A0A549YKB7 · A0A549YKB7_9BACI

  • Protein
    Isoleucine--tRNA ligase
  • Gene
    ileS
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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).

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site553L-isoleucyl-5'-AMP (UniProtKB | ChEBI)
Binding site597ATP (UniProtKB | ChEBI)
Binding site885Zn2+ (UniProtKB | ChEBI)
Binding site888Zn2+ (UniProtKB | ChEBI)
Binding site905Zn2+ (UniProtKB | ChEBI)
Binding site908Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionaminoacyl-tRNA editing activity
Molecular FunctionATP binding
Molecular Functionisoleucine-tRNA ligase activity
Molecular FunctiontRNA binding
Molecular Functionzinc ion binding
Biological Processisoleucyl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Isoleucine--tRNA ligase
  • EC number
  • Alternative names
    • Isoleucyl-tRNA synthetase
      (IleRS
      )

Gene names

    • Name
      ileS
    • ORF names
      FH966_11870

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NKC851-2
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Lentibacillus

Accessions

  • Primary accession
    A0A549YKB7

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain27-633Aminoacyl-tRNA synthetase class Ia
Motif57-67'HIGH' region
Motif594-598'KMSKS' region
Domain677-831Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase anticodon-binding
Domain882-910Zinc finger FPG/IleRS-type

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    918
  • Mass (Da)
    105,362
  • Last updated
    2019-10-16 v1
  • Checksum
    3F99C732F9411A9C
MDYKDTLLMPKTKFPMRGNLPNKEPERQQKWDDDRIYEKGLERTQGRPLFILHDGPPYANGDLHIGHALNKILKDFITRYKSMSGYHAPYVPGWDTHGLPIETALTKKKKVDRKKMSIPEFRQKCAEYAMAQLDNQRNQFKKLGVRGDWENPYITLTKDYEAAQIRVFGEMAKKGYIYRGLKPVYWSPSSESALAEAEIEYHDKRSPSIYVTFDVTDGKDVLDGDEKIIIWTTTPWTIPANLGIAFHPELEYAVVAVNDEKYVIAHELLETLTETLEWENPEVIKTFKGEKADKVVARHPFYNRDSLVMLGEHVTTDAGTGCVHTAPGHGEDDFYMSRTYGIEPLSPVDDKGYFTSEAPGFEGLFYDQANKVITEKLDEAGALLQLTFITHSYPHDWRTKKPTIFRATSQWFASIKDFRQDILDEINQINWYPAWGETRLYNMVRDREDWCISRQRTWGVPMPVFYAEDGTPIINDETIAHVSNLFAEHGSNVWFEWEANELLPEGFTSEHSPNGKFTKETDIMDVWFDSGSSHEAVLMGREDHKRPADVYLEGSDQYRGWFNSSISTAVAVTGKAPFETIISHGFTLDGNGRKMSKSLGNVMDPLKVQKQLGSDILRLWVSSVDYQADVRISQEILKQISEAYRKIRNTIRFMLGNLADFNPEKDAVPEAEMEEADRYMLHRLQHVLKNVRDSYDVYEFSPIYSQIHNFCTVDLSSFYLDFAKDILYIEAVNSHRRRSIQTAYYEIVTTLVKLLTPIIPHTADEVWEYIPGVTEESVQLTDIPEPRDITGFSELYEKWDSFMQVRDDVLKALEEAREAKIIGKSLEAKLTIVPKDNKTKEVLDGIPNVHQLFIVSEADITEEAPDANEYANVHVLVEKHPGEKCARCWTAAENVGQDEHHPDLCSRCADIVNEHYSA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VJMZ01000001
EMBL· GenBank· DDBJ
TRM12328.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp