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Q73HW7 (SYI_WOLPM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 69. 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:WD_0423
OrganismWolbachia pipientis wMel [Complete proteome] [HAMAP]
Taxonomic identifier163164 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeWolbachieaeWolbachia

Protein attributes

Sequence length1111 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 – 11111111Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098572

Regions

Motif52 – 6211"HIGH" region HAMAP-Rule MF_02003
Motif645 – 6495"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6481ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q73HW7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: A8673A51D27841F7

FASTA1,111128,833
        10         20         30         40         50         60 
MKSKHYPDTV SSPDFLSLEK EIIKFWQENK VFERSVEERS KDNCFVFYDG PPFANGLPHY 

        70         80         90        100        110        120 
GHLLTGFIKD AFARYQTMLQ KRVERRFGWD CHGLPAEMGA EKELGISGRT EIEKFGIDKF 

       130        140        150        160        170        180 
NDHCRTSVMK FSSEWEKYVN RQARWVDFHN DYKTMDKSFM ESVMWAFKQL YDKGLVYESV 

       190        200        210        220        230        240 
RVVPYSWACE TPLSNFETRL DNAYREKVSK AVTVAFELLE NPQQFKSVKR KCKLLAWTTT 

       250        260        270        280        290        300 
PWTLPSNLAL AIGKDIKYCA VSVHPLMSFQ RVTLESISGS QCLGTGMTGS SEGSSMNGEI 

       310        320        330        340        350        360 
YIFAESYLEK FISHSEQNNI PYENCNIKLK ANDLAGLSYK PLFDYFKDTK NAFRVFIADY 

       370        380        390        400        410        420 
VTEEDGTGVV HTAPGFGEED FYLCQSHDIP VICPIDNSGK FTAEVSDLAG VHVFDANDTV 

       430        440        450        460        470        480 
IKKLKGQGSW FKTEQYIHNY PHCWRTDTPL IYRTMPSWYV AVTKFKSRMV ELNKRVNWIP 

       490        500        510        520        530        540 
NHIRDGQFGK WLEGAHDWSI SRNRFWGTPI PVWKSDDARY PRVDVYGSIE ELERDFNVKI 

       550        560        570        580        590        600 
DDLHRPFIDT LTRLNPDDPT GKSVMRRVPD VFDCWFESGS MPFAQIHYPF ENKEWFESAD 

       610        620        630        640        650        660 
FITEYIAQTR GWFYTLFVLS TALFNREPFK NCICHGVVLD VKGQKLSKRL NNYADPMEVF 

       670        680        690        700        710        720 
DRYGSDALRF LMLSGSIICG GNLLLDKEGN SIRDVLKNVI KPIWNSYHFF TMYANADGIK 

       730        740        750        760        770        780 
AEVCKDYQST IDRYMISKCF EAVESIQASM NSYSSQEACK ILIDFFEVLN NWYIRRSRER 

       790        800        810        820        830        840 
FWKSDLDQDK TDAYNVLYTV FYYILRAAAP LLPLITENIW QGLKYEETSV HLANFPQLEK 

       850        860        870        880        890        900 
FDSQLIAKMD LVREVCNSAL SIRNTFNIRI RQPLGSMIIY HQSSCSFLEG EPLSVIPEFF 

       910        920        930        940        950        960 
PVIQVADTGI QCAADSNEYQ EMIKDEVNVK SLELVNRLEG IASLELKLNF PLLGKRIPDK 

       970        980        990       1000       1010       1020 
IKKLVQYVKE GKWKQVENEQ IFLGDESENY IIEKGEYELL LKANSEYSSV FDNNKGIVIL 

      1030       1040       1050       1060       1070       1080 
NTELNDELIL EGLARDVVRL IQETRKQADF HISDRIRVII KTEEEKIKEA INTWFEYIKE 

      1090       1100       1110 
QTLALSLDIN TEIGTNFYSK EYQDLSVSIE R 

« Hide

References

[1]"Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a streamlined genome overrun by mobile genetic elements."
Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., Brownlie J.C., McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R., Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F., Nelson W.C. expand/collapse author list , Mohamoud Y., Lee P., Berry K.J., Young M.B., Utterback T.R., Weidman J.F., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H., O'Neill S.L., Eisen J.A.
PLoS Biol. 2:327-341(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017196 Genomic DNA. Translation: AAS14146.1.
RefSeqNP_966212.1. NC_002978.6.

3D structure databases

ProteinModelPortalQ73HW7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING163164.WD0423.

Proteomic databases

PRIDEQ73HW7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS14146; AAS14146; WD_0423.
GeneID2738789.
KEGGwol:WD0423.
PATRIC24029422. VBIWolEnd21207_0419.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMATEGIDQT.
OrthoDBEOG644ZM1.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycWEND163164:GJ8W-417-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 2 hits.
HAMAPMF_02003. Ile_tRNA_synth_type2.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. 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. 3 hits.
SSF50677. SSF50677. 2 hits.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_WOLPM
AccessionPrimary (citable) accession number: Q73HW7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 69 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