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C5B7M4 (SYI_EDWI9) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 38. 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:NT01EI_0679
OrganismEdwardsiella ictaluri (strain 93-146) [Complete proteome] [HAMAP]
Taxonomic identifier634503 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEdwardsiella

Protein attributes

Sequence length948 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 – 948948Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000216235

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif613 – 6175"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9111Zinc By similarity
Metal binding9141Zinc By similarity
Metal binding9311Zinc By similarity
Metal binding9341Zinc By similarity
Binding site5721Aminoacyl-adenylate By similarity
Binding site6161ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
C5B7M4 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 2399B079470C2A0C

FASTA948105,791
        10         20         30         40         50         60 
MSDYKNTLNL PETGFPMRGD LAKREPGMLQ HWYEQDLYGI IRNAKQGKKS FILHDGPPYA 

        70         80         90        100        110        120 
NGSIHIGHSV NKILKDIIIK SKGLSGYDSP YIPGWDCHGL PIELKVEQLI GKPGEKYSAA 

       130        140        150        160        170        180 
EFREQCRAYA AEQVAGQKAD FIRLGVLGDW EHPYLTMDYG TEANIIRALA RIVDNGHLMK 

       190        200        210        220        230        240 
GAKPVHWCPD CGSSLAEAEV EYYDKVSPSI DVRFAAVDKA QVLAKFGVSE AKGDVNVVIW 

       250        260        270        280        290        300 
TTTPWTLPAN RAVALHPELE YQLVQVEGEC LILAADLVES VMKRAGIDYW QVLGSCKGEA 

       310        320        330        340        350        360 
LELLHFCHPF MNFDVPIIMG DHVTLDAGTG AVHTAPGHGP DDYVVGQKYG LEIANPVGSN 

       370        380        390        400        410        420 
GCYLPGTHPV LDGLFVFKAN DIVIDLLKDS GALLHVEKLT HSYPCCWRHK SPIIFRATPQ 

       430        440        450        460        470        480 
WFISMDRQGL RSQSLAEIDR IERQGLDEQN LSGWIPAWGK ARIESMVANR PDWCISRQRT 

       490        500        510        520        530        540 
WGVPMAMLVH KETQELHPRT TELMEMVAKR VEQAGIQAWW DLDIRDLLGD EADQYEKVPD 

       550        560        570        580        590        600 
TLDVWFDSGS TSYSVVDARP EFNGHSPDMY LEGSDQHRGW FMSSLMISVA MKGKAPYRQV 

       610        620        630        640        650        660 
LTHGFTVDGQ GRKMSKSVGN VVSPQQVMNK LGGDILRLWV ASTDYTSEMA VSDEILKRSA 

       670        680        690        700        710        720 
DAYRRIRNTA RFLLANLNGF DPCKDMVKPE DMVVLDRWAV GCAKQAQDEI IAAYENYDFH 

       730        740        750        760        770        780 
EVVQRLMQFC SVEMGSFYLD IIKDRQYTAK ADSVARRSCQ TALYHIAEAL VRWMAPILSF 

       790        800        810        820        830        840 
TADEVWGYLP GDRAQFVFTE EWYQGLFGLD AAEQMNDAFW AELLKVRGEV NRVIEQARND 

       850        860        870        880        890        900 
KKVGGSLEAA ITLYADEALA TQLDSLQDEL RFVLITSAAR VQPLVQATAD AVASELAGLK 

       910        920        930        940 
VGLGKADGSK CPRCWHYSTA IGQDAAHPQL CPRCVTNVAG QGEERKFA 

« Hide

References

[1]"Complete genome sequence of Edwardsiella ictaluri 93-146."
Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C., Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 93-146.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001600 Genomic DNA. Translation: ACR67901.1.
RefSeqYP_002932136.1. NC_012779.2.

3D structure databases

ProteinModelPortalC5B7M4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING634503.NT01EI_0679.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR67901; ACR67901; NT01EI_0679.
GeneID7962013.
KEGGeic:NT01EI_0679.
PATRIC21834582. VBIEdwIct114273_0611.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycEICT634503:GCMY-674-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_EDWI9
AccessionPrimary (citable) accession number: C5B7M4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: April 16, 2014
This is version 38 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