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Q8K9Z2 (SYI_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BUsg_142
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

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_0000098367

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif604 – 6085"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9031Zinc By similarity
Metal binding9061Zinc By similarity
Metal binding9211Zinc By similarity
Metal binding9241Zinc By similarity
Binding site5631Aminoacyl-adenylate By similarity
Binding site6071ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K9Z2 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: F062A0A37E7132B1

FASTA938110,233
        10         20         30         40         50         60 
MNDYKNTLNL PKTQFSMRAN LSQKEPKILK NWYDNNLYKL IRQKKEGKKI FFLHDGPPYA 

        70         80         90        100        110        120 
NGNIHIGHAV NKILKDIIIK SKNMSGFDAP YIPSWDCHGL PIEQKVEEQM GLKSNNIITT 

       130        140        150        160        170        180 
IFQKKCRKYA EKQIKKQKKD FIRLGVIGDW ENAHLTMDFK NEANIIKTLS KIIEKKYLYK 

       190        200        210        220        230        240 
ESKPIHWCLK CYSSLSDAEI EHFDKESDSI FVAIKSKNNK ILKEVLNLNI SSEKDIYLPI 

       250        260        270        280        290        300 
WTTTPWTLPS SQAITVNPIF EYQIIETKKY NLILAKELVK NVMKILEINH WNILSSFKGK 

       310        320        330        340        350        360 
ILEGKKFLHP FLENISLPVI LGDHVNLDSG TGAVHTAPDH GPDDYIVSQK YKIKTMNLVD 

       370        380        390        400        410        420 
FKGNYINNIH PKLNGVNIFQ ANEIIINLLI KKDCLLHHNI LKHSYPHCWR HKTPVIFRAT 

       430        440        450        460        470        480 
EQWFINIDQK KLRYKTLEEI KKVSWIPKWG GSRIEEMIKK RPDWCVSRQR KWGVPMCLFL 

       490        500        510        520        530        540 
HKKTGKIHPE NTLLIKKIIK KVELEGIEAW WKINLKEMLG ETYNMYNQTF DILDVWFESG 

       550        560        570        580        590        600 
NTHTVIKYKN KKYSKNHADM FLEGSDQHRG WFMSSLIISM LVKNQSPYSE VLTHGFVVDK 

       610        620        630        640        650        660 
NGQKMSKSIG NTISPNEVVK TLGGDILRLW VASSNYSNDI SISNEILKRS SDIYRRIRNT 

       670        680        690        700        710        720 
ARFMLANIND FNPQKNTVLK ENMVLLDRWA ISQAKIVQEE IIEFYKKYNF HAIIKRLMYF 

       730        740        750        760        770        780 
CSIEMGSFYL DIIKDRQYTL KTNSQERRSC QTAIYYIINA LVRWIAPILS FTADEIWNHL 

       790        800        810        820        830        840 
PGKHAQYVFT EEWFNKLFDL DKNDLFNREF WKNLIEMKNE INKFLETEIK NKNINNSLEA 

       850        860        870        880        890        900 
CLILYVTPEV KKTLNILGEE LKFIFLTSKV KIELYNTAPI NSTKSKKISN FKIFLKKIKE 

       910        920        930 
KKCPRCWHYN IFIENNNDKI CTRCILNTKG NGEKRFFI 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67710.1.
RefSeqNP_660499.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9Z2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg142.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67710; AAM67710; BUsg_142.
GeneID1005959.
KEGGbas:BUsg142.
PATRIC21247065. VBIBucAph100086_0146.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-152-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.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 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_BUCAP
AccessionPrimary (citable) accession number: Q8K9Z2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 86 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries