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A0KG39 (SYI_AERHH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 61. 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:AHA_0682
OrganismAeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [Complete proteome] [HAMAP]
Taxonomic identifier380703 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Protein attributes

Sequence length953 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 – 953953Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022037

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif618 – 6225"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9161Zinc By similarity
Metal binding9191Zinc By similarity
Metal binding9361Zinc By similarity
Metal binding9391Zinc By similarity
Binding site5771Aminoacyl-adenylate By similarity
Binding site6211ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A0KG39 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: B14EE34C3A6A5265

FASTA953106,106
        10         20         30         40         50         60 
MSDYKHTLNL PETEFPMRGD LAKREPNMLK RWYDQDLYGA IRRAKAGKPS FILHDGPPYA 

        70         80         90        100        110        120 
NGSIHIGHSV NKILKDIIIK SKGLSGFDSP YVPGWDCHGL PIELKVEGMV GKPGEKVSAA 

       130        140        150        160        170        180 
EFRAECRKYA KTQIEAQKTD FIRLGVLGDW EHPYLTMDFG TEANIIRSMA KIVENGHLHK 

       190        200        210        220        230        240 
GSKPVHWCTD CGSALAEAEV EYYDKNSPSI DVRFKAVDEA GVAAKFDCAE GHTGKGPISA 

       250        260        270        280        290        300 
VIWTTTPWTL PANRGIAMHA DLDYALVQVE GEHPERLILA AELVKDVMDR AGIEQFHNLG 

       310        320        330        340        350        360 
YAKGAALELL RFNHPFYSFD VPVVLGDHVT LDAGTGAVHT APGHGQEDFV VGQKYGLEVA 

       370        380        390        400        410        420 
NPVGSNGVYL PDTELFAGQH VFKANASVVE VLTERGALLH HKVFNHSYPH CWRHKTPIIF 

       430        440        450        460        470        480 
RATPQWFISM EQKGLRQRAL EEIERIEQDG IKQHGQSGWV PAWGKNRIQA MVENRPDWCI 

       490        500        510        520        530        540 
SRQRTWGVPI SLFVHKETQE LHPESVRLMH EVAKRVEQSG IQAWWDLDKA ELLGSDADLY 

       550        560        570        580        590        600 
DKVPDTLDVW FDSGSTHSSV VDARPEFNGN PADMYLEGSD QHRGWFMSSL MIGVAMKDKA 

       610        620        630        640        650        660 
PYNQVLTHGF TVDGQGRKMS KSIGNVVSPQ DVMNKLGADI LRLWVASTDY TGEMTVSDEI 

       670        680        690        700        710        720 
LKRSADAYRR IRNTARFLLA NLNGFNPATD MVAPADMVVV DRWAVGRAKA VQAEIMAAFD 

       730        740        750        760        770        780 
EYNFHGVTQK LMQFCSIEMG SFYLDVIKDR QYTAKADSLA RRSCQTALYH IAEAMVRWMA 

       790        800        810        820        830        840 
PIMSFTADEI WALLPGERGE FVFTEEWYDG LFGLEAGETL NDDFWAEILT VRGEVNKALE 

       850        860        870        880        890        900 
VARGEKRIGG SLQAELTLFA KPALAARLNA LADELRFVLL TSKAKVVSVD AAPADAVATE 

       910        920        930        940        950 
RDDLWLSVAQ SAAAKCDRCW HHVEDVGTIA GHEEICGRCV TNVEGDGETR QFA 

« Hide

References

[1]"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades."
Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.
J. Bacteriol. 188:8272-8282(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 7966 / NCIB 9240.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000462 Genomic DNA. Translation: ABK37838.1.
RefSeqYP_855224.1. NC_008570.1.

3D structure databases

ProteinModelPortalA0KG39.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING380703.AHA_0682.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK37838; ABK37838; AHA_0682.
GeneID4487674.
KEGGaha:AHA_0682.
PATRIC20778878. VBIAerHyd135212_0684.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycAHYD380703:GH2M-683-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_AERHH
AccessionPrimary (citable) accession number: A0KG39
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: April 16, 2014
This is version 61 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