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Q5GSS3 (SYI_WOLTR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. 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:Wbm0363
OrganismWolbachia sp. subsp. Brugia malayi (strain TRS) [Complete proteome] [HAMAP]
Taxonomic identifier292805 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeWolbachieaeWolbachia

Protein attributes

Sequence length1134 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 – 11341134Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098573

Regions

Motif52 – 6211"HIGH" region HAMAP-Rule MF_02003
Motif656 – 6605"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6591ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5GSS3 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: A3EDE2284B90E9B1

FASTA1,134131,811
        10         20         30         40         50         60 
MKPKHYPDTI SSPDFSSLEK EIIKFWQENK IFEQSVEKRS KDNCFVFYDG PPFANGLPHY 

        70         80         90        100        110        120 
GHLLTGFIKD AFARYQTMLQ KKVERRFGWD CHGLPAEMGA EKELGISGRT EIEKFGIEKF 

       130        140        150        160        170        180 
NNYCRTSVMK FSSEWEKYVN RQARWVDFHN DYKTMDRSFM ESVIWAFKQL YDKGLVYESV 

       190        200        210        220        230        240 
RVVPYSWACE TPLSNFETRL DTAYRKKTSK AVTVAFELLE NPQQFKQKCK LLAWTTTPWT 

       250        260        270        280        290        300 
LPSNLALAIG KDIEYCAVSV HSSVSFQHVT LESREKETWI PLSRTGMTEE GTETVTEDNE 

       310        320        330        340        350        360 
VSLVNNEIYI FAEDYLEKFI GHCEQNNIPY ENCNTKLKAD DLAGLSYKPL FNYFKGTKNA 

       370        380        390        400        410        420 
FRVFIADYVT GEDGTGVVHT APGFGEEDFY LCQSHDIPAI CPIDNSGRFT AEVSDLTGIH 

       430        440        450        460        470        480 
VFDTNDAIIK KLKEQGNWFK TEQYIHNYPH CWRTDTPLIY RAMPSWYVAV TKFKERMIEL 

       490        500        510        520        530        540 
NKRVNWIPTH IRDGQFGKWL ERAHDWSISR NRFWGTPIPI WKSDNARYPR VDVYGSIAEL 

       550        560        570        580        590        600 
ERDFNVKVND LHRPFIDSLT RPNPDDPTGK SIMRRVPDVF DCWFESGSVP FAQVHYPFEN 

       610        620        630        640        650        660 
KEWFESNFPA DFITEYIAQT RGWFYTLFVL STALFDSEPF KNCICHGVVL DVKGQKLSKR 

       670        680        690        700        710        720 
LNNYADPMEV FDKYGSDALR FLMLSGSIVC GGNLFLNKEG SSIRDVLKNV MKPIWNSYHF 

       730        740        750        760        770        780 
FTMYANADGI KAEVCKDYKS TIDSYMIFKC FEAVESIQAS MSNYNSQEAC KILIDFFEVL 

       790        800        810        820        830        840 
NNWYIRRSRE RFWKSNLDQD KTDAYNVLYT VFYYILRAAV PLLPLITETI WQGLKYKEIS 

       850        860        870        880        890        900 
VHLADFPQLE RYDSELIAKM DLVREICNSA LSIRNTFNIR VRQPLGSMTV YHQSSCSFLE 

       910        920        930        940        950        960 
SKPLSVVIPK FSPVIPMRDT GTQKEKKWSN AEMKTSMNEY QEMIKDEVNV KELKLVNSLE 

       970        980        990       1000       1010       1020 
GIASLELKLN FPMLGKRIPD KVKKLVQYVK EGKWKQVDNE QVFLGNESES YIIEKDEYEL 

      1030       1040       1050       1060       1070       1080 
LLKTNSEYSS VFGDNKGIVI LNTALDDALV LEGLARDVVR LIQEARKQAD FHISDRIRVI 

      1090       1100       1110       1120       1130 
IKTEDEKIKR AINTWGEYIR EQTLSLSLEI NIEIGDNFYS KEYQDLIVGI ELNC 

« Hide

References

[1]"The Wolbachia genome of Brugia malayi: endosymbiont evolution within a human pathogenic nematode."
Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N., Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J., Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S. expand/collapse author list , Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D., Koonin E., Slatko B.
PLoS Biol. 3:599-614(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TRS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017321 Genomic DNA. Translation: AAW70951.1.
RefSeqYP_198193.1. NC_006833.1.

3D structure databases

ProteinModelPortalQ5GSS3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292805.Wbm0363.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW70951; AAW70951; Wbm0363.
GeneID3266894.
KEGGwbm:Wbm0363.
PATRIC24032379. VBIWolEnd7741_0567.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAYETLYEC.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycWEND292805:GH18-409-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_WOLTR
AccessionPrimary (citable) accession number: Q5GSS3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2005
Last modified: May 14, 2014
This is version 68 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