Reviewed,
UniProtKB/Swiss-Prot Q6G4S5 (SYI_BARHE)
Last modified
February 9, 2010.
Version 39.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Isoleucyl-tRNA synthetase EC=6.1.1.5 Alternative name(s): Isoleucine--tRNA ligase Short name=IleRS | ||||
| Gene names |
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| Organism | Bartonella henselae (Rochalimaea henselae) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 38323 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella |
Protein attributes
| Sequence length | 971 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 MF_02002 |
| Catalytic activity | ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP MF_02002 |
| Subunit structure | Monomer By similarity. HAMAP MF_02002 |
| Subcellular location | Cytoplasm By similarity HAMAP 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 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 Nucleotide-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | isoleucyl-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 isoleucine-tRNA ligase activityInferred from electronic annotation. Source: HAMAP zinc ion 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 – 971 | 971 | Isoleucyl-tRNA synthetase HAMAP MF_02002 | PRO_0000098353 | |||||
Regions | |||||||||
| Motif | 64 – 74 | 11 | "HIGH" region HAMAP MF_02002 | ||||||
| Motif | 643 – 647 | 5 | "KMSKS" region HAMAP MF_02002 | ||||||
Sites | |||||||||
| Binding site | 602 | 1 | Aminoacyl-adenylate By similarity | ||||||
| Binding site | 646 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae." Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E. Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49882 / Houston 1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX897699 Genomic DNA. Translation: CAF27070.1. |
| RefSeq | YP_033110.1. |
3D structure databases | |
| SMR | Q6G4S5. Positions 8-965. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2865553. |
| GenomeReviews | Gene locus BH02580 in contig BX897699_GR. |
| KEGG | bhe:BH02580. |
| NMPDR | fig|283166.1.peg.238. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG577712. |
| OMA | KQVLTHG. |
| PhylomeDB | Q6G4S5. |
Enzyme and pathway databases | |
| BioCyc | BHEN283166:BH02580-MONOMER. |
| BRENDA | 6.1.1.5. 277357. |
Family and domain databases | |
| HAMAP | MF_02002. Ile_tRNA_synth_type1. [Tree] |
| InterPro | IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR002301. Ile-tRNA-synt_Ia. IPR015905. Ile-tRNA-synt_Ia_N. IPR018353. Isoleucyl-tRNA_synthetase. 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_Ia_edit. [Graphical view] |
| Gene3D | G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. |
| PANTHER | PTHR11946:SF9. Ile-tRNA-synt_Ia. 1 hit. |
| Pfam | PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 1 hit. [Graphical view] |
| PRINTS | PR00984. TRNASYNTHILE. |
| TIGRFAMs | TIGR00392. ileS. 1 hit. |
| PROSITE | PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYI_BARHE | ||||||||
| Accession | Primary (citable) accession number: Q6G4S5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


