Q0SU18 (SYE_CLOPS) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 45.
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: Glutamate--tRNA ligase EC=6.1.1.17 Alternative name(s): Glutamyl-tRNA synthetase Short name=GluRS | ||||
| Gene names |
| ||||
| Organism | Clostridium perfringens (strain SM101 / Type A) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 289380 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium |
Protein attributes
| Sequence length | 552 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity. HAMAP MF_00022_B |
| Catalytic activity | ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B |
| Subunit structure | Monomer By similarity. HAMAP MF_00022_B |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00022_B. |
| Sequence similarities | Belongs to the class-I aminoacyl-tRNA synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glutamyl-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 glutamate-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 – 552 | 552 | Glutamate--tRNA ligase HAMAP MF_00022_B | PRO_0000367651 | |||||
Regions | |||||||||
| Motif | 41 – 51 | 11 | "HIGH" region HAMAP MF_00022_B | ||||||
| Motif | 293 – 297 | 5 | "KMSKS" region HAMAP MF_00022_B | ||||||
Sites | |||||||||
| Binding site | 296 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "Skewed genomic variability in strains of the toxigenic bacterial pathogen, Clostridium perfringens." Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Khouri H. Paulsen I.T.Genome Res. 16:1031-1040(2006) [PubMed: 16825665] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SM101 / Type A. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000312 Genomic DNA. Translation: ABG86873.1. |
| RefSeq | YP_698389.1. NC_008262.1. |
3D structure databases | |
| ProteinModelPortal | Q0SU18. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q0SU18. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4204243. |
| GenomeReviews | Gene locus CPR_1067 in contig CP000312_GR. |
| KEGG | cpr:CPR_1067. |
| PATRIC | 19490425. VBICloPer122123_1043. |
| TIGR | CPR_1067. |
Phylogenomic databases | |
| eggNOG | COG0008. |
| HOGENOM | HBG628189. |
| OMA | DKETAND. |
| ProtClustDB | PRK01406. |
Enzyme and pathway databases | |
| BioCyc | CPER289380:CPR_1067-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00022_B. Glu_tRNA_synth_B. [Tree] |
| InterPro | IPR008925. aa-tRNA-synth_I_codon-bd. IPR020751. aa-tRNA-synth_I_codon-bd_sub2. 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. G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit. |
| 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. |
| SUPFAM | SSF48163. tRNA-synt_bind. 1 hit. |
| TIGRFAMs | TIGR00464. GltX_bact. 1 hit. |
| PROSITE | PS00178. AA_TRNA_LIGASE_I. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYE_CLOPS | ||||||||
| Accession | Primary (citable) accession number: Q0SU18 | ||||||||
| 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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