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Q83G52 (SYI_TROWT) 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:TWT_477
OrganismTropheryma whipplei (strain Twist) (Whipple's bacillus) [Complete proteome] [HAMAP]
Taxonomic identifier203267 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeTropheryma

Protein attributes

Sequence length1056 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.

Sequence caution

The sequence AAO44574.1 differs from that shown. Reason: Erroneous initiation.

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 – 10561056Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098571

Regions

Motif63 – 7311"HIGH" region HAMAP-Rule MF_02003
Motif632 – 6365"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6351ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83G52 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: D1D531A27E790967

FASTA1,056119,751
        10         20         30         40         50         60 
MCDQGEVSSQ NSSDYKEQRP TPRPNLPKIE ESVLAFWSSD KTFEASLEQR QHGKRWVFYD 

        70         80         90        100        110        120 
GPPFANGLPH FGHLLTGYIK DAIPRYQTMR GQYVPRVFGW DTHGLPAELE AMKRLGITEK 

       130        140        150        160        170        180 
SQIESMGIAS FNEAARKSVL TYVDQWEEYV NRQARWVDFK NGYKTLDLDY MESVLWAFKT 

       190        200        210        220        230        240 
LYKKGVIYEG YKVLPYCWND QTPLSNHELR MDDEVYKQRL DDSLTVTFPL IGQKAKTCGL 

       250        260        270        280        290        300 
DGVAALAWTT TPWTLPSNMA LIVSPNVEYV VVSSARQNSN SDFLLCKSSL DSYAECLGYE 

       310        320        330        340        350        360 
SGQDARASIR RTLLGKEIEG IHYKPLFDYY ADLHNAFTIL SDNYVDVTEG TGIVHASPAH 

       370        380        390        400        410        420 
GEDDKRVCDA FGVPTVVSIN DAACFTDVIS NYAGMHIFDA NAVIRSDLSR DGRILRHESY 

       430        440        450        460        470        480 
KHSYPHCWRC RSPLIYKAVT SWFFRITDSV NRMLELNQQI NWVPKSVKNG QFAKWLSSAK 

       490        500        510        520        530        540 
DWSISRTRYW GTPIPVWKSD NPEYPRIDCY GSLKELEDDF GIKLTDLHRP EIDRLTRPNP 

       550        560        570        580        590        600 
DDPTGASTMR RVPDVLDVWF DAASMPFAQL HYPFENIERF EANKSADFIV EYAGQIRGWF 

       610        620        630        640        650        660 
YLLHAMSTAL FDGVAFKNAI CHGIVLGDDG QKASKSLRNY PDVYDVFENE GSDAVRWYLI 

       670        680        690        700        710        720 
SSSILRGGSL IVSRKKIQDA IRQYITPLWS SWYFFHIYSE AARPGGYKAR FSVDSQDILD 

       730        740        750        760        770        780 
RYILSKTGLL VEDVTRFMDS FDMASAALQL RDFVAVLTNW YIRRSRDRFW DGSDTGAFDT 

       790        800        810        820        830        840 
LYTVLETLCR LGAVFVPMVS EHVYKCLTNS RSVHLSDWPD VATFPNETGL VETMDRVRKI 

       850        860        870        880        890        900 
CSTGLSLRKR LGIKARQPLS SAHIRVAQVG SLAQYKDIIS GELNVKTVSI EEGSCTQRML 

       910        920        930        940        950        960 
KILPRVAGPR LAGDVQTVIA AARRGDWTDH DGHVTAGGIP LLENEYQLVA GAQDSKNSQP 

       970        980        990       1000       1010       1020 
LPFGGSVTLD TRIDETLRSE GVARDTVRQI QIARKEKDLN ITDRISLEVC VPDEQVKNNL 

      1030       1040       1050 
LAFSELICKE TLCDRLDILV KKGIDGITVS LEKFRQ 

« Hide

References

[1]"Tropheryma whipplei twist: a human pathogenic Actinobacteria with a reduced genome."
Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M., Claverie J.-M.
Genome Res. 13:1800-1809(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Twist.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014184 Genomic DNA. Translation: AAO44574.1. Different initiation.
RefSeqNP_787605.1. NC_004572.3.

3D structure databases

ProteinModelPortalQ83G52.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203267.TWT477.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO44574; AAO44574; TWT_477.
GeneID1089357.
KEGGtwh:TWT477.
PATRIC23997503. VBITroWhi72342_0621.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMADWNLSRS.
OrthoDBEOG644ZM1.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycTWHI203267:GJDK-509-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_TROWT
AccessionPrimary (citable) accession number: Q83G52
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 72 of the entry and version 2 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