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Q6D0C3 (SYI_PECAS) 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:ECA3876
OrganismPectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica) [Complete proteome] [HAMAP]
Taxonomic identifier218491 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium

Protein attributes

Sequence length937 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.

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 – 937937Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098383

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif602 – 6065"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9001Zinc By similarity
Metal binding9031Zinc By similarity
Metal binding9201Zinc By similarity
Metal binding9231Zinc By similarity
Binding site5611Aminoacyl-adenylate By similarity
Binding site6051ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6D0C3 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 983DCA36BCCE24D2

FASTA937104,856
        10         20         30         40         50         60 
MSDYKTTLNL PETGFPMRGD LAKREPDMLK RWYEQDLYGI IRNAKKGKKT FILHDGPPYA 

        70         80         90        100        110        120 
NGSIHIGHSV NKILKDIIVK SKGLSGYDSP YVPGWDCHGL PIELKVEQLI GKPGEKVSAA 

       130        140        150        160        170        180 
EFRAECRKYA AEQVAGQKAD FIRLGVLGDW DRPYLTMDFK TEANIIRALG RIIENGHLHK 

       190        200        210        220        230        240 
GAKPVHWCAD CGSALAEAEV EYYDKTSPSI DVTFNASDVA AVLAKFGVSR VDGPISLVIW 

       250        260        270        280        290        300 
TTTPWTLPAN RAISLNAEFD YQLVQIDGQA LILAADLVES VMKRVGVTQW IVLGDCKGAD 

       310        320        330        340        350        360 
LELLRFKHPF LGFDVPAILG DHVTLDAGTG AVHTAGGHGP DDYVISQKYN LEIANPVGPN 

       370        380        390        400        410        420 
GCYLSGTYPE LDGKFVFKAN DLIVEILREK SMLLHVEKLQ HSYPCCWRHK SPIIFRATPQ 

       430        440        450        460        470        480 
WFVSMDQKGL RKQSLSEIKD VQWIPDWGQA RIEAMVANRP DWCISRQRTW GVPMSLFVHK 

       490        500        510        520        530        540 
ETEELHPRTA ELIEAVAKRV EADGIQAWWD LDPADVLGAD ADNYVKVPDT LDVWFDSGST 

       550        560        570        580        590        600 
HASVVDVRPE FGGHEADMYL EGSDQHRGWF MSSLMISTAI KGKAPYRQVL THGFTVDGQG 

       610        620        630        640        650        660 
RKMSKSIGNT VSPQDVMNKL GADILRLWIG STDYSGEIAV SDEILKRSAD AYRRIRNTAR 

       670        680        690        700        710        720 
FLLANLNGFD PQKDSVKPED MVVLDRWAVG CAKAAQDEIL EAYESYDFHR VVQRLMQFCS 

       730        740        750        760        770        780 
IEMGSFYLDI IKDRQYTAKG DSVARRSCQT ALYHISEALV RWMAPIMSFT ADELWNYLPG 

       790        800        810        820        830        840 
ERAQYVFTEE WYDGLFALDA SETMNDAFWA DVLKVRSEVN KVIEQARNDK RIGGSLEASV 

       850        860        870        880        890        900 
TLYADANLAD KLNQLRQELH FALLTSKARV ERYENAPDSA QATELTGLKI ALSEAEGHKC 

       910        920        930 
PRCWHYETDI GSNADHPEVC GRCATNVGGN GEERKFV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX950851 Genomic DNA. Translation: CAG76774.1.
RefSeqYP_051964.1. NC_004547.2.

3D structure databases

ProteinModelPortalQ6D0C3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218491.ECA3876.

Proteomic databases

PRIDEQ6D0C3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG76774; CAG76774; ECA3876.
GeneID2882280.
KEGGeca:ECA3876.
PATRIC20483157. VBIPecAtr54885_3932.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPATR218491:GJNB-3952-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 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_PECAS
AccessionPrimary (citable) accession number: Q6D0C3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: August 16, 2004
Last modified: April 16, 2014
This is version 72 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