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Q0AAD1 (SYI_ALKEH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. 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:Mlg_0852
OrganismAlkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1) [Complete proteome] [HAMAP]
Taxonomic identifier187272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeAlkalilimnicola

Protein attributes

Sequence length941 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 – 941941Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022040

Regions

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

Sites

Metal binding9041Zinc By similarity
Metal binding9071Zinc By similarity
Metal binding9241Zinc By similarity
Metal binding9271Zinc By similarity
Binding site5621Aminoacyl-adenylate By similarity
Binding site6061ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0AAD1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 2B8F9AE6731EAC86

FASTA941105,903
        10         20         30         40         50         60 
MSDYKHTLNL PKTGFPMRGN LAKREPERLA GWYQTDLYGR LRRERAGKPR FVLHDGPPYA 

        70         80         90        100        110        120 
NGDIHIGHAV NKILKDIIIK ARSMDGYDVP YVPGWDCHGL PIELMVEKKR GKAGAKVSPR 

       130        140        150        160        170        180 
AFRDACREFA ASQVDGQRED FKRLGVLGDW DNPYLTMDYR TEADILRALG RIIQRGHVTR 

       190        200        210        220        230        240 
GFKPVHWCAD CGSALAEAEV EYEEKTSPAI DVRFAVLEPE ELDRRAGLGG EAAAAGRVAI 

       250        260        270        280        290        300 
PIWTTTPWTL PANQAVALHP ELEYVVVAFD DELLVLAAEL VESAMARYEV DDYRVVGRCD 

       310        320        330        340        350        360 
GAVLEGLRLA HPFLEREVPV ILGGHVTTDG GTGAVHTAPG HGQDDYVVGQ QYDLPTDNPV 

       370        380        390        400        410        420 
DGNGVFLPDT PFFAGQHVFK ANPKVVDLLA ERGALLHHEP YRHSYPHCWR HKTPILFRAT 

       430        440        450        460        470        480 
PQWFISLDKA GMREHAMAAI KGVSWHPEWG QARIESMVNG RPDWCISRQR NWGVPIALFV 

       490        500        510        520        530        540 
DKRSGEPHPE SERLIEAVAR RVEEAGVDAW FELDPAELLG ADAERYEKVT DILDVWFDSG 

       550        560        570        580        590        600 
VTHATVLERR DELQVPADLY LEGSDQHRGW FQSSLLTSVG VRETAPYKGV LTHGFTVDEK 

       610        620        630        640        650        660 
GHKMSKSRGN VVAPQKVMDT LGADILRLWV ASSDYSAEMA VSDGILKRTA DAYRRMRNTA 

       670        680        690        700        710        720 
RFLLANLNGF EPAEHAVAPP DMLPLDRWAV DRAYLLQQQV REAYERYEFH RIYQMVHNFC 

       730        740        750        760        770        780 
VVDLGGFYLD VIKDRQYTTK PDSLARRSCQ TALWHVAEGL VRWLAPIISF TAEEIWEHLP 

       790        800        810        820        830        840 
GERSDSVLLE TWYEGLFPLD DSDPFGRAFW DDVLAVRAGV NRELEQLRND KVIGASLQAE 

       850        860        870        880        890        900 
VQLFCPPELK AKLDRLGDEL RFVLITSEAR VEDLERAPVE SVEVPGENGQ GFRLFAAASQ 

       910        920        930        940 
HPKCTRCWHH RPDVGHHADH PELCGRCVSN VDGEGETRHY A 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000453 Genomic DNA. Translation: ABI56206.1.
RefSeqYP_741696.1. NC_008340.1.

3D structure databases

ProteinModelPortalQ0AAD1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING187272.Mlg_0852.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI56206; ABI56206; Mlg_0852.
GeneID4270789.
KEGGaeh:Mlg_0852.
PATRIC20860933. VBIAlkEhr114327_0851.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycAEHR187272:GHAX-881-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_ALKEH
AccessionPrimary (citable) accession number: Q0AAD1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 67 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