P41257 (SYI_CAMJE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 103.
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: Isoleucine--tRNA ligase EC=6.1.1.5 Alternative name(s): Isoleucyl-tRNA synthetase Short name=IleRS | ||||
| Gene names |
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| Organism | Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 192222 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter › ![]() |
Protein attributes
| Sequence length | 917 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) By similarity. HAMAP-Rule MF_02002 |
| Catalytic activity | ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02002 |
| Cofactor | Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_02002 |
| Subunit structure | Monomer By similarity. HAMAP-Rule MF_02002 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_02002. |
| Domain | IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)) By similarity. HAMAP-Rule MF_02002 |
| Sequence similarities | Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. |
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 Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | isoleucyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP regulation of translational fidelityInferred from electronic annotation. Source: GOC |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: HAMAP aminoacyl-tRNA editing activityInferred from electronic annotation. Source: InterPro isoleucine-tRNA ligase activityInferred from electronic annotation. Source: HAMAP zinc ion bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 917 | 917 | Isoleucine--tRNA ligase HAMAP-Rule MF_02002 | PRO_0000098372 | |||||
Regions | |||||||||
| Motif | 59 – 69 | 11 | "HIGH" region HAMAP-Rule MF_02002 | ||||||
| Motif | 610 – 614 | 5 | "KMSKS" region HAMAP-Rule MF_02002 | ||||||
Sites | |||||||||
| Metal binding | 890 | 1 | Zinc By similarity | ||||||
| Metal binding | 893 | 1 | Zinc By similarity | ||||||
| Metal binding | 905 | 1 | Zinc By similarity | ||||||
| Metal binding | 908 | 1 | Zinc By similarity | ||||||
| Binding site | 569 | 1 | Aminoacyl-adenylate By similarity | ||||||
| Binding site | 613 | 1 | ATP By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 144 | 1 | D → N in AAA91296. Ref.1 | ||||||
| Sequence conflict | 223 | 1 | E → K in AAA91296. Ref.1 | ||||||
| Sequence conflict | 362 | 1 | G → R in AAA91296. Ref.1 | ||||||
| Sequence conflict | 527 | 1 | K → N in AAA91296. Ref.1 | ||||||
| Sequence conflict | 592 | 1 | A → T in AAA91296. Ref.1 | ||||||
| Sequence conflict | 621 | 1 | S → P in AAA91296. Ref.1 | ||||||
| Sequence conflict | 697 | 1 | T → S in AAA91296. Ref.1 | ||||||
| Sequence conflict | 759 | 1 | M → I in AAA91296. Ref.1 | ||||||
| Sequence conflict | 769 | 1 | P → S in AAA91296. Ref.1 | ||||||
| Sequence conflict | 816 | 1 | A → V in AAA91296. Ref.1 | ||||||
| Sequence conflict | 900 | 1 | N → D in AAA91296. Ref.1 | ||||||
| Sequence conflict | 915 | 1 | V → I in AAA91296. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "An isoleucyl-tRNA synthetase gene from Campylobacter jejuni." Hong Y., Wong T., Bourke B., Chan V.L. Microbiology 141:2561-2567(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 43431 / TGH 9011 / Serotype O:3. |
| [2] | "The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. Barrell B.G.Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U15295 Genomic DNA. Translation: AAA91296.1. AL111168 Genomic DNA. Translation: CAL35179.1. |
| PIR | B81309. |
| RefSeq | YP_002344456.1. NC_002163.1. |
3D structure databases | |
| ProteinModelPortal | P41257. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P41257. 13 interactions. |
| STRING | 192222.Cj1061c. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAL35179; CAL35179; Cj1061c. |
| GeneID | 905353. |
| KEGG | cje:Cj1061c. |
| PATRIC | 20059080. VBICamJej33762_1043. |
Phylogenomic databases | |
| eggNOG | COG0060. |
| HOGENOM | HOG000246402. |
| KO | K01870. |
| OMA | KQVLTHG. |
| ProtClustDB | PRK05743. |
Enzyme and pathway databases | |
| BioCyc | CJEJ192222:GJTS-1035-MONOMER. |
Family and domain databases | |
| Gene3D | 3.40.50.620. 2 hits. 3.90.740.10. 1 hit. |
| HAMAP | MF_02002. Ile_tRNA_synth_type1. |
| InterPro | IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR002301. Ile-tRNA-ligase. IPR023585. Ile-tRNA-ligase_type1. IPR014729. Rossmann-like_a/b/a_fold. IPR009080. tRNAsynth_1a_anticodon-bd. IPR013155. V/L/I-tRNA-synth_anticodon-bd. IPR009008. Val/Leu/Ile-tRNA-synth_edit. [Graphical view] |
| PANTHER | PTHR11946:SF9. PTHR11946:SF9. 1 hit. |
| Pfam | PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 1 hit. [Graphical view] |
| PRINTS | PR00984. TRNASYNTHILE. |
| SUPFAM | SSF47323. tRNAsyn_1a_bind. 1 hit. SSF50677. ValRS_IleRS_edit. 1 hit. |
| TIGRFAMs | TIGR00392. ileS. 1 hit. |
| PROSITE | PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYI_CAMJE | ||||||||
| Accession | Primary (citable) accession number: P41257 Secondary accession number(s): Q0P9J1, Q9PNN0 | ||||||||
| 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 |

Clusters with
