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Q82AC9 (SYI_STRAW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. 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:SAV_6130
OrganismStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680) [Complete proteome] [HAMAP]
Taxonomic identifier227882 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

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
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_0000098563

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
Q82AC9 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: B08ACA994C0BA6BA

FASTA1,047117,130
        10         20         30         40         50         60 
MKPPQYRQVP AQVDLPALEH AVLDFWREQK IFAKSLEQSE GRPEWVFYEG PPTANGMPGA 

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

       130        140        150        160        170        180 
NAKCRESVTR HTDAFEELTS RMGYWTDLND PYRTMDPEYI ESVWWSLKEI FNKGLLVQDY 

       190        200        210        220        230        240 
RVAPWCPQDE TGLSDHELAQ GYETIVDPSV YVRFPLTSGP LAGRAALLVW TTTPWTLVSN 

       250        260        270        280        290        300 
TAVAAHPDVT YVVATNGEEK LVVAEPLVEK ALGEGWETTG ETFTGAEMER WTYQRPFELV 

       310        320        330        340        350        360 
EFPAPAHYVV NAEYVTTEDG TGLVHQSPAF GEDDLKVCRE YGLPVVNPVR TNGTFEEDVP 

       370        380        390        400        410        420 
LVGGVFFKKA DEKLTEDLQN RGLLFKHIPY EHSYPHCWRC HTALLYYAQP SWYIRTTAVK 

       430        440        450        460        470        480 
DRLLQENEKT NWFPESVKHG RFGDWLNNNV DWALSRSRFW GTPLPLWTCE EGHLTCVGSR 

       490        500        510        520        530        540 
AELSELTGTD QSNLDPHRPF IDAVTFACPQ DGCGRTATRV 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 
FQALYARTSG WAPSEADPAP ADRPVLDRWL LSELHALTDQ VTQALESYDT QRAGKLLSAF 

       730        740        750        760        770        780 
VDDLSNWYVR RSRRRFWQGD KAALRTLHEV VETVTRLMAP LTPFITERVW QDLVFPVTPG 

       790        800        810        820        830        840 
APESVHLASW PEADLSAIDP ELSKQMVLVR RLVELGRATR AESGVKTRQP LSRALVAVAG 

       850        860        870        880        890        900 
FETLDRELHA QITEELNVTS LAALSEVGGS LVDTTAKANF RALGKRFGKG VQAVAKAVAG 

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

       970        980        990       1000       1010       1020 
LRQAGLARDA IRLIQEARKN SGLDVADRIA LRWTSTDPEV IAALSEHSEL IADEVLATDF 

      1030       1040 
AQGEADDTYG EPFTDESLSL TFRLRKA 

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000030 Genomic DNA. Translation: BAC73841.1.
RefSeqNP_827306.1. NC_003155.4.

3D structure databases

ProteinModelPortalQ82AC9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227882.SAV_6130.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC73841; BAC73841; SAV_6130.
GeneID1211413.
KEGGsma:SAV_6130.
PATRIC23726294. VBIStrAve112782_6500.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAPRFKTMK.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycSAVE227882:GJU1-6210-MONOMER.

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_STRAW
AccessionPrimary (citable) accession number: Q82AC9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 75 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