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A3D1G5 (SYI_SHEB5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:Sbal_1054
OrganismShewanella baltica (strain OS155 / ATCC BAA-1091) [Complete proteome] [HAMAP]
Taxonomic identifier325240 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length940 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 – 940940Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022116

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif605 – 6095"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9031Zinc By similarity
Metal binding9061Zinc By similarity
Metal binding9231Zinc By similarity
Metal binding9261Zinc By similarity
Binding site5641Aminoacyl-adenylate By similarity
Binding site6081ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A3D1G5 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: EA8F41CC9F30A278

FASTA940105,748
        10         20         30         40         50         60 
MSDYKFTLNL PETEFPMRGN LANREPEMLE RWTKDGLYQQ IRDSRIGRTP FILHDGPPYA 

        70         80         90        100        110        120 
NGSIHIGHSV NKILKDIIVK SKTMSGFDAP YVPGWDCHGL PIELKVEQKV GKPGQKISAA 

       130        140        150        160        170        180 
EFREECRKYA AEQVNGQRED FIRLGVLGDW QNPYLTMDFS TEANIVRSLS KVIESGHLHK 

       190        200        210        220        230        240 
GVKPVHWCTD CGSALAEAEV EYEDKTSPAI DVAFVAADSK AVAAKFGVSD YSHPVSMVIW 

       250        260        270        280        290        300 
TTTPWTLPAN RALSLSPELD YSLVEFEKDG VTQALILAEV LVESCLTRYN VESHTVLGSA 

       310        320        330        340        350        360 
KGAAFELVRF NHPFLDFDVP AILGDHVTTD AGTGIVHTAP GHGQDDFVVG QKYGLEVANP 

       370        380        390        400        410        420 
VGDNGVYKPD TEYFAGQHVF KANDNVVALL REKSALLNHV AYRHSYPHCW RHKTPIIFRA 

       430        440        450        460        470        480 
TPQWFISMDN HGLRTQALKE IEQTQWIPDW GQSRIEKMVE NRPDWCISRQ RTWGVPITLF 

       490        500        510        520        530        540 
VNRETEELHP DSVSLMERVA SRIEQQGIQA WWDLDAAELL GDEAEQYRKV TDTLDVWFDS 

       550        560        570        580        590        600 
GSTFSSVVAA RPEFHGHGVD LYLEGSDQHR GWFMSSLMIS TAMNGKAPYK QVLTHGFTVD 

       610        620        630        640        650        660 
GKGRKMSKSI GNVIAPQTVT NKLGADILRL WVAATDYSGE MTVSDEILNR SADAYRRIRN 

       670        680        690        700        710        720 
TARFLLANLN GFEPAKDLVA VEDMVALDRW VVRRAAALQQ EIIEAYEQYN FHIVTQKLMQ 

       730        740        750        760        770        780 
FCSVELGSFY LDIIKDRQYT AKQEGHARRS CQSALYLISE AMVRWIAPIL SFTADEVWQL 

       790        800        810        820        830        840 
LPGERDAYVF TQEWYQGLKS VTLATDLSDD YWQQLLTVRN EVNKVIEQAR RDKRIGGSLE 

       850        860        870        880        890        900 
AEVTLFADAA LTEQLTHIGD ELRFVLLTSE AKVLPLADAT SEAVETELAS LKLLVASSTA 

       910        920        930        940 
EKCERCWHHR EEVGTIEAHP TLCTRCVTNI EGDGEVRLFA 

« Hide

References

[1]"Complete sequence of chromosome of Shewanella baltica OS155."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I., Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS155 / ATCC BAA-1091.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000563 Genomic DNA. Translation: ABN60578.1.
RefSeqYP_001049447.1. NC_009052.1.

3D structure databases

ProteinModelPortalA3D1G5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING325240.Sbal_1054.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN60578; ABN60578; Sbal_1054.
GeneID4841392.
KEGGsbl:Sbal_1054.
PATRIC37180887. VBISheBal55297_1296.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycSBAL325240:GCTA-1078-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_SHEB5
AccessionPrimary (citable) accession number: A3D1G5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 20, 2007
Last modified: May 14, 2014
This is version 54 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