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Q6NGD7 (SYI_CORDI) 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:DIP1589
OrganismCorynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) [Complete proteome] [HAMAP]
Taxonomic identifier257309 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length1052 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 – 10521052Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098536

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02003
Motif627 – 6315"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6301ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6NGD7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 0E045969A137FBCD

FASTA1,052118,486
        10         20         30         40         50         60 
MSDAVGGVYP RVDMSGGTNV FPDMERQVLE YWKDDETFKA SLTNREENPE YVFYDGPPFA 

        70         80         90        100        110        120 
NGLPHYGHLL TGYVKDIVPR YQTMKGKLVN RVFGWDCHGL PAELEAEKQL GIKDKGEIEA 

       130        140        150        160        170        180 
MGLESFNNYC AKSVLEYTQE WKDYVTRQAR WVDFDNGYKT MDMDFMESVM WAFKTLYDKG 

       190        200        210        220        230        240 
LIYQGFRVLP YSWAEHTPLS NQETRLDDSY KMRQDPTLTV TFPITGVKDD SAADASLVGA 

       250        260        270        280        290        300 
YALAWTTTPW TLPSNLALAV NPQVNYVEVK VGDQGAEAIR GQRVLLAEAL VGAYAKELGE 

       310        320        330        340        350        360 
DHEVLTVRPG SELVGLTYQP IFSYFADHEN AFQILAAEYV TTEDGTGIVH QAPAFGEDDM 

       370        380        390        400        410        420 
NTCKEYGIEV VIPVDMDGKF TSLVPEYQGQ LVFDANKSII ADLKAAGRVV RHQTIEHSYP 

       430        440        450        460        470        480 
HSWRSGEPLI YMALPSWFVE VTKIRDRMVE LNKEIDWMPS HIRDGQFGKW LEGARDWNIS 

       490        500        510        520        530        540 
RNRYWGSPIP VWVSDDENYP RVDVYGSLEE LERDFGVRPE SLHRPHIDEL TRPNPDDPTG 

       550        560        570        580        590        600 
KSTMRRVPEV LDCWFESGSM PFAQKHYPFE NKDWFDTHSP ADFIVEYSGQ TRGWFYTLHV 

       610        620        630        640        650        660 
LATALFDRPA FKKVVAHGIV LGDDGTKMSK SRRNYPDVNE VFNRDGSDAM RWFLMSSPIL 

       670        680        690        700        710        720 
RGGNLIVTEQ GIREGVRQAL LPMWNAYSFL QLYSSKPAQW SVDSSDVLDR YILAKLHDVV 

       730        740        750        760        770        780 
AAVGDALDNT DIARACDEVR TFCDALTNWY VRRSRDRFWA GDTEHPEAFY TLYTVLETLT 

       790        800        810        820        830        840 
RVTAPLLPMV SEVIWRGLTG ERSVHLADFP QADQFPADDD LVRAMDEVRG VCSATSSVRK 

       850        860        870        880        890        900 
AHKLRNRLPL PKVTVALPES ARLADFADII RDEVNVKEVA LTSDVDSVGR FDVVVNAKVA 

       910        920        930        940        950        960 
GPRLCKDVQR AIKAVKSGNY ERRGDTVVAD GIELVAGEFT ERLVAADPDS TTQIDGVDGL 

       970        980        990       1000       1010       1020 
VVLDMTLTEE LEAEGWAADV IRGLQDARKA SGFEVSDRIE VKLVVPEEKK EWALRHTDMI 

      1030       1040       1050 
AGEVLATSFE VVTGEPAEHD IVAGVTATVQ KV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248358 Genomic DNA. Translation: CAE50114.1.
RefSeqNP_939931.1. NC_002935.2.

3D structure databases

ProteinModelPortalQ6NGD7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257309.DIP1589.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE50114; CAE50114; DIP1589.
GeneID2650778.
KEGGcdi:DIP1589.
PATRIC21484388. VBICorDip47633_1570.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAENRDWFE.
OrthoDBEOG644ZM1.

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.
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. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_CORDI
AccessionPrimary (citable) accession number: Q6NGD7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2004
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