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Q5HGN8 (SYI_STAAC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. 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:SACOL1206
OrganismStaphylococcus aureus (strain COL) [Complete proteome] [HAMAP]
Taxonomic identifier93062 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length917 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 – 917917Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098464

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif595 – 5995"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8861Zinc By similarity
Metal binding8891Zinc By similarity
Metal binding9061Zinc By similarity
Metal binding9091Zinc By similarity
Binding site5541Aminoacyl-adenylate By similarity
Binding site5981ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HGN8 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 800E8384630FB0FC

FASTA917104,886
        10         20         30         40         50         60 
MDYKETLLMP KTDFPMRGGL PNKEPQIQEK WDAEDQYHKA LEKNKGNETF ILHDGPPYAN 

        70         80         90        100        110        120 
GNLHMGHALN KILKDFIVRY KTMQGFYAPY VPGWDTHGLP IEQALTKKGV DRKKMSTAEF 

       130        140        150        160        170        180 
REKCKEFALE QIELQKKDFR RLGVRGDFND PYITLKPEYE AAQIRIFGEM ADKGLIYKGK 

       190        200        210        220        230        240 
KPVYWSPSSE SSLAEAEIEY HDKRSASIYV AFDVKDDKGV VDADAKFIIW TTTPWTIPSN 

       250        260        270        280        290        300 
VAITVHPELK YGQYNVNGEK YIIAEALSDA VAEALDWDKA SIKLEKEYTG KELEYVVAQH 

       310        320        330        340        350        360 
PFLDRESLVI NGDHVTTDAG TGCVHTAPGH GEDDYIVGQK YELPVISPID DKGVFTEEGG 

       370        380        390        400        410        420 
QFEGMFYDKA NKAVTDLLTE KGALLKLDFI THSYPHDWRT KKPVIFRATP QWFASISKVR 

       430        440        450        460        470        480 
QDILDAIENT NFKVNWGKTR IYNMVRDRGE WVISRQRVWG VPLPVFYAEN GEIIMTKETV 

       490        500        510        520        530        540 
NHVADLFAEH GSNIWFEREA KDLLPEGFTH PGSPNGTFTK ETDIMDVWFD SGSSHRGVLE 

       550        560        570        580        590        600 
TRPELSFPAD MYLEGSDQYR GWFNSSITTS VATRGVSPYK FLLSHGFVMD GEGKKMSKSL 

       610        620        630        640        650        660 
GNVIVPDQVV KQKGADIARL WVSSTDYLAD VRISDEILKQ TSDVYRKIRN TLRFMLGNIN 

       670        680        690        700        710        720 
DFNPDTDSIP ESELLEVDRY LLNRLREFTA STINNYENFD YLNIYQEVQN FINVELSNFY 

       730        740        750        760        770        780 
LDYGKDILYI EQRDSHIRRS MQTVLYQILV DMTKLLAPIL VHTAEEVWSH TPHVKEESVH 

       790        800        810        820        830        840 
LADMPKVVEV DQALLDKWRT FMNLRDDVNR ALETARNEKV IGKSLEAKVT IASNDKFNAS 

       850        860        870        880        890        900 
EFLTSFDALH QLFIVSQVKV VDKLDDQATA YEHGDIVIEH ADGEKCERCW NYSEDLGAVD 

       910 
ELTHLCPRCQ QVVKSLV 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: COL.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000046 Genomic DNA. Translation: AAW38043.1.
RefSeqYP_186069.1. NC_002951.2.

3D structure databases

ProteinModelPortalQ5HGN8.
SMRQ5HGN8. Positions 1-917.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93062.SACOL1206.

Proteomic databases

PRIDEQ5HGN8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW38043; AAW38043; SACOL1206.
GeneID3237867.
KEGGsac:SACOL1206.
PATRIC19528656. VBIStaAur112458_1181.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycSAUR93062:GCEP-1191-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_STAAC
AccessionPrimary (citable) accession number: Q5HGN8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 15, 2005
Last modified: April 16, 2014
This is version 74 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