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A5GIJ6 (A5GIJ6_SYNPW) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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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 EMBL CAK22761.1
Ordered Locus Names:SynWH7803_0335 EMBL CAK22761.1
OrganismSynechococcus sp. (strain WH7803) [Complete proteome] [HAMAP]
Taxonomic identifier32051 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length968 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

Motif68 – 7811"HIGH" region By similarity HAMAP-Rule MF_02002
Motif625 – 6295"KMSKS" region By similarity HAMAP-Rule MF_02002

Sites

Metal binding9381Zinc By similarity HAMAP-Rule MF_02002
Metal binding9411Zinc By similarity HAMAP-Rule MF_02002
Metal binding9581Zinc By similarity HAMAP-Rule MF_02002
Metal binding9611Zinc By similarity HAMAP-Rule MF_02002
Binding site5841Aminoacyl-adenylate By similarity HAMAP-Rule MF_02002
Binding site6281ATP By similarity HAMAP-Rule MF_02002

Sequences

Sequence LengthMass (Da)Tools
A5GIJ6 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 022836DCB2D0BA68

FASTA968108,194
        10         20         30         40         50         60 
MSKETRDAAE GRPSYKDTLN LLQTGFGMRA NAVKREPELQ AFWRDNGIDG QLGLNNSGPT 

        70         80         90        100        110        120 
FTLHDGPPYA NGALHMGHAL NKVLKDVINK YQVLQGRRVR YVPGWDCHGL PIELKVLQSM 

       130        140        150        160        170        180 
DQEQRQALTP IKLRKKAAAY ARKQVDGQMK GFQRWGIWAD WDQPYLTLQK EYEAAQIKVF 

       190        200        210        220        230        240 
GEMVLKGHIY RGLKPVHWSP SSRTALAEAE LEYPDGHTSP SVYVAFPAVE VPVPLRETLQ 

       250        260        270        280        290        300 
SHGVELPADA AALGQALQVA IWTTTPWTLP ANLAVSVNER LDYALVDDGN GRLLVVAAEL 

       310        320        330        340        350        360 
IESLSKTLER PLQQRATVKG ALLAGLVYRH PLLDRTSPVV IGGDYITTES GTGLVHTAPG 

       370        380        390        400        410        420 
HGVDDFHTGQ KHGLPVLCPV DEAGTLTAEA GPFAGLNVLK DANPGIIEAL EQAGALLKQE 

       430        440        450        460        470        480 
AYSHRYPYDW RTKKPTIFRA TEQWFASVEG FRQDALDAID QVQWTPASGR NRIEAMVKER 

       490        500        510        520        530        540 
GDWCISRQRT WGVPIPVFYH RSNGEVLLNA DTLSHIETLI AAHGGDVWWE KDEADLLPPA 

       550        560        570        580        590        600 
YADQADQWRK GTDTMDVWFD SGSSWAAVSS QRESLSYPAD LYLEGSDQHR GWFQSSLLTS 

       610        620        630        640        650        660 
VAVNGHAPYK RVLTHGFALD EKGRKMSKSL GNVVDPMVII EGGKNQKQEP AYGADVLRLW 

       670        680        690        700        710        720 
VSSVDYSTDV PIGAGILRQL ADVYRKVRNT SRYLLGNLHD FNPATDAIAV EDLPLLDRWM 

       730        740        750        760        770        780 
LQRTAEVMDE ITEAFESYEF FRFFQLLQNF CVTDLSNFYL DIAKDRLYVS APADRRRRSC 

       790        800        810        820        830        840 
QTVMALIIER LAGLIAPVLC HMAEDIWQNL PYPVEETSVF QRGWPTAPDR WRDASLNEPM 

       850        860        870        880        890        900 
QQLRELRTSV NKVLEDCRSR GELGASLEAA VRLEAHNPSL QSALQWLNDQ GHAEVDGLRD 

       910        920        930        940        950        960 
WLLVSQLQIG GEPWAELLAN HDDDVALIEV ARARGSKCER CWHYESDVGQ HADHPHLCGR 


CVSVLGRL 

« Hide

References

[1]Genoscope
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WH7803.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CT971583 Genomic DNA. Translation: CAK22761.1.
RefSeqYP_001224058.1. NC_009481.1.

3D structure databases

ProteinModelPortalA5GIJ6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING32051.SynWH7803_0335.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAK22761; CAK22761; SynWH7803_0335.
GeneID5146786.
KEGGsyx:SynWH7803_0335.
PATRIC23826716. VBISynSp43824_0339.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

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 nameA5GIJ6_SYNPW
AccessionPrimary (citable) accession number: A5GIJ6
Entry history
Integrated into UniProtKB/TrEMBL: June 12, 2007
Last sequence update: June 12, 2007
Last modified: April 16, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)