Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B6EMY6 (SYI_ALISL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. 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:VSAL_I0580
OrganismAliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238)) [Complete proteome] [HAMAP]
Taxonomic identifier316275 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

Protein attributes

Sequence length952 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 – 952952Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189119

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif617 – 6215"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9151Zinc By similarity
Metal binding9181Zinc By similarity
Metal binding9351Zinc By similarity
Metal binding9381Zinc By similarity
Binding site5761Aminoacyl-adenylate By similarity
Binding site6201ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B6EMY6 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: A0926B7211DC6395

FASTA952106,898
        10         20         30         40         50         60 
MSDYKETLNL PETGFPMRGN LANREPVMLK HWYDEDLYGE IRKAKKGKKS FILHDGPPYA 

        70         80         90        100        110        120 
NGDIHIGHAL NKILKDIIIK SKTLSGFDAP YIPGWDCHGL PIELMVEKKK GKPGQKISAA 

       130        140        150        160        170        180 
EFREECRKYA AVQVEGQKES FKRLGIMGEW DKPYRTMDFG TEANIIRSLG KIADQGHLLK 

       190        200        210        220        230        240 
GFKPVHWCTD CGSALAEAEV EYQDKFSPSI DVRFVAADEA ATLAKFSTPE GHQGEGELSV 

       250        260        270        280        290        300 
VIWTTTPWTL PANRAVALHA DLEYVLVQVE AHGEQKAERL ILASELAKSV MDRAGIEHFH 

       310        320        330        340        350        360 
NLGFAKGSEL ELLQFNHPFY GFTVPAILGE HVTVDSGTGI VHTAPGHGQE DFVVGKKYDL 

       370        380        390        400        410        420 
EIANPVGSNG VYLPDTELFA GQHVFKANDS VIDVLKEKGA LLHHHAIEHS YPHCWRHKTP 

       430        440        450        460        470        480 
IIFRATPQWF ISMDQAGLRA KALEEVKSVE WMPEWGQSRI EGMIEGRPEW CISRQRTWGV 

       490        500        510        520        530        540 
PIALFVHKET SELHPDSLEL IEKVAKLVEE KGIQAWWDLD IAELMGEDDA TKYEKVLDTL 

       550        560        570        580        590        600 
DVWFDSGVTH FSVVDSREEY NFPQEERTHS ADLYLEGSDQ HRGWFQSSLI SSVAMKGKAP 

       610        620        630        640        650        660 
YRQVLTHGFV VDGNGRKMSK SVGNVVAPKD VTNKLGADIL RLWVASTDYT NEVAVSDEIL 

       670        680        690        700        710        720 
KRSADAYRRI RNTARFFLAN LNGFNPETDI VPAEEMVALD RWAVGRAFAA QEEIIKSYDE 

       730        740        750        760        770        780 
YNLHEVTQRL MHFCSIEMGS FYLDVIKDRQ YTAKKSGHAQ RSCQTALYYI VEALVRWMAP 

       790        800        810        820        830        840 
IMSFTADEIW NEMPGKRDKF VFTGEWYEGL FDLAEGEDLN NEFWSKIQAV RASVNKLLEA 

       850        860        870        880        890        900 
ARGEKVIGGS LQAEITLYAD DALAAKINKL DNELRFVLLT SSATVKPLSE KSDSAKATEL 

       910        920        930        940        950 
DGLFVDVAAS EAAKCERCWH HVADVGTIEG HEEVCGRCVS NVEGEGEERK FA 

« Hide

References

[1]"The genome sequence of the fish pathogen Aliivibrio salmonicida strain LFI1238 shows extensive evidence of gene decay."
Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S., Thurston S., Parkhill J., Willassen N.P., Thomson N.R.
BMC Genomics 9:616-616(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LFI1238.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM178379 Genomic DNA. Translation: CAQ78265.1.
RefSeqYP_002262100.1. NC_011312.1.

3D structure databases

ProteinModelPortalB6EMY6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316275.VSAL_I0580.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ78265; CAQ78265; VSAL_I0580.
GeneID6989100.
KEGGvsa:VSAL_I0580.
PATRIC20851263. VBIAliSal95923_0687.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKKRIELM.
OrthoDBEOG644ZM1.

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_ALISL
AccessionPrimary (citable) accession number: B6EMY6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: November 25, 2008
Last modified: May 14, 2014
This is version 44 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