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Q65ZU1 (SYI_BORGA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. 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:BG0858
OrganismBorrelia garinii (strain PBi) [Complete proteome] [HAMAP]
Taxonomic identifier290434 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group

Protein attributes

Sequence length1042 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_02003

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003

Cofactor

Zinc By similarity. HAMAP-Rule MF_02003

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02003

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02003.

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_02003

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 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 – 10421042Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098526

Regions

Motif48 – 5811"HIGH" region HAMAP-Rule MF_02003
Motif594 – 5985"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site5971ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65ZU1 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 6389CBC417E852C4

FASTA1,042122,408
        10         20         30         40         50         60 
MFKKVENKAN FPKIEEKILK FWNDNKIFEK SMEQREGCEE FTFYDGPPFA TGLPHFGHFV 

        70         80         90        100        110        120 
PNTIKDIIPR YQTMKGKYVK RNFGWDTHGL PVEYEVEKKL GISGKYEIEN YGIENFNKEC 

       130        140        150        160        170        180 
KKIVLRYTEE WKNIILRLGR WVDFEKGYKT MDISFMESVW WVFKNLYNKG LIYESYYVLP 

       190        200        210        220        230        240 
YSPKLATPLS NFEVNLGEYK EVNDPSLTIK FKIKDKNEYL LAWTTTPWTL PSNLGIAVGK 

       250        260        270        280        290        300 
EIEYSKIFDK KKEEILILGS KKINSYFDDE NAYTIIEKFK GSQLQGIEYE PIFNYFLEQK 

       310        320        330        340        350        360 
DKGAFKVHTA DYITTDDGTG IVHIAPFGEE DYRVLKKHTN VDIIDPLDAE CKFTNRVKDF 

       370        380        390        400        410        420 
KGLFVKDADK KIIENLKLRN FLFKRENYLH RYPFCYRTNY PIIYRPISSW FVNVEKIKTQ 

       430        440        450        460        470        480 
LLEVNEKINW MPAHLKKGRF GKWLENAKDW AISRNRFWGN PIPIWICSKT GKKICVGSRK 

       490        500        510        520        530        540 
ELEELSGQKI EDLHKDKIDK ITWPSKDGGT FIRTSEVLDC WFESGAMPYA SNHYPFANES 

       550        560        570        580        590        600 
NFKNIFPADF IAEGLDQTRG WFYTLTILGT SLFENTAFKN VIVNGLVLSS DGRKMSKSFK 

       610        620        630        640        650        660 
NYTDPMEVIN TFGADALRLY LIMSPVVKAD DLKYSDNGVR DVLKNIIIPI WNAYSFFTTY 

       670        680        690        700        710        720 
AIIDKFKPTK NLSLVKSNNL DKWIISELES LKKILNKEID KYNLTKSIES LLEFIDKLNN 

       730        740        750        760        770        780 
WYIRRSRRRF WKSENDKDKN DAYETLYYAI KTLMILLAPF IPFITEEIYQ NLKTDEDKQS 

       790        800        810        820        830        840 
IHLNDYPKAN ENFIDKTIEE KINLARKITS MARSLRSLHN IKIRMPISTI YVVTKNQNEQ 

       850        860        870        880        890        900 
NMLIEMQEII LDEINVKEMK IKSNEEELIT YKAKANFKEL GKKLGKDMKT VSIEISKLKN 

       910        920        930        940        950        960 
EDIIKIINGI SHEIKVDNAK YYLSLNDIIL ERDEKDNLKV INEESITIGI DSLITQELYL 

       970        980        990       1000       1010       1020 
EGLTREFVRQ IQNLRKEKNF DVSDRINLYI ENNATLEEIL NKFEKYIKTE TLALNIILNK 

      1030       1040 
SKLEKKINLD NDIFTIIGIE KC 

« Hide

References

[1]"Comparative analysis of the Borrelia garinii genome."
Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U., Schilhabel M., Wilske B., Suehnel J., Platzer M.
Nucleic Acids Res. 32:6038-6046(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PBi.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000013 Genomic DNA. Translation: AAU07680.1.
RefSeqYP_073272.1. NC_006156.1.

3D structure databases

ProteinModelPortalQ65ZU1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290434.BG0858.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU07680; AAU07680; BG0858.
GeneID2957738.
KEGGbga:BG0858.
PATRIC20567293. VBIBorGar102262_0943.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000246403.
KOK01870.
OMADWNLSRS.
OrthoDBEOG644ZM1.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycBGAR290434:BG0858-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02003. Ile_tRNA_synth_type2.
InterProIPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
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.
[Graphical view]
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYI_BORGA
AccessionPrimary (citable) accession number: Q65ZU1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 11, 2004
Last modified: April 16, 2014
This is version 72 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