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Q89AU9 (SYI_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isoleucine--tRNA ligase

EC=6.1.1.5
Alternative name(s):
Isoleucyl-tRNA synthetase
Short name=IleRS
Gene names
Name:ileS
Ordered Locus Names:bbp_139
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length939 AA.
Sequence statusComplete.
Protein existenceInferred 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 processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processisoleucyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

aminoacyl-tRNA editing activity

Inferred from electronic annotation. Source: InterPro

isoleucine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 939939Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098366

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif603 – 6075"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9031Zinc By similarity
Metal binding9061Zinc By similarity
Metal binding9221Zinc By similarity
Metal binding9251Zinc By similarity
Binding site5621Aminoacyl-adenylate By similarity
Binding site6061ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89AU9 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: AF3D7233544B22EC

FASTA939110,381
        10         20         30         40         50         60 
MKDYKTTLNL PKTNFSMKGN LSKKEPFILK KWNDNNIYSL IKKQNIGKKK FFLNDGPPYA 

        70         80         90        100        110        120 
NGNIHIGHAI NKILKDIVIK FKTLSGFDTY YTPSWDCHGL PIEHKVEKTI KKENILITKK 

       130        140        150        160        170        180 
EFRIKCRNYA QSQVNNQKLE FIRLGVFGDW ENSYLTMNFK NEANIARTLM KMFKYGYVYQ 

       190        200        210        220        230        240 
DFKPVHWCIN CKSALAEAEV EYHNKLSNSI IIKFKLAHNI NFWNQIFKND HNQDIHLVVW 

       250        260        270        280        290        300 
TTTPWTLPAS QAIALNPNFK YQLIQTNNNL FIISEKSVPD TMNKMGIQKW KKIHIFLGKN 

       310        320        330        340        350        360 
ISNLKVIHPF LNTTIPVILA DHVTQELGTG IVHTAPEFGQ DDYYACKKNN INFTPTIDKK 

       370        380        390        400        410        420 
GHFLNNIHPK LNNINIFKSI KIVIKLLNNN NALLHSEKLV HSYPYCWRHK TPIISRATQQ 

       430        440        450        460        470        480 
WFININHNNL RNRCIKYIQE VKWIPHWSKN RMIEMIINRP DWCISRQRTW GVPIPIFIHR 

       490        500        510        520        530        540 
KTGKLHPDTI KLSQKIIQNI ETNGIQAWFD ITEKSFLGEL FKQYKKVTDV IDVWFESGSI 

       550        560        570        580        590        600 
QLSNIYNKIQ HQHNNISDLY IEGLDQHRGW FMSSLIISAA ISNQTPYKKV ITHGFVVDKN 

       610        620        630        640        650        660 
KKKMSKSIGN TVHPSEVINT LGSDILRLWT ASTNYSKEMS ISQETLIHIS DYYRRIRNTA 

       670        680        690        700        710        720 
RFLLANLHEF NPENDLINAK NMIILDKWAI GKALHIQKKI IKSYKNYNFH DVIKYLMNFC 

       730        740        750        760        770        780 
SLDMGTFYLE IIKDRQYTTQ KNSIARRSCQ TAMYLILTAF VKWITPILPF TSDELWEYIP 

       790        800        810        820        830        840 
GTNKNKFVFL ELWSNQLFDL NHKDTMNHEY WNQLLIIKTE VNKALEHARQ NKIIRKSLEA 

       850        860        870        880        890        900 
HMTLYVNETI KCNLKLLNKE LKFLFITSKV EIKNFYEAPK DAFQSETITN FKTIIKKMNG 

       910        920        930 
IKCPRCWHII TKIKNNKNHE ICKRCILNTI GPGELRQFL 

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO26873.1.
RefSeqNP_777768.1. NC_004545.1.

3D structure databases

ProteinModelPortalQ89AU9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224915.bbp139.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO26873; AAO26873; bbp_139.
GeneID1058147.
KEGGbab:bbp139.
PATRIC21245057. VBIBucAph80364_0135.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-139-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02002. Ile_tRNA_synth_type1.
InterProIPR001412. 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.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_BUCBP
AccessionPrimary (citable) accession number: Q89AU9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries