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Q8UHJ6 (SYI_AGRT5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 78. 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:Atu0686
ORF Names:AGR_C_1230
OrganismAgrobacterium tumefaciens (strain C58 / ATCC 33970) [Reference proteome] [HAMAP]
Taxonomic identifier176299 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex

Protein attributes

Sequence length967 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

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
Nucleotide-binding
   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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 967967Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098339

Regions

Motif64 – 7411"HIGH" region HAMAP-Rule MF_02002
Motif641 – 6455"KMSKS" region HAMAP-Rule MF_02002

Sites

Binding site6001Aminoacyl-adenylate By similarity
Binding site6441ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8UHJ6 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 709A52EC5623ED0F

FASTA967108,483
        10         20         30         40         50         60 
MSDTAEKLDY STTLYLPQTD FPMRAGLPQK EPETVKRWQD MGLYKKLRAS AAGREKFVLH 

        70         80         90        100        110        120 
DGPPYANGNI HIGHALNKIL KDVITRSFQM RGFDANYVPG WDCHGLPIEW KIEEAYRARG 

       130        140        150        160        170        180 
KNKDEVPVNE FRKECRDFAA GWIKVQSEEF KRLGIEGDFE NPYTTMNFHA EARIAGELLK 

       190        200        210        220        230        240 
IARSGQLYRG SKPIMWSVVE RTALAEAEVE YHDVESDMIW VKFPVKDAAP ALSGVSVVIW 

       250        260        270        280        290        300 
TTTPWTIPGN RAIAFSSRVE YGLFEVESAQ NDFGPQTGEK LIFARKLADE AAAKAKLTFK 

       310        320        330        340        350        360 
FVRDVKSEEL AAITCAHPLA SLGYDFPVPL LDGDHVTDDA GTGFVHTAPS HGREDFDAWT 

       370        380        390        400        410        420 
NSVRTLEARG IDTKIPFPVD DAGFYTEDAP GFGPSAEGGA ARVMDDNGKK GDANERVIKA 

       430        440        450        460        470        480 
LIAANNLFAR GRLKHSYPHS WRSKKPVIFR NTPQWFVYMD KELGDGTTLR SRSLDAIDQT 

       490        500        510        520        530        540 
RFVPASGQNR LRAMIEGRPD WVLSRQRSWG VPIAVFADEQ GEVLVDEAVN ARILEAFEAE 

       550        560        570        580        590        600 
GADAWFAEGA KERFLGNDHD HAKWQQVMDI LDVWFDSGCT HTFTLEDRPD MKWPADVYLE 

       610        620        630        640        650        660 
GSDQHRGWFH SSLLESCATR GRAPYNAVVT HGFTMDEQGR KQSKSLGNVV APQDVMKESG 

       670        680        690        700        710        720 
ADILRLWVMT TDYWEDQRLG KAIIQTNIDA YRKLRNTVRW MLGTLAHDNG EEIAYADLPE 

       730        740        750        760        770        780 
LEKLVLHRLS ELDKVVRDGY DAFDFKKITR ALIDFANVEL SAFYFDIRKD TLYCDAPSSL 

       790        800        810        820        830        840 
KRRASLSVIA KLFDCLVTWL APMLPFTTEE AWLSRYPDAE SVHLAQFPEI PAEWKNDALE 

       850        860        870        880        890        900 
AKWEKIRKVR TVVTGALEVE RREKRIGSSL EAAPVVHIAD SDLLAALSGQ DFAEICITSA 

       910        920        930        940        950        960 
ITVVGDEGPA DGFRLQEVAK VVVEQKLAEG VKCARSWRIT TDVGSDPQYP DVSARDAAAL 


RELAALK 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE007869 Genomic DNA. Translation: AAK86495.1.
PIRAH2660.
F97442.
RefSeqNP_353710.1. NC_003062.2.

3D structure databases

ProteinModelPortalQ8UHJ6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176299.Atu0686.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK86495; AAK86495; Atu0686.
GeneID1138191.
KEGGatu:Atu0686.
PATRIC20811077. VBIAgrTum91616_0682.

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAERLMLHQ.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycAGRO:ATU0686-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_AGRT5
AccessionPrimary (citable) accession number: Q8UHJ6
Secondary accession number(s): Q7D0X7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: June 1, 2002
Last modified: May 14, 2014
This is version 78 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