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Q9S2X5 (SYI_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. 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:SCO2076
ORF Names:SC4A10.09
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group

Protein attributes

Sequence length1047 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_02003

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003

Cofactor

Zinc By similarity. HAMAP-Rule MF_02003

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02003

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02003.

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_02003

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference 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 – 10471047Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098564

Regions

Motif52 – 6211"HIGH" region HAMAP-Rule MF_02003
Motif600 – 6045"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6031ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9S2X5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 288C99247ADA7666

FASTA1,047116,886
        10         20         30         40         50         60 
MTTPQYRQVP AQVDLPALEH AVLDFWREQK IFAKSLEQSE GRPEWVFYEG PPTANGMPGA 

        70         80         90        100        110        120 
HHIEARVFKD VFPRFRTMRG YHVGRKAGWD CHGLPVELAV EKELGFSGKQ DIEAYGIAEF 

       130        140        150        160        170        180 
NAKCRESVTR HTDAFEELTT RMGYWADLQD PYRTMDPEYI ESVWWSLKEI FNKGLLVQDH 

       190        200        210        220        230        240 
RVAPWCPRCG TGLSDHELAQ GYETVVDPSV YVRFPLTSGP LAGEAALVVW TTTPWTLVSN 

       250        260        270        280        290        300 
TAVAAHPDVT YVVATDGEEK LVVAEPLLAK ALGEGWETTG QSFTGAEMER WTYQRPFELV 

       310        320        330        340        350        360 
EFPEPAHYVV NADYVTTEDG TGLVHQSPAF GEDDLKVCRA YGLPVVNPVR PDGTFEEDVP 

       370        380        390        400        410        420 
LVGGVFFKKA DEKLTEDLET RGLLFKHIPY EHSYPHCWRC HTALLYYAQP SWYIRTTAIK 

       430        440        450        460        470        480 
DRLLQENEKT NWFPDAVKHG RYGDWLNNNI DWALSRNRYW GTPLPIWRCA EDHLTVVGSR 

       490        500        510        520        530        540 
AELTELSGTD QSSLDPHRPF IDDVTFTCAQ EGCSLEAVRV PEVIDAWYDS GSMPFAQWGY 

       550        560        570        580        590        600 
PYKNKELFES RYPAQFISEA IDQTRGWFYT LMAVGTLVFD KSSYENVVCL GHILAEDGRK 

       610        620        630        640        650        660 
MSKHLGNILQ PIPLMDQHGA DAVRWFMAAG GSPWAARRVG HGTIQEVVRK TLLTYWNTVA 

       670        680        690        700        710        720 
FQALYARTTG WAPSEADPAP ADRPVLDRWL LSELHALTDQ VTQALDAYDT QRAGKLLSAF 

       730        740        750        760        770        780 
VDDLSNWYVR RSRRRFWQGD KAALRTLHEV VETVTKLMAP LTPFITERVW QDLVVPVTPG 

       790        800        810        820        830        840 
APESVHLSSW PEADLTAIDP ELSKQMVLVR RLVELGRATR AESGVKTRQP LSRALIAVAG 

       850        860        870        880        890        900 
FDTLSPELHS QITEELNVAS LASLSEVGGS LVDTTAKANF RALGKRFGKR VQDVAKAVAA 

       910        920        930        940        950        960 
ADAAALSLAL REGTASVEVD GETVTLAPDE VIITETPREG WSVASDSGAT VALDLELTEE 

       970        980        990       1000       1010       1020 
LRRAGLARDA IRLIQEARKN SGLDVADRIA LRWTATDPAT IAALTDHSGL ISDEVLATDF 

      1030       1040 
AQGEADDSYG APFTDEGLSL VFRLRKQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL939111 Genomic DNA. Translation: CAB51985.1.
PIRT34946.
RefSeqNP_626335.1. NC_003888.3.

3D structure databases

ProteinModelPortalQ9S2X5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO2076.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB51985; CAB51985; CAB51985.
GeneID1097510.
KEGGsco:SCO2076.
PATRIC23733800. VBIStrCoe124346_2109.

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAERLMLHQ.
OrthoDBEOG644ZM1.
PhylomeDBQ9S2X5.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02003. Ile_tRNA_synth_type2.
InterProIPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
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]
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.
ProtoNetSearch...

Entry information

Entry nameSYI_STRCO
AccessionPrimary (citable) accession number: Q9S2X5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 76 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