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P41972 (SYI1_STAAU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. 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
OrganismStaphylococcus aureus
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length917 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Subunit structure

Monomer.

Subcellular location

Cytoplasm 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 term3D-structure
Direct protein sequencing
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_0000098463

Regions

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

Sites

Metal binding8861Zinc
Metal binding8891Zinc
Metal binding9061Zinc
Metal binding9091Zinc
Binding site5541Aminoacyl-adenylate
Binding site5981ATP By similarity
Binding site6321tRNA
Binding site6401tRNA

Secondary structure

................................................................................................................................................................ 917
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P41972 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 8A2B644A03A85636

FASTA917104,885
        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 AFNVKDDKGV 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]"Analysis and toxic overexpression in Escherichia coli of a staphylococcal gene encoding isoleucyl-tRNA synthetase."
Chalker A.F., Ward J.M., Fosberry A.P., Hodgson J.E.
Gene 141:103-108(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 9144 / Oxford / NCIB 6571 / NCTC 6571.
[2]"Insights into editing from an Ile-tRNA synthetase structure with tRNAIle and mupirocin."
Silvian L.F., Wang J., Steitz T.A.
Science 285:1074-1077(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH METAL IONS; ILE-TRNA AND MUPIROCIN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X74219 Genomic DNA. Translation: CAA52296.1.
PIRS40178.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFYX-ray2.20A1-917[»]
1QU2X-ray2.20A1-917[»]
1QU3X-ray2.90A1-917[»]
ProteinModelPortalP41972.
SMRP41972. Positions 1-917.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL1982.
DrugBankDB00410. Mupirocin.

Proteomic databases

PRIDEP41972.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Other

EvolutionaryTraceP41972.

Entry information

Entry nameSYI1_STAAU
AccessionPrimary (citable) accession number: P41972
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 98 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries