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Q9RUP8 (SYI_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. 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:DR_1335
OrganismDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]
Taxonomic identifier243230 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length1078 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
Reference 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 – 10781078Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098542

Regions

Motif52 – 6211"HIGH" region HAMAP-Rule MF_02003
Motif637 – 6415"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6401ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RUP8 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: DF007ED70528F70F

FASTA1,078120,273
        10         20         30         40         50         60 
MTKRTFAPVP TQPNFRQLEA DILQKWKDEQ VFEQTQTRPA PAGEFVFYEG PPTANGKPAL 

        70         80         90        100        110        120 
HHVLARSFKD LFPRFKVMQG HHVTRKGGWD THGLPVEISV EKKLGWLGRN HGASREELEE 

       130        140        150        160        170        180 
FNRLCRTSVW ETIQDWNELT ERMGYWLDLG DPYITYQNSY VESVWNLLRR LHEKGLVAQD 

       190        200        210        220        230        240 
YKVVPLSPRI SSTLSRAELG EVDSYRMVDD PSVYVRLPIV WDTLPERAHA ALSSLSGEQR 

       250        260        270        280        290        300 
QGLSLLVWTT TPWTLPSNTL AAVNPDLDYV VADSPSGRVI VAEGAVERLS ALHKDAAPLE 

       310        320        330        340        350        360 
VLARFKGRDL EWVEYEPPFP EVASQLGVVS ELHERRDGKP VLHFVVMADF VSDVDGSGVA 

       370        380        390        400        410        420 
HEAPAYGAED LEVARAYGVP LMFGVDDHGI LQVTHEQGKF FKDADKGLIA DMKARGLMFW 

       430        440        450        460        470        480 
AGTLKHRYPF HDRTGDPILY FAKKGWYIRT SQVAGEMLAQ NEKINWVPGN IKHGRFGNWL 

       490        500        510        520        530        540 
EGNVDWAISR ERYWGTPLPF WQSESGQLRV IGSVAELSEL AGRDLSDLDL HRPYIDDITF 

       550        560        570        580        590        600 
TLDGEEYRRV PEVLDVWFDS GSMPYAQWGL LLNEQGEAVR GAEQFAKHYP ADYICEAIDQ 

       610        620        630        640        650        660 
TRGWFYSLHA ISTMLYDQPA YKNVICLGHI VDEKGLKMSK SKGNVVAPLP LFDQYGADSV 

       670        680        690        700        710        720 
RWYMFMASDP GDQKRFSERL VAEAQRSYVN TLWNVYSFFV LYANLDQPDL AAAPAVAERP 

       730        740        750        760        770        780 
EMDRWLLARL EETVRDVTAA LESYDARSGG RALEGFVDDL SNWYVRRSRS RFWGEGGTVD 

       790        800        810        820        830        840 
TAAYATLHEA LLVVSQLTAP FTPFLADALY RNLSGEESSV HLTPWPTVRA ERLDRKLTAD 

       850        860        870        880        890        900 
MAAVMKVVEL GRAVRGAHNL KTRQPLAGVQ VRAASPEALD ALKRSQTQIM EELNVKAVTF 

       910        920        930        940        950        960 
LEGDTDLVQY SLRPNLPVVG KQYGKQLPVL KKALTEADAR AVATAVQAGQ GFSVQADGVT 

       970        980        990       1000       1010       1020 
FDLTPGSVLV DAKAPEGVAA AEDAGYLVAF DTALTPELVR EGLARDLVRA IQEARKAAGF 

      1030       1040       1050       1060       1070 
EVQDRIALAL ELDGEALEAA QAWQDFIAGE VLAEQVAYGS GEGFRAEVEG GAVTLKKL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000513 Genomic DNA. Translation: AAF10907.1.
PIRE75407.
RefSeqNP_295058.1. NC_001263.1.

3D structure databases

ProteinModelPortalQ9RUP8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243230.DR_1335.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF10907; AAF10907; DR_1335.
GeneID1798492.
KEGGdra:DR_1335.
PATRIC21630266. VBIDeiRad64572_1531.

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMARVEHMVE.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycDRAD243230:GH46-1364-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. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYI_DEIRA
AccessionPrimary (citable) accession number: Q9RUP8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 83 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