P96551 (SYE1_HELPY) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 88.
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 1 EC=6.1.1.17 Alternative name(s): Glutamyl-tRNA synthetase 1 Short name=GluRS 1 | ||||
| Gene names |
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| Organism | Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 85962 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter › ![]() |
Protein attributes
| Sequence length | 463 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-Rule MF_00022 |
| Catalytic activity | ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022 |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| 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 Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | glutamyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: HAMAP glutamate-tRNA ligase activityInferred from electronic annotation. Source: HAMAP tRNA bindingInferred 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 – 463 | 463 | Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022 | PRO_0000119576 | |||||
Regions | |||||||||
| Motif | 10 – 20 | 11 | "HIGH" region HAMAP-Rule MF_00022 | ||||||
| Motif | 238 – 242 | 5 | "KMSKS" region HAMAP-Rule MF_00022 | ||||||
Sites | |||||||||
| Binding site | 241 | 1 | ATP By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 369 | 1 | V → I Ref.2 | ||||||
| Sequence conflict | 398 | 1 | A → V Ref.2 | ||||||
| Sequence conflict | 411 | 1 | R → H Ref.2 | ||||||
| Sequence conflict | 454 | 1 | V → L Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. Venter J.C.Nature 388:539-547(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695. |
| [2] | Akopyants N.S., Kersulyte D., Clifton S.W., Youree B.E., Reece C.A., Roe B.A., Berg D.E. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 351-463. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE000511 Genomic DNA. Translation: AAD07544.1. AC000108 Genomic DNA. No translation available. |
| PIR | D64579. |
| RefSeq | NP_207274.1. NC_000915.1. YP_006934396.1. NC_018939.1. |
3D structure databases | |
| ProteinModelPortal | P96551. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-3351N. |
| MINT | MINT-165494. |
| STRING | 85962.HP0476. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAD07544; AAD07544; HP_0476. |
| GeneID | 13869664. 898901. |
| KEGG | heo:C694_02440. hpy:HP0476. |
| PATRIC | 20592223. VBIHelPyl33062_0500. |
Phylogenomic databases | |
| eggNOG | COG0008. |
| KO | K01885. |
| OMA | RYRDFKG. |
| ProtClustDB | PRK01406. |
Family and domain databases | |
| Gene3D | 1.10.10.350. 1 hit. 1.10.1160.10. 1 hit. 3.40.50.620. 2 hits. |
| HAMAP | MF_00022_B. Glu_tRNA_synth_B. |
| InterPro | IPR008925. aa-tRNA-synth_I_codon-bd. IPR020751. aa-tRNA-synth_I_codon-bd_sub2. IPR001412. aa-tRNA-synth_I_CS. IPR004527. Glu-tRNA-ligase_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] |
| PANTHER | PTHR10119. PTHR10119. 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. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYE1_HELPY | ||||||||
| Accession | Primary (citable) accession number: P96551 | ||||||||
| 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 |
| Helicobacter pylori Helicobacter pylori (strain 26695): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
