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Q97ES0 (SYI_CLOAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. 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:CA_C3038
OrganismClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) [Reference proteome] [HAMAP]
Taxonomic identifier272562 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length1035 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 – 10351035Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098533

Regions

Motif48 – 5811"HIGH" region HAMAP-Rule MF_02003
Motif589 – 5935"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site5921ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q97ES0 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 5FC26B022AFDAA86

FASTA1,035119,411
        10         20         30         40         50         60 
MYKKVDSSKS FVDIERDVLK LWHEKEIVKK SFNSNQDGEY FSFYDGPPTA NGRPHVGHII 

        70         80         90        100        110        120 
TRVMKDLIPR YKVMKGYKVP RKAGWDTHGL PVELEIEKKL GISGKPQIEE YGIEKFVKEC 

       130        140        150        160        170        180 
KESVFSYVSL WKDMSEKLGY WVDMENPYVT YHNDYIESVW WALKQMWDKD LLYKGHKIVP 

       190        200        210        220        230        240 
YCPRCGTALS SHEVAQGYKD VKEATAFVKF KVKGEENKYI LAWTTTPWTL PSNVALAINK 

       250        260        270        280        290        300 
AYDYVEVINN GEHLILAKAL LTVLEGEYEV VSEFKGEKLL GMEYEQLFKF ANPDKKAFYV 

       310        320        330        340        350        360 
VHGDFVTLSD GTGIVHIAPA YGEDDNMLGK KYDLPLINLV NGEGKFVDEV EPWKGLFVKK 

       370        380        390        400        410        420 
ADPKILEYMK ENGTLYKSEK FTHSYPHCWR CDTPLLYYPR DSWFVRMTSL RDKLVENNNK 

       430        440        450        460        470        480 
IHWYPDNIRT GRFGKFVENV IDWGISRDRY WGTPLPIWQC ECGHRDCVGS IEELKEKGIN 

       490        500        510        520        530        540 
VPENIELHKP YIDEVKLTCP KCGKPMTRTE EVIDCWFDSG SMPFAQLHYP FENKEVFENT 

       550        560        570        580        590        600 
FPAQFISEAV DQTRGWFYTL LAISTSIFDK SSFENCIVLG HVLDKHGLKM SKHKGNVVDP 

       610        620        630        640        650        660 
FDVLDNQGAD ACRWHFYTSS APWLPTRFSQ EDVAETQRKF LSTLWNVYSF YVLYAEIDKF 

       670        680        690        700        710        720 
NPNDYKDFVS GNVMDKWIVS RLNTLTKDVG NYLDSYGITQ AALEIQDFVD DLSNWYVRRN 

       730        740        750        760        770        780 
RSRYWTQELT DDKVGAYVTL YRVLVTLSKV AAPFIPFMTE QIYQSLVTSI NEGAEESVHL 

       790        800        810        820        830        840 
CKWPEYDESL IDSSLEEEMK LAISIVKLGR SARNGANIKN RQPLYEMRVS TKALPDYYGD 

       850        860        870        880        890        900 
IIRDELNVKK VEFGADLSKY VNFEIKPNLP VLGKSYGKLI PKIRKEISSM DQMKLAERVR 

       910        920        930        940        950        960 
SGEAVKIDVD GTEIELNSEN LLVTMQGLEG FAFAGIGEIG IVLETTITDE LREEGYLREV 

       970        980        990       1000       1010       1020 
LSKVQNMRKE SGFEVADKIE IYVSGNEKLE NVIRKFEDTI KKETLATDII YSENKEAAIY 

      1030 
NINGEELNVF VKKNC 

« Hide

References

[1]"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum."
Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.
J. Bacteriol. 183:4823-4838(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001437 Genomic DNA. Translation: AAK80978.1.
PIRG97273.
RefSeqNP_349638.1. NC_003030.1.

3D structure databases

ProteinModelPortalQ97ES0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272562.CA_C3038.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK80978; AAK80978; CA_C3038.
GeneID1119221.
KEGGcac:CA_C3038.
PATRIC32040485. VBICloAce74127_3221.

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMADWNLSRS.
OrthoDBEOG644ZM1.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycCACE272562:GJIH-3121-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.
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_CLOAB
AccessionPrimary (citable) accession number: Q97ES0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2001
Last modified: April 16, 2014
This is version 76 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