tRNA_synth. [Tree] |
| InterPro | IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II. IPR004154. Anticodon-bd. IPR012675. Beta-grasp_ferredoxin-type. IPR004095. TGS. IPR012676. TGS-like. IPR002320. Thr-tRNA-synth_IIa. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view] |
| Gene3D | G3DSA:3.40.50.800. Anticodon_bd. 1 hit. G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit. |
| KO | K01868. |
| Pfam | PF03129. HGTP_anticodon. 1 hit. PF02824. TGS. 1 hit. PF00587. tRNA-synt_2b. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view] |
| PRINTS | PR01047. TRNASYNTHTHR. |
| SMART | SM00863. tRNA_SAD. 1 hit. [Graphical view] |
| SUPFAM | SSF52954. Anticodon_bd. 1 hit. SSF81271. TGS-like. 1 hit. SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit. |
| TIGRFAMs | TIGR00418. ThrS. 1 hit. |
| PROSITE | PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYT_BORPA | ||||||||
| Accession | Primary (citable) accession number: Q7W912 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| SIMILARITY comments Index of protein domains and families |

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