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A9NG38 (SYI_ACHLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. 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:ACL_0702
OrganismAcholeplasma laidlawii (strain PG-8A) [Complete proteome] [HAMAP]
Taxonomic identifier441768 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesAcholeplasmatalesAcholeplasmataceaeAcholeplasma

Protein attributes

Sequence length896 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 – 896896Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000216231

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif584 – 5885"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8691Zinc By similarity
Metal binding8721Zinc By similarity
Metal binding8851Zinc By similarity
Metal binding8881Zinc By similarity
Binding site5431Aminoacyl-adenylate By similarity
Binding site5871ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9NG38 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 9BBDA617784DDC24

FASTA896103,532
        10         20         30         40         50         60 
MNYKDTLLMP KTDFEMRGNL GKREPEIQKH WESIDLYNKV LEKNKDNTPF VLHDGPPYAN 

        70         80         90        100        110        120 
NNIHIGHAFQ KTLKDFVLRY QTMSGRYTPY IPGWDTHGLP IENEVTKSGV DRKQLTRAEF 

       130        140        150        160        170        180 
RKICREYAIK QVEVQRAQFK RLGILGDWDN PYLTLDKSYI ADQVRVFSQM VDKGIIYKGL 

       190        200        210        220        230        240 
KPIYWSPSSE SAFAEAEIEY MDKQSKSIYV GFDMMGDKFP NTKLLIWTTT PWTLPANLAV 

       250        260        270        280        290        300 
SVHPNFDYVW FNNDGKNYIA LKELLPKLVE KLGFSHAKVL KEFKGSTLEF MNYKHPLYDR 

       310        320        330        340        350        360 
VSPIILGEHV TAEDGTGLVH TAPGHGEDDY FVGKKYNLDL LSPVDEKGHM TEEAGPYAGM 

       370        380        390        400        410        420 
FYEKANAQIV EDLRENGHLL YDETITHSYP HDWRTKKPVI FRSTPQWFAS IDMLKGDLLE 

       430        440        450        460        470        480 
AIKGVKWHTS WGEVRLTNMI KDRNDWVISR QRVWGVPIPI FYDNENNPLL DRKLIDHVAS 

       490        500        510        520        530        540 
LFEVHGSDIW YEWDVEKLLP SDYEGPRDLT KELDIMDVWF DSGTSYNILK RRGLPFPADM 

       550        560        570        580        590        600 
YLEGSDQYRG WFNSSLTTAI AVDGVSPYKE IVSHGFVLDG KGRKMSKSLG NVIDPLTVMN 

       610        620        630        640        650        660 
DQGADVLRLW VASVDYEADV RISNDLMKQV SESYRKFRNT FRFMLGVLDG FNPEVNYIGW 

       670        680        690        700        710        720 
SMRGQLNRVM TDKYYVLATK VNESYAKYNF VEVTRLIIPF VVNDLSAFYL DYTKDSLYCD 

       730        740        750        760        770        780 
AEDDFERRAI QSTIYDILLG LLRLLTPIMP HTTSEAYDSL KYKEYDNIYL EKMPIGGKLK 

       790        800        810        820        830        840 
EPKLQENYDI FDELRNHVLK HLELAREAKV IGKSLDAHLD LSVDQTTYDA LEYLDLLNKL 

       850        860        870        880        890 
DKILIVSSVH ITKADQLDIK VSKADGHVCA RCWNIVKEVN QNDVCVRCES VLEGLK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000896 Genomic DNA. Translation: ABX81318.1.
RefSeqYP_001620694.1. NC_010163.1.

3D structure databases

ProteinModelPortalA9NG38.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING441768.ACL_0702.

Proteomic databases

PRIDEA9NG38.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX81318; ABX81318; ACL_0702.
GeneID5803218.
KEGGacl:ACL_0702.
PATRIC20638124. VBIAchLai134690_0682.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycALAI441768:GI40-702-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.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
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.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_ACHLI
AccessionPrimary (citable) accession number: A9NG38
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: February 5, 2008
Last modified: April 16, 2014
This is version 55 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