A0A0N0ZW18 · A0A0N0ZW18_CHRID
- ProteinIsoleucine--tRNA ligase
- GeneileS
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1131 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
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).
Catalytic activity
- tRNA(Ile) + L-isoleucine + ATP = L-isoleucyl-tRNA(Ile) + AMP + diphosphate
Cofactor
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | aminoacyl-tRNA editing activity | |
Molecular Function | ATP binding | |
Molecular Function | isoleucine-tRNA ligase activity | |
Molecular Function | tRNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | isoleucyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIsoleucine--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Weeksellaceae > Chryseobacterium group > Chryseobacterium
Accessions
- Primary accessionA0A0N0ZW18
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 19-722 | Aminoacyl-tRNA synthetase class Ia | ||||
Sequence: VAEFWKQNKTFSKSVEIREGNPEFVFYEGPPSANGMPGIHHVMARALKDIFCRFQTQNGKQVFRKAGWDTHGLPVELGVEKELGITKEDIGKKISIEDYNKACREAVMRYTGVWNDLTEKIGYWVDLEDPYITYKSKYMETVWWLLKQLYNKDLLYKGYTIQPYSPKAGTGLSSAELNMPGTYHDVSDTTVVAQFKVKKDSSALFNDVDGDVHILAWTTTPWTLPSNTALTVGRDIEYVLVKTFNQYTFEPITVVLSRVLLPKVFGKKYTEGTDEDFANYTPEVKVIPFRILKEFTGEKLVDTRYEQLVPWFTPNDNPENAFRVILGDFVTTEDGTGIVHTAPTFGADDARVAKMAQPEIPPMLIKDESDNLVPLVDLQGKFIQGENVPEVFSGKYIKNEYYDEGTAPEKSWDVELAILLKTENKAFKVEKYVHSYPHCWRTDKPVLYYPLDSWFVKMTAVKDRLVDLNKEINWKPKSTGEGRFANWLENVNDWNLSRSRYWGIPLPIWRTDDLKEEKIIGSVEELYNEIEKSIAAGFMKENPFKGFVIGNMSEQNYALVDLHKNIVDQIIIVSESGKAMKRESDLIDVWFDSGSMPYAQLHYPFENKEMIDNNKAFPADFIAEGVDQTRGWFYTLHAIGTAVFDSVAYKNVMSNGLVLDKNGLKMSKSKGNAVDPFETLSIYGPDATRWYMISNANPWENLKF | ||||||
Motif | 49-59 | 'HIGH' region | ||||
Sequence: PSANGMPGIHH | ||||||
Motif | 683-687 | 'KMSKS' region | ||||
Sequence: KMSKS | ||||||
Domain | 768-920 | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase anticodon-binding | ||||
Sequence: DRWILSELNLLIKEVKAFYEDYEPTRVARAINIFVNDNLSNWYVRLCRRRFWKGDYSDDKISAYQTLYTCLEVVAKLSAPIAPFFMDQLYQDLNKVTGKENCESVHLTDFPVADESLIDEDLVEKTHLAQTITSLVLSIRRAESLKVRQPLQR |
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)).
Sequence similarities
Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,131
- Mass (Da)129,813
- Last updated2015-12-09 v1
- Checksum8C0D6752B47FB67F
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LJOD01000005 EMBL· GenBank· DDBJ | KPE51339.1 EMBL· GenBank· DDBJ | Genomic DNA |