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Q1LSS9 (SYI_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:BCI_0556
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

Protein attributes

Sequence length938 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 – 938938Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022042

Regions

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

Sites

Metal binding9011Zinc By similarity
Metal binding9041Zinc By similarity
Metal binding9211Zinc By similarity
Metal binding9241Zinc By similarity
Binding site5611Aminoacyl-adenylate By similarity
Binding site6051ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1LSS9 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 697B57DCEEB6DAAA

FASTA938107,240
        10         20         30         40         50         60 
MIDYKNTLNL PKTQFAMRGN LAIREPIMLK RWHQQDLYQL ICQATQGKKT FFLHDGPPYA 

        70         80         90        100        110        120 
NGSIHIGHSV NKILKDIIIK SKRLMGYCSP YIPGWDCHGL PIELKVEQLI GKPGKKVSAS 

       130        140        150        160        170        180 
EFIIACRNYA SEQVTWQKKD FIRLGVLGDW DNIYRTMDFH TEANIIRTLS KIIENGHVYQ 

       190        200        210        220        230        240 
GNKPVHWCID CRSALAEAEV EYYDYTSPSI YVIFAATNTH DVAARFGIPN VLSSISFLVW 

       250        260        270        280        290        300 
TTTPWTIPAN RAISIHPNLN YQLVKVNQQG FILAADLVTS VLTYLGIQNW TVVKNIKGYV 

       310        320        330        340        350        360 
LELLRFSHPF MKFDVPVVLS NHVTINVGTG VVHTSPSHGP DDYLIGREYN LEIVNIVGPD 

       370        380        390        400        410        420 
GCYLPGTFSL LDGTSVYQSN QTVISLLKDR GALLHTGTIQ HSYPHCWRHK TPLIFRATPQ 

       430        440        450        460        470        480 
WFISMDKKKL RQQSLKEIKK IQWIPSNSQA SITNMVNNRQ DWCISRQRIW GVPMSLFVHN 

       490        500        510        520        530        540 
HTKKLHPQTS EIMEYVAKQV EKKGIQAWWD LDPIKILGDD IVNYSKINDI LDVWFDSGST 

       550        560        570        580        590        600 
HSSVINAQTE FANHEIDMYL EGADQHRGWF MSSLISSTAI KGKAPYKTVI THGFAVDSNG 

       610        620        630        640        650        660 
RKMSKSIGNV VSPQQVVDKL GADILRLWVA STNYTDDMTI SDEILKRSVD TYRRIRNTAR 

       670        680        690        700        710        720 
FLLANLNGFE PKQHSVSIDK MIILDQWAID RAQVAQDEII AAYNSYEFHS VVQRIMQFCS 

       730        740        750        760        770        780 
VEMGSFYLDI IKDRQYTTQY NSIARRSCQT ALFHIIEAMV RWIAPIISFT ADEIWGFIPG 

       790        800        810        820        830        840 
KRSPSVFIEE WYKNLSRLDA EQHMNDTYWN TLLQVRSDVN YLIEQARIKK NIGSSLETQV 

       850        860        870        880        890        900 
TLYSEPILAM QLRQLGNELH FVLLTSAVQI ADYQEADNNA LQSTRIKGLK ITLNHATGRK 

       910        920        930 
CQRCWHYEQD IGNNTQYPEI CGRCVINIAG NGEERKFV 

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000238 Genomic DNA. Translation: ABF14142.1.
RefSeqYP_588985.1. NC_007984.1.

3D structure databases

ProteinModelPortalQ1LSS9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374463.BCI_0556.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF14142; ABF14142; BCI_0556.
GeneID4056571.
KEGGbci:BCI_0556.
PATRIC21074621. VBIBauCic75062_0527.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycBCIC374463:GI6Q-556-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_BAUCH
AccessionPrimary (citable) accession number: Q1LSS9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: May 14, 2014
This is version 62 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