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Q73JB2 (SYI_TREDE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. 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:TDE_2663
OrganismTreponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222) [Complete proteome] [HAMAP]
Taxonomic identifier243275 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema

Protein attributes

Sequence length1100 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 – 11001100Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098568

Regions

Motif48 – 5811"HIGH" region HAMAP-Rule MF_02003
Motif626 – 6305"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6291ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q73JB2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 90A17F4C6F320E8D

FASTA1,100125,760
        10         20         30         40         50         60 
MYKPVDPKVD FAKQEEDVLK FWEKNDVFKK SVSSRDGRDN YIFFDGPPFA TGLPHFGHFV 

        70         80         90        100        110        120 
PGTIKDIIPR YKTMKGFRVE RRFGWDCHGL PVENLIEKEL GLNSKTDIEK YGIDKFNEAC 

       130        140        150        160        170        180 
RASVLRYVKE WKQTITRLGR WVDFENDYKT MEPAFMESIW WVMKSLWEKG LLYEGYYILP 

       190        200        210        220        230        240 
YCPRCSTVLS NHELNLGGYK DVHDPAITVR FKTLSPVKTS PAGKAFEGKN ALPSDTYLLA 

       250        260        270        280        290        300 
WTTTPWTLPS NLGLAVGADI DYALIEYDGA HYIMAVPRLE AYFAKSGKEE AKEYKLIWTK 

       310        320        330        340        350        360 
KGAELEGLRY EPLFPYFKNL AADENGKNAE AGQGAFRVLI GDFVTTEDGT GIVHTAPGFG 

       370        380        390        400        410        420 
EDDNRIFKDT GVPTVCPVDA ECKFTHEVSD YQGLFVKDAD KQIMERLKTE GKLFKKAQIL 

       430        440        450        460        470        480 
HSYPHCWRCS SPLIYRAVAS WFVSVTKIKD KLLNANSKIN WQPDHIKTGR FGKWLEGARD 

       490        500        510        520        530        540 
WAISRNRYWG NPIPIWKCPD CGETICVGSR EELKELSGVF PEDMHKHFVD KISIPCKKCG 

       550        560        570        580        590        600 
GTMKRVSEVL DCWFESGSMP YAQQHYPFEN KEHFEKNFPA DFISEGLDQT RGWFYTLTIL 

       610        620        630        640        650        660 
AAALFDEPAF KNCIVNGLVL AEDGKKMSKS LRNYTDPNEV IKQFGADALR LFLMNSNVVK 

       670        680        690        700        710        720 
ADDLKYSDEG VRDVLKGILI PFWNSYSFYI TYANIDGVKP PHNAKVDGKD EGVEEFLAKL 

       730        740        750        760        770        780 
NNPLDLWILS VTEKLVADVT EALDKYDLSQ AIPPMVEYID LLNNWYIRRS RRRFWKSEND 

       790        800        810        820        830        840 
GDKSQAYETL YRALKKFSLV AAPVVPFITE SIWQNLRTES DALSIHLADY PDYNEKIRNS 

       850        860        870        880        890        900 
ELEFKMKTVQ KAVSMGRALR YQFNLKIRQP LKAVEIVTLN PEEKRVLLEM EESIIEELNV 

       910        920        930        940        950        960 
KEVIFHEKED ELVEYSAKAN FKVLGKELGP LMKKAAAIIE QMNSSEIQNI MEGATLSIDI 

       970        980        990       1000       1010       1020 
EGKSVEITAD KIVINRIEKA SLKIVNEGTL TVGLNTELTE ELLMEGYIRD LVRGIQTLRK 

      1030       1040       1050       1060       1070       1080 
ECGLDVTDRI KLYLSASQKN ADNKELEKAF ELFKDYVCDE TLTVQSSWLK TGELTKLGSI 

      1090       1100 
KTSLVEAGDY EWEIGIEKNN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017226 Genomic DNA. Translation: AAS13180.1.
RefSeqNP_973261.1. NC_002967.9.

3D structure databases

ProteinModelPortalQ73JB2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243275.TDE2663.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS13180; AAS13180; TDE_2663.
GeneID2741108.
KEGGtde:TDE2663.
PATRIC20527384. VBITreDen445_2517.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAKWIISEI.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycTDEN243275:GJ7G-2712-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_TREDE
AccessionPrimary (citable) accession number: Q73JB2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 69 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