Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C6CJ51 (C6CJ51_DICZE) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Isoleucine--tRNA ligase HAMAP-Rule MF_02002

EC=6.1.1.5 HAMAP-Rule MF_02002
Alternative name(s):
Isoleucyl-tRNA synthetase HAMAP-Rule MF_02002
Gene names
Name:ileS HAMAP-Rule MF_02002
Ordered Locus Names:Dd1591_0548 EMBL ACT05430.1
OrganismDickeya zeae (strain Ech1591) [Complete proteome] [HAMAP] EMBL ACT05430.1
Taxonomic identifier561229 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

Protein attributes

Sequence length941 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 SAAS SAAS002301

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02002 SAAS SAAS002301

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_02002 SAAS SAAS002301

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02002 SAAS SAAS002301

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02002 SAAS SAAS002301.

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. HAMAP-Rule MF_02002

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Motif58 – 6811"HIGH" region By similarity HAMAP-Rule MF_02002
Motif606 – 6105"KMSKS" region By similarity HAMAP-Rule MF_02002

Sites

Metal binding9041Zinc By similarity HAMAP-Rule MF_02002
Metal binding9071Zinc By similarity HAMAP-Rule MF_02002
Metal binding9241Zinc By similarity HAMAP-Rule MF_02002
Metal binding9271Zinc By similarity HAMAP-Rule MF_02002
Binding site5651Aminoacyl-adenylate By similarity HAMAP-Rule MF_02002
Binding site6091ATP By similarity HAMAP-Rule MF_02002

Sequences

Sequence LengthMass (Da)Tools
C6CJ51 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: B50EF4CDAB815911

FASTA941104,510
        10         20         30         40         50         60 
MSDYKTTLNL PETGFPMRGD LAKREPDMLK RWYEQDLYGI IRGAKKGKKT FILHDGPPYA 

        70         80         90        100        110        120 
NGNIHIGHSV NKILKDIIIK SKGLSGYDSP YVPGWDCHGL PIELKVEQLV GKPGEKVSAA 

       130        140        150        160        170        180 
QFRAECRKYA AEQVAGQKKD FIRLGVLGDW DRPYLTMDFK TEANIIRALG RIIENGHLHK 

       190        200        210        220        230        240 
GAKPVHWCAD CGSALAEAEV EYYDKTSPAI DVAFNAVDRA AVLAKFGLTA DAVDGDVALV 

       250        260        270        280        290        300 
IWTTTPWTLP ANRAIALNAD IDYVLIQVAG KAIIVAQGLA DAVIKRVAGN DASLLLGHTV 

       310        320        330        340        350        360 
KGSDLELLRF RHPFMGFDVP AILGDHVTLD AGTGAVHTAG GHGPDDYVIS QKYQLEIANP 

       370        380        390        400        410        420 
VGPNGCYLAG TFPELDGLFV FKANDKIVEL LRERGALLHH EKLQHSYPCC WRHKSPILFR 

       430        440        450        460        470        480 
ATPQWFVSMD QNGLRKQSLS EIKGVQWIPD WGQARIESMV ANRPDWCISR QRTWGVPMSL 

       490        500        510        520        530        540 
FVHKETQALH PRTAELIEAV AKRVEQDGIQ AWWDLNPADL LGAEAAEYEK VPDTLDVWFD 

       550        560        570        580        590        600 
SGSTHASVVD VRPEFSGHAA DMYLEGSDQH RGWFMSSLMI STAIKGKAPY RQVLTHGFTV 

       610        620        630        640        650        660 
DGQGRKMSKS IGNTVSPQDV MDKLGADILR LWIGSTDYSG EIAVSDEILK RSADAYRRIR 

       670        680        690        700        710        720 
NTARFLLANL NGFDPAQHSV KPEDMVVLDR WAVGCAKAAQ DEIVDAYESY DFHHVVQRLM 

       730        740        750        760        770        780 
QFCSIEMGSF YLDIIKDRQY TAKHDSVARR SCQTALFHIA EALVRWMAPI MSFTADEIWA 

       790        800        810        820        830        840 
YLPGERAQFV FTEEWYDGLF GLADSESMND TFWADMLNVR GEVNKVIEQA RNDKRIGGSL 

       850        860        870        880        890        900 
EAAVTLYADD ALFAQLGRLQ GELHFALLTS KAHLAHYEDA PADAQQSELP GLKVVLTKAD 

       910        920        930        940 
GEKCPRCWHY ETDIGSDAAH PDVCGRCATN VGGNGEERKF V 

« Hide

References

[1]"Complete sequence of Dickeya zeae Ech1591."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Balakrishnan V., Glasner J., Perna N.T.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ech1591 EMBL ACT05430.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001655 Genomic DNA. Translation: ACT05430.1.
RefSeqYP_003002909.1. NC_012912.1.

3D structure databases

ProteinModelPortalC6CJ51.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561229.Dd1591_0548.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT05430; ACT05430; Dd1591_0548.
GeneID8119831.
KEGGdze:Dd1591_0548.
PATRIC21796948. VBIDicZea111179_0555.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycDZEA561229:GJ85-567-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.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 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 nameC6CJ51_DICZE
AccessionPrimary (citable) accession number: C6CJ51
Entry history
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: April 16, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)