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

Q7U9G9 (SYI_SYNPX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. 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:SYNW0289
OrganismSynechococcus sp. (strain WH8102) [Complete proteome] [HAMAP]
Taxonomic identifier84588 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length974 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

Cofactor

Binds 1 zinc ion per subunit By similarity. 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
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 – 974974Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098491

Regions

Motif69 – 7911"HIGH" region HAMAP-Rule MF_02002
Motif626 – 6305"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9391Zinc By similarity
Metal binding9421Zinc By similarity
Metal binding9591Zinc By similarity
Metal binding9621Zinc By similarity
Binding site5851Aminoacyl-adenylate By similarity
Binding site6291ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7U9G9 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: DF0058516CAE6565

FASTA974108,998
        10         20         30         40         50         60 
MSKETRDAAA EGRPSYKDTL NLLQTGFGMR ANAVKREPEL QAFWSDNGID GQLGLQNDGP 

        70         80         90        100        110        120 
TFTLHDGPPY ANGALHMGHA LNKVLKDVIN KYQVLKGRRV RYVPGWDCHG LPIELKVLQS 

       130        140        150        160        170        180 
MDQEQRKALT PIKLRKKAAA YARKQVDGQM KGFQRWGIWA DWEQPYLTLQ KEYEAAQIKV 

       190        200        210        220        230        240 
FGEMVLKGHI YRGLKPVHWS PSSRTALAEA ELEYPDGHTS PSVYVAFPAM EVPTPLRDAL 

       250        260        270        280        290        300 
KAEGLELPTE TDALRQALQV AIWTTTPWTL PANLAVSVNE RLDYALVDDG SGRMLVVAAD 

       310        320        330        340        350        360 
LIESLSTTLE RPLKHRATVK GALLAGLIYR HPLLDRTSPV VIGGEYITTE SGTGLVHTAP 

       370        380        390        400        410        420 
GHGVDDFHTG QKHGLPVLCP VDEAGTLTAE AGPFAGLNVL KDANPGIIEA LEQAGALLKQ 

       430        440        450        460        470        480 
EAYSHRYPYD WRTKKPTIFR ATEQWFASVE GFRQDALDAI DQVQWTPASG RNRIEAMVKE 

       490        500        510        520        530        540 
RGDWCISRQR TWGVPIPVFY HHSNGEVLLN ADTLSHIETL IASHGADVWW EKDETDLLPP 

       550        560        570        580        590        600 
AYANQADQWR KGTDTMDVWF DSGSSWAAVS SQRESLSYPA DLYLEGSDQH RGWFQSSLLT 

       610        620        630        640        650        660 
SVAVNGHAPY KRVLTHGFAL DEKGRKMSKS LGNVVDPMVI IEGGKNQKQE PPYGADVLRL 

       670        680        690        700        710        720 
WVSSVDYSAD VPIGAGILRQ LADVYRKVRN TSRYLLGNLH DFNPASDAIA VADLPLLDRW 

       730        740        750        760        770        780 
MLQRTAEVMH EITEAFESYE FFRFFQLLQN FCVTDLSNFY LDIAKDRLYV SAPTDQRRRS 

       790        800        810        820        830        840 
CQTVMALIIE RLAGFIAPVL CHMAEDIWQN LPYPVQETSV FQRGWPTIPS DWRNDTLSAP 

       850        860        870        880        890        900 
VQQLRDLRAA VNKVLEDCRG RQELGASLEA AVRIDARSPE LQAALSWLND NGDPDVDGLR 

       910        920        930        940        950        960 
DWLLVSQLQL GGEPWAEVLS NHEDELALIE VSRARGTKCE RCWHYEGDVG QHPDHAHICG 

       970 
RCVGVLERRT HQLV 

« Hide

References

[1]"The genome of a motile marine Synechococcus."
Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P., Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T., Dufresne A., Partensky F., Webb E.A., Waterbury J.
Nature 424:1037-1042(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WH8102.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX569689 Genomic DNA. Translation: CAE06804.1.
RefSeqNP_896384.1. NC_005070.1.

3D structure databases

ProteinModelPortalQ7U9G9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING84588.SYNW0289.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE06804; CAE06804; SYNW0289.
GeneID1732105.
KEGGsyw:SYNW0289.
PATRIC23831959. VBISynSp27240_0292.

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 nameSYI_SYNPX
AccessionPrimary (citable) accession number: Q7U9G9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2003
Last modified: April 16, 2014
This is version 70 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