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B9DPP7 (SYI_STACT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 43. 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:Sca_0806
OrganismStaphylococcus carnosus (strain TM300) [Complete proteome] [HAMAP]
Taxonomic identifier396513 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length915 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 – 915915Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189198

Regions

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

Sites

Metal binding8851Zinc By similarity
Metal binding8881Zinc By similarity
Metal binding9051Zinc By similarity
Metal binding9081Zinc By similarity
Binding site5541Aminoacyl-adenylate By similarity
Binding site5981ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B9DPP7 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: CD884BE7F8D48E30

FASTA915105,313
        10         20         30         40         50         60 
MNYKDTLLMP KTDFPMRGGL PKKEPEIQKQ WDEQDLYHKI LEKNKGHESY ILHDGPPYAN 

        70         80         90        100        110        120 
GNLHMGHALN KILKDFIVRY KSMQGYYSPY VPGWDTHGLP IEQALTKKGV KRKEMPISEF 

       130        140        150        160        170        180 
RKLCEEFALE QIDIQKKDFK RLGVNGDFND PYITLKPEYE AAQIRLFGEM ADRGLIYKGK 

       190        200        210        220        230        240 
KPVYWSPSSE SSLAEAEIEY HDKRSPSIYV AFDVKDGKGV VDEDAKFIIW TTTPWTLPSN 

       250        260        270        280        290        300 
VAITVHPDLK YGQYNVNGEK YVVGQDLVEE VAEELGWDKE DIQLEKEFTG KELEYVETQH 

       310        320        330        340        350        360 
PFIDRVSLVI NGLHVTTDAG TGAVHTAPGH GEDDYIVGQK YNLPVISPLN DKGVFTEEGG 

       370        380        390        400        410        420 
QFEGMFYDKA NKAVTDLLKE NGSLLKLKFI THSYPHDWRT KKPVIFRATP QWFASISKVR 

       430        440        450        460        470        480 
QDILDAIEDT NFKVDWGKTR IYNMIRDRGE WVISRQRVWG VPLPVFYTEN GDIIMDKEVI 

       490        500        510        520        530        540 
YHVANLFEKY GSNVWFDRDA KDLLPEGFTH PGSPNGEFTK EEDIMDVWFD SGSSHRGVLE 

       550        560        570        580        590        600 
TRPELSFPAD LYLEGSDQYR GWFNSSITTA VATRGQSPYK FLLSHGFVMD GEGKKMSKSL 

       610        620        630        640        650        660 
GNVIVPDQIV KQKGADIARL WVSSVDYLSD VRISDEILKQ TADVYRKIRN TLRFMLGNVN 

       670        680        690        700        710        720 
DFNPETDAVP ESDLLEVDRY LLNRLREFTE SIINHYDNFD YLNIYQEVQN FINVELSNFY 

       730        740        750        760        770        780 
LDYGKDILYI EKQDSHKRRS MQTVLYQILV DMTKLLAPIL AHTSEEVWSY IPHVKEESVH 

       790        800        810        820        830        840 
LADMPEVVKP DEELLEKWNT FMKLRDDVNR ALEEARNNKV IGKSLEAKVI IGSNESFDAA 

       850        860        870        880        890        900 
DFLKDFENLH QLFIVSQVEV EEKVEDGNEY YYGDIKVVHA DGEKCERCWN YSTELGSVNG 

       910 
LDHLCPRCQG VVADL 

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References

[1]"Genome analysis of the meat starter culture bacterium Staphylococcus carnosus TM300."
Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C., Goetz F.
Appl. Environ. Microbiol. 75:811-822(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TM300.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM295250 Genomic DNA. Translation: CAL27716.1.
RefSeqYP_002633901.1. NC_012121.1.

3D structure databases

ProteinModelPortalB9DPP7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING396513.Sca_0806.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7550289.
KEGGsca:Sca_0806.
PATRIC19602386. VBIStaCar105558_0807.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMALGRRSCQ.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycSCAR396513:GJ9G-821-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_STACT
AccessionPrimary (citable) accession number: B9DPP7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 43 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