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Q057X9 (SYI_BUCCC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. 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:BCc_093
OrganismBuchnera aphidicola subsp. Cinara cedri (strain Cc) [Complete proteome] [HAMAP]
Taxonomic identifier372461 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length941 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 – 941941Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022044

Regions

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

Sites

Metal binding9041Zinc By similarity
Metal binding9071Zinc By similarity
Metal binding9241Zinc By similarity
Metal binding9271Zinc By similarity
Binding site5641Aminoacyl-adenylate By similarity
Binding site6081ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q057X9 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: D00F6241B1F556BC

FASTA941112,919
        10         20         30         40         50         60 
MINIKKSLNL PKTKFPMKAN LAYKENEILE TWKKINLYNK LHKNKKKNKQ FFLQDGPPYA 

        70         80         90        100        110        120 
NGNIHIGHAV NKILKDIILK FKRMSGFFSP YIPCWDCHGL PIEHIIEKKL SKKKINKKEF 

       130        140        150        160        170        180 
RKICFKYVLK QVEKQKNDFI RLGIIANWDN INLSTDYINQ SNTIKVLTKI VEKGLIYRDL 

       190        200        210        220        230        240 
KPVYWCFDCQ SALAEAEIEY KFKKSISIYI EYKLIENSIL KNNFFKNYNK KIFNNISILI 

       250        260        270        280        290        300 
FTTTPWTIPT CQAIAINPKL YYQIIKINKK YYICIEELTK KIFKKNNIKK WKIILSFKGK 

       310        320        330        340        350        360 
EIEHIKCFHP FLNTQIPIIL SKHVSNQLGT GAVHMSPDHG YEDFIACKKY KIIPKQIVDS 

       370        380        390        400        410        420 
HGFYKIKKYS QLNNIHIFNK ENKIIYILKK NKKLFFFQTI NHNYPHCWRH KKPIIFRATP 

       430        440        450        460        470        480 
QWFINLSKKN FKEDTFNKIK KILWIPSWGK NKMKKMLKIR PDWCISRQRI WGIPLPFFIH 

       490        500        510        520        530        540 
KNTGELHPNT VMIMKKIVKK IRNHGYKIWW ESNVNTWIKK DSETYRKVND VLDVWFESGA 

       550        560        570        580        590        600 
NHQLKIYKHN IKNKKNYVAD LYLEGSDQHR GWFMSSLIIS MITKTIPPYL SVITHGFVLD 

       610        620        630        640        650        660 
KNGQKMSKSL NNNISPKKII QKKGADILRL WVAYTNYTND ISISNEILEQ ISDNYRRIRN 

       670        680        690        700        710        720 
TIRFLFSNIF DFKANIHIIK YEKMLFLDQW IIEKTYNYQR KIIKKYSQYQ FHKVIKKIIN 

       730        740        750        760        770        780 
FCSIELGSCY LELIKDRQYT MHKNSIERRS SQTAIFYILQ FLVRWIAPIL SFTAEEIWSQ 

       790        800        810        820        830        840 
LQEKKEKSIF MTQWYKNKQL IKKKSTYNLF FWKKIFAIRK EINLFIETEK KNKFIKNSLE 

       850        860        870        880        890        900 
IILLLYINKK LFNFLLLFNN ELKFIFLVSE TQLHKYSSAP SLAIKSKKIK KFKILIKKSK 

       910        920        930        940 
KIKCPRCWNY TKKNNFLKNK NSICNKCIKN INQTNKKHIF L 

« Hide

References

[1]"A small microbial genome: the end of a long symbiotic relationship?"
Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M., Silva F.J., Moya A., Latorre A.
Science 314:312-313(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Cc.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000263 Genomic DNA. Translation: ABJ90570.1.
RefSeqYP_802663.1. NC_008513.1.

3D structure databases

ProteinModelPortalQ057X9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING372461.BCc_093.

Proteomic databases

PRIDEQ057X9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ90570; ABJ90570; BCc_093.
GeneID4440638.
KEGGbcc:BCc_093.
PATRIC21246129. VBIBucAph7855_0089.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycBAPH372461:GHAJ-93-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_BUCCC
AccessionPrimary (citable) accession number: Q057X9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: April 16, 2014
This is version 59 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