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Q8DGI7 (SYI_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:tlr2330
OrganismThermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP]
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus

Protein attributes

Sequence length953 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.

Sequence caution

The sequence BAC09882.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 953953Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098489

Regions

Motif61 – 7111"HIGH" region HAMAP-Rule MF_02002
Motif605 – 6095"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9221Zinc By similarity
Metal binding9251Zinc By similarity
Metal binding9421Zinc By similarity
Metal binding9451Zinc By similarity
Binding site5641Aminoacyl-adenylate By similarity
Binding site6081ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DGI7 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: EDC235E0D3C77843

FASTA953107,523
        10         20         30         40         50         60 
MTDATPDYKD TVNLPQTTFE MRANAATREP QLQAFWAQHK IYETLQQTNP GEVFILHDGP 

        70         80         90        100        110        120 
PYANGALHIG HALNKILKDI INKYQLLRGR KVHYRPGWDC HGLPIELKVL QNLKPEQRAQ 

       130        140        150        160        170        180 
LTPLTLRQQA KEFALKTVAE QKQSFQRYGV WGDWAHPYLT LTPDYEAAQI GVFGEMVLRG 

       190        200        210        220        230        240 
YIYRGLKPVH WSPSSKTALA EAELEYPEGH TSRSLYAAFE VIELPQGLAK AWYNALGKLG 

       250        260        270        280        290        300 
VAIWTTTPWT IPANLAVSVN PDLTYALVEV QPSERYKHLI VAKDLVERLS DTLGRTLKVV 

       310        320        330        340        350        360 
ATAKGADLEH SRYRHPLFER EGKILIGGDY VTTESGTGLV HTAPGHGLED YGVGQRYGLP 

       370        380        390        400        410        420 
ILSPVDENGC FTAEAGPFAG LNVLQEGNAA VIAALQECGA LLKEEPYVHK YPYDWRTKKP 

       430        440        450        460        470        480 
TIFRATEQWF ASVEGFRDAA LRAIAEVKWI PAQGENRITA MVAERSDWCI SRQRSWGVPI 

       490        500        510        520        530        540 
PVFYDKETGE PLLTAETIAH VQAIIRDRGS DAWWELSVAE LLPESLRDQA DRYEKGTDTM 

       550        560        570        580        590        600 
DVWFDSGSSW AAVLGDQQAD LYLEGSDQHR GWFQSSLLTR VAVKGQAPYK AVLTHGFVLD 

       610        620        630        640        650        660 
EQGRKMSKSL GNVTDPREVI EGGKNQKQDP PYGADVLRLW VSSVDYANDV PIGKNILRQL 

       670        680        690        700        710        720 
ADVYRKIRNT ARFLLGNLHD FEPEQDMIPY AQLPALDRYM LHRLHEVFSE VTAAFDSFQF 

       730        740        750        760        770        780 
YRFFQTIQNL CVVDLSNFYL DIAKDRLYIS AATGDRRRSC QTVLAIALQN LARAIAPVLP 

       790        800        810        820        830        840 
HLAEDIWQHL PFKTPYLSVF QSGWVQLSAQ WQDNALAAEW QRLRQLRLEV NKVLEKARAE 

       850        860        870        880        890        900 
KLIGSSLEAK VWLYVADSEW RDRLAQMNPR DALSGNGVDE LRYLFLVSQV ELMPQPQAVD 

       910        920        930        940        950 
VPYVLEAEGL WIGVGHAQGE KCVRCWNYSE SVGQSALHPQ LCDRCQAALQ GEF 

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References

[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000039 Genomic DNA. Translation: BAC09882.1. Different initiation.
RefSeqNP_683120.1. NC_004113.1.

3D structure databases

ProteinModelPortalQ8DGI7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING197221.tlr2330.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC09882; BAC09882; BAC09882.
GeneID1011751.
KEGGtel:tlr2330.
PATRIC23930126. VBITheElo119873_2442.

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Family and domain databases

Gene3D3.40.50.620. 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_THEEB
AccessionPrimary (citable) accession number: Q8DGI7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: February 19, 2014
This is version 74 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