Q63BZ8 (SYI2_BACCZ) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 71.
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 2 EC=6.1.1.5 Alternative name(s): Isoleucyl-tRNA synthetase 2 Short name=IleRS 2 | ||||
| Gene names |
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| Organism | Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 288681 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › ![]() |
Protein attributes
| Sequence length | 1033 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_02003 |
| Catalytic activity | ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003 |
| Cofactor | Zinc By similarity. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| 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_02003 |
| Sequence similarities | Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 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 |
| 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 – 1033 | 1033 | Isoleucine--tRNA ligase 2 HAMAP-Rule MF_02003 | PRO_0000098518 | |||||
Regions | |||||||||
| Motif | 47 – 57 | 11 | "HIGH" region HAMAP-Rule MF_02003 | ||||||
| Motif | 590 – 594 | 5 | "KMSKS" region HAMAP-Rule MF_02003 | ||||||
Sites | |||||||||
| Binding site | 593 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. Gilna P.J. Bacteriol. 188:3382-3390(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ZK / E33L. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000001 Genomic DNA. Translation: AAU18279.1. |
| RefSeq | YP_083569.1. NC_006274.1. |
3D structure databases | |
| ProteinModelPortal | Q63BZ8. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 288681.BCZK1977. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAU18279; AAU18279; BCE33L1977. |
| GeneID | 3024309. |
| KEGG | bcz:BCZK1977. |
| PATRIC | 18887486. VBIBacCer95304_2082. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0060. |
| KO | K01870. |
| OMA | SRSRYWG. |
| ProtClustDB | PRK06039. |
Enzyme and pathway databases | |
| BioCyc | BCER288681:GHG7-2477-MONOMER. |
Family and domain databases | |
| Gene3D | 3.40.50.620. 2 hits. 3.90.740.10. 1 hit. |
| HAMAP | MF_02003. Ile_tRNA_synth_type2. |
| InterPro | IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR002301. Ile-tRNA-ligase. IPR023586. Ile-tRNA-ligase_type2. 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] |
| 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 | SYI2_BACCZ | ||||||||
| Accession | Primary (citable) accession number: Q63BZ8 | ||||||||
| 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
