Q67KZ3 (GLUQ_SYMTH) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 55.
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: Glutamyl-Q tRNA(Asp) synthetase Short name=Glu-Q-RSs EC=6.1.1.- | ||||
| Gene names |
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| Organism | Symbiobacterium thermophilum [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 2734 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiales Family XVIII. Incertae Sedis › Symbiobacterium |
Protein attributes
| Sequence length | 323 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon By similarity. HAMAP MF_01428 |
| Cofactor | Binds 1 zinc ion per subunit By similarity. HAMAP MF_01428 |
| Sequence similarities | Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. |
Ontologies
| Keywords | |
|---|---|
| Ligand | ATP-binding Metal-binding Nucleotide-binding Zinc |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glutamyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro tRNA modificationInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate-tRNA ligase activityInferred from electronic annotation. Source: InterPro metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 323 | 323 | Glutamyl-Q tRNA(Asp) synthetase HAMAP MF_01428 | PRO_0000208328 | |||||
Regions | |||||||||
| Region | 5 – 9 | 5 | Glutamate binding By similarity | ||||||
| Motif | 8 – 18 | 11 | "HIGH" region HAMAP MF_01428 | ||||||
| Motif | 249 – 253 | 5 | "KMSKS" region HAMAP MF_01428 | ||||||
Sites | |||||||||
| Metal binding | 105 | 1 | Zinc By similarity | ||||||
| Metal binding | 107 | 1 | Zinc By similarity | ||||||
| Metal binding | 129 | 1 | Zinc By similarity | ||||||
| Metal binding | 133 | 1 | Zinc By similarity | ||||||
| Binding site | 41 | 1 | Glutamate By similarity | ||||||
| Binding site | 193 | 1 | Glutamate By similarity | ||||||
| Binding site | 211 | 1 | Glutamate By similarity | ||||||
| Binding site | 252 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism." Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T. Nucleic Acids Res. 32:4937-4944(2004) [PubMed: 15383646] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: T / IAM 14863. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AP006840 Genomic DNA. Translation: BAD41653.1. |
| RefSeq | YP_076497.1. NC_006177.1. |
3D structure databases | |
| ProteinModelPortal | Q67KZ3. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2980023. |
| GenomeReviews | Gene locus STH2668 in contig AP006840_GR. |
| KEGG | sth:STH2668. |
| NMPDR | fig|292459.1.peg.2556. |
| PATRIC | 23783512. VBISymThe116959_2661. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG628189. |
| OMA | LAPPRFA. |
| ProtClustDB | PRK05710. |
Enzyme and pathway databases | |
| BioCyc | STHE292459:STH2668-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01428. Glu_Q_tRNA_synth. [Tree] |
| InterPro | IPR001412. aa-tRNA-synth_I_CS. IPR022380. Glu-Q_TRNA(Asp)_Synthase. IPR004527. Glu-tRNA-synth_Ib_bac/mito. IPR000924. Glu/Gln-tRNA-synth_Ib. IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl. IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view] |
| Gene3D | G3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits. |
| KO | K01885. |
| PANTHER | PTHR10119. Glu_tRNA-synt_1c. 1 hit. PTHR10119:SF1. PTHR10119:SF1. 1 hit. |
| Pfam | PF00749. tRNA-synt_1c. 1 hit. [Graphical view] |
| PRINTS | PR00987. TRNASYNTHGLU. |
| TIGRFAMs | TIGR03838. Queuosine_YadB. 1 hit. |
| PROSITE | PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GLUQ_SYMTH | ||||||||
| Accession | Primary (citable) accession number: Q67KZ3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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