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Q9X7E5 (SYI_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 88. 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:ML1195
ORF Names:MLCB458.10
OrganismMycobacterium leprae (strain TN) [Complete proteome] [HAMAP]
Taxonomic identifier272631 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length1059 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 – 10591059Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098548

Regions

Motif59 – 6911"HIGH" region HAMAP-Rule MF_02003
Motif637 – 6415"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6401ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9X7E5 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 67FC7659E9399E39

FASTA1,059119,809
        10         20         30         40         50         60 
MTNSAYPRTD LGADQRGGSP NFPALEAQVL DYWSNDDTFR ASIARCDDAP EYVFYDGPPF 

        70         80         90        100        110        120 
ANGLPHYGHL LTGYVKDIVP RYRTMCGYKV ERRFGWDTHG LPAELEVERQ LGITDKSQID 

       130        140        150        160        170        180 
AMGIAAFNEA CRKSVLRYTE EWQAYVTRQA RWVDFDNDYK TLDLSYMESV IWAFKQLWDK 

       190        200        210        220        230        240 
GLAYESYRVL PYCWRDETPL SNHELRMDDD VYQSRQDPAV TLGFKVLGGD DEDLVGAYLL 

       250        260        270        280        290        300 
VWTTTPWTLP SNLAVAVHPD VTYVDVRAGD RRFVLAQARL TAYARELGDE PEVLATYRGA 

       310        320        330        340        350        360 
DLLGRHYLPP FQYFYESARN AFQVLPGDFV TTDDGTGIVH IAPAYGEDDM ATADKVGIVP 

       370        380        390        400        410        420 
VTPVDSNGCF DATVPDYQGQ HVFEANAQII RDLKNQSGSA AVNGAVLLRH ETYEHPYPHC 

       430        440        450        460        470        480 
WRCRNPLIYR AVSSWFVAVT EFRDRMVELN QQITWYPEHV KDGQFGKWLQ GARDWSISRN 

       490        500        510        520        530        540 
RYWGTPIPVW KSDDPDYPRI DVYGSLDELE RDFGVRPTNL HRPYIDELTR PNPDDPTGLS 

       550        560        570        580        590        600 
TMRRIPDVFD VWFDSGSMPY AQVHYPFEND DWFDGFDSAD SDKQVDAHYP GDFIVEYIGQ 

       610        620        630        640        650        660 
ARGWFYTLHV LATALFDRPA FKTCIAHGVV LGSNGQKMSK SLRNYPDVTE IFDRDGSDAM 

       670        680        690        700        710        720 
RWFLMASPIL RGGNLIITEP GIREGMRQVL LPLWNAYSFL ALYAPKIGTW HTDVSHVLDR 

       730        740        750        760        770        780 
YILAKLAVLR DDLSQAMEVC DISGACEQLR QFTEPLTNWY LRRSRARFWD EDVDAIDTLH 

       790        800        810        820        830        840 
TVLEVTARLA APLLPLITEI IWRSVTGGRS VHLTDWPQAN QLPADPDLVA VMDQVRQVCS 

       850        860        870        880        890        900 
AASSLRKAKK LRVRLPLPKL VVAVYNSQRL KPYIDLIGDE LNVKQIELTD AIDTYGRFEF 

       910        920        930        940        950        960 
TVNARVAGPR LGRDVQAAIK VVKAGEGVAN PDGTLTAGPV VLQPDEYSSR LVAANPEFTA 

       970        980        990       1000       1010       1020 
ELPDGSGLVV LDDTVTPELE AEGWAKDRIR ELQELRKLIG LDVSDRIRVL MSVPAERADW 

      1030       1040       1050 
ARVHRDFIAR EILATSFEFG EPADSVAIGD GVRVSLLKV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL049478 Genomic DNA. Translation: CAB39575.1.
AL583921 Genomic DNA. Translation: CAC31576.1.
PIRE87058.
RefSeqNP_301871.1. NC_002677.1.

3D structure databases

ProteinModelPortalQ9X7E5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272631.ML1195.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC31576; CAC31576; CAC31576.
GeneID910297.
KEGGmle:ML1195.
PATRIC18054508. VBIMycLep78757_2194.

Organism-specific databases

LepromaML1195.
CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMARVEHMVE.
OrthoDBEOG644ZM1.

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.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. 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.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_MYCLE
AccessionPrimary (citable) accession number: Q9X7E5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: May 14, 2014
This is version 88 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