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Q5FKU5 (SYI_LACAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 71. 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:LBA0817
OrganismLactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) [Complete proteome] [HAMAP]
Taxonomic identifier272621 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length927 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 – 927927Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098401

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif594 – 5985"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8861Zinc By similarity
Metal binding8891Zinc By similarity
Metal binding9061Zinc By similarity
Metal binding9091Zinc By similarity
Binding site5531Aminoacyl-adenylate By similarity
Binding site5971ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5FKU5 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: F62F379E86F0D5E9

FASTA927106,244
        10         20         30         40         50         60 
MRIKDTLNLG KTKFKMRGNL PVREAEWEKE WEDNHLYEQR LKLNEGHPRF DLHDGPPFAN 

        70         80         90        100        110        120 
GNIHMGHALN KISKDIIVRY KNMNGYYAPY VPGWDTHGLP VEQQLAKKGI DRKTMDRAKY 

       130        140        150        160        170        180 
RELCRQYAEE QVQKQMTDFK RLGVMADWDN PYITLQHEFE GQEIRVFGEM YKKGYIYKGK 

       190        200        210        220        230        240 
KPVYWSWSSE STLAEAEVEY KDVEANSIFV AFPVVDSKGI IDPKDTYFVI WTTTPWTIPA 

       250        260        270        280        290        300 
NEAICVNPKF DYSVVQVGDK KYVVATGLLD KVAEEIGWDD YKVVQTVKGA DMEYMKAKHP 

       310        320        330        340        350        360 
LYDKESLVTE GFHVTLDDGT GLVHTAPGFG ADDFNVGQKY DLPVFSPVDA HGRYTDEVPE 

       370        380        390        400        410        420 
LEGMFYQDVD KLMVEKLKDA GALLKLKVFT HSYPHDWRTK KPVIFRATTQ WFASIAPFRD 

       430        440        450        460        470        480 
QILEQIDNAK FIPSWGKTRL YNMIKDRGDW VISRQRAWGV PLPIFYAEDG TPIVTPETIE 

       490        500        510        520        530        540 
HIAEIFDKEG SNAWYTHTAK ELLPEGFTSE HSPNGEFTKE KDILDVWFDS GSSWSGVMEK 

       550        560        570        580        590        600 
RDGLHYPADL YLEGSDQYRG WFNSSLITSV AVTGKAPYKE VLSQGFVLDD KGHKMSKSLG 

       610        620        630        640        650        660 
NVISPNDVIK RMGAEIIRLW VAQADTTSDV AVSMGILQQS AESYRKIRNT FRYMLANTSD 

       670        680        690        700        710        720 
FDPKENGVAY DDLRSVDQYM EIKLNDLVAE CLAAYDKFDF TTVFKKIFNF ISNDLSAFYL 

       730        740        750        760        770        780 
DFAKDVLYIE GKNSLERRSM QTVIYDAAVK LTKILTPILP HTMEEIWGFL KEPEDYVQLA 

       790        800        810        820        830        840 
NMPKVENYTN HDELLENWGK FMNLRDDVLK ALEDARNKKL IGKSFEAAVT IYPDKETKAM 

       850        860        870        880        890        900 
LDDLDADFRQ ILIVSKLTIV DGEAPENAEK LNNASIVVEH AEGEVCPRCR MIRTDIGEDP 

       910        920 
KLPELCERCA KIVEEDFPEA AQEGLEE 

« Hide

References

[1]"Complete genome sequence of the probiotic lactic acid bacterium Lactobacillus acidophilus NCFM."
Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L., McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S., Hamrick A., Cano R., Klaenhammer T.R.
Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700396 / NCK56 / N2 / NCFM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000033 Genomic DNA. Translation: AAV42679.1.
RefSeqYP_193710.1. NC_006814.3.

3D structure databases

ProteinModelPortalQ5FKU5.
SMRQ5FKU5. Positions 1-915.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272621.LBA0817.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV42679; AAV42679; LBA0817.
GeneID3251646.
KEGGlac:LBA0817.
PATRIC22196728. VBILacAci7974_0779.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

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_LACAC
AccessionPrimary (citable) accession number: Q5FKU5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2005
Last modified: May 14, 2014
This is version 71 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