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Q8D2R0 (SYI_WIGBR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:WIGBR2940
OrganismWigglesworthia glossinidia brevipalpis [Complete proteome] [HAMAP]
Taxonomic identifier36870 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeWigglesworthia

Protein attributes

Sequence length940 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 – 940940Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098502

Regions

Motif59 – 6911"HIGH" region HAMAP-Rule MF_02002
Motif604 – 6085"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9031Zinc By similarity
Metal binding9061Zinc By similarity
Metal binding9231Zinc By similarity
Metal binding9261Zinc By similarity
Binding site5631Aminoacyl-adenylate By similarity
Binding site6071ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8D2R0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: F7443E32F0FC4BFE

FASTA940110,118
        10         20         30         40         50         60 
MMNDYKNTLN LPKTKFPMKA NLLISELKIL ECWKKNNLYS IIRENKKGKK TFFLHDGPPY 

        70         80         90        100        110        120 
ANGDIHIGHA VNKILKDIII KFKSLFGFDA PYMPGWDCHG LPIELQVEKK INQNINKINH 

       130        140        150        160        170        180 
KIFREKCRNY ALDQVNKQKK EFIRLGVIGD WNNPYLTMDF HTEANILRTF KNLIKKKYLY 

       190        200        210        220        230        240 
RGIKPINWCI DCKSSLSDSE IDYNIKESNS IDVSFSACDN NKILKIFNSE KKFDKIKAII 

       250        260        270        280        290        300 
WTTTPWTIIA NRAISVNPNF IYLLVKCNKE IFIIAESLLD KTLARLNIKK SKILGSVYGK 

       310        320        330        340        350        360 
KLKFLYFKHP LNKIHVPMIL NEYVDFKSGS GIVHVAPNYG EEDYIIGKKY KLNMYDPIDS 

       370        380        390        400        410        420 
NGNYLPGTFP GLDGLNIFKS EEVVLNLLKN NHSLYSKKII NHSYPHCWRH KSPTFFRATN 

       430        440        450        460        470        480 
QWFFNIDNNN LRNKTISEIK KILWIPKWGM NQIIDLLSNR PDWCISRQRV WGVPIAVFIN 

       490        500        510        520        530        540 
KKNKEIHPNT VELIEKVSKK IEKKGVQAWW DINKSEILDK DSDKYKKVLD TLDVWFDSGS 

       550        560        570        580        590        600 
TYYSILIKKW NSLNKNKVDL YLEGSDQYRG WFMSSIILSI AITGGIPCKK ILAHGFVVDS 

       610        620        630        640        650        660 
NGKKMSKSIG NVISPKDIIN EFGADILRLW VASSDYKSDI SISKEILLRT VDIYRRIRNT 

       670        680        690        700        710        720 
SRFLLSNLND FNPEFNSINL ENMLSIDQWA IIKTNNRQKK IKNAYEEYNF HKVVSNIVDF 

       730        740        750        760        770        780 
CSLDMGSFYL DIIKDRQYTN YIDSLARRSC QTAILYIIEC LVRWIMPILS FTSHEIWKYI 

       790        800        810        820        830        840 
PGKREKYVFL SEWVKEIPCE NINSYISKSL WKILIKIKNE INKIIEIKKL EDKIKSSLEL 

       850        860        870        880        890        900 
KITLYAESFI FEELILLKKE LNFAFLVSYV SIKKYENSKE NAFKSKSIKN LKILAEKFDG 

       910        920        930        940 
KKCLRCWNYT NDIVNDVKYN KICNRCINNI NGVEEKRKYF 

« Hide

References

[1]"Genome sequence of the endocellular obligate symbiont of tsetse flies, Wigglesworthia glossinidia."
Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M., Aksoy S.
Nat. Genet. 32:402-407(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000021 Genomic DNA. Translation: BAC24440.1.
RefSeqNP_871297.1. NC_004344.2.

3D structure databases

ProteinModelPortalQ8D2R0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING36870.WGLp294.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC24440; BAC24440; BAC24440.
GeneID1257094.
KEGGwbr:WGLp294.
PATRIC24024772. VBIWigGlo15804_0323.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAKPVHWCL.
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_WIGBR
AccessionPrimary (citable) accession number: Q8D2R0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2003
Last modified: May 14, 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