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

A1AW09 (SYI_RUTMC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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:Rmag_0340
OrganismRuthia magnifica subsp. Calyptogena magnifica [Complete proteome] [HAMAP]
Taxonomic identifier413404 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriasulfur-oxidizing symbionts

Protein attributes

Sequence length922 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 – 922922Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022113

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif593 – 5975"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8851Zinc By similarity
Metal binding8881Zinc By similarity
Metal binding9051Zinc By similarity
Metal binding9081Zinc By similarity
Binding site5521Aminoacyl-adenylate By similarity
Binding site5961ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A1AW09 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: CF5316BC7F9E8F8A

FASTA922105,262
        10         20         30         40         50         60 
MSDYKSSLNL PATQFPMKAN LANREGGFLK KWQNDGLYDQ IRQQNQGKPK FVLHDGPPYA 

        70         80         90        100        110        120 
NGDIHIGHTV NKVLKDMIVK SKSLSGFDAP YVPGWDCHGL PIEFNVEKKY GKVGVKIDAS 

       130        140        150        160        170        180 
TFRSKCRKYA DQQVLKQKQD FQRLGILSDW DNPYLTKDFQ YESDIVRALG RIVKNGHVSK 

       190        200        210        220        230        240 
GYKPVHWCTE CGSALAETEV EYKDNQSEAI DVKFRIIDDS VFNMNKPVSV VIWTTTPWTL 

       250        260        270        280        290        300 
PANEAVALHP ELNYVLVDIG DEYLLLAQAL VETSISRYGI EATIGEQTFS GSELEGLKIK 

       310        320        330        340        350        360 
HPFYDKQVPI ILGEYVTIDA GTGAVHTAPA HGQEDFIVGL KYNLPVECLV DIKGVFFKET 

       370        380        390        400        410        420 
ELLGGQFIFK ANDSVIEILK QANTLVKHES LMHSYPHCWR HKTPVIFRAT PQWFISMQKN 

       430        440        450        460        470        480 
GLIDTVNREI SKVQWMPDWG KKRIELMMDS RPDWCISRQR FWGVPITLFV HKQTGELHPN 

       490        500        510        520        530        540 
TQALFVSIAN RIEKEGIEAW FKSDAQDFIG NDANDYDKTT DILDVWFDSG VSHFTVLKAR 

       550        560        570        580        590        600 
KELSNVADLY LEGADQHRGW FQLSLISSVA INGKAPYKNV LTHGFVVDKN GKKMSKSLGN 

       610        620        630        640        650        660 
VMSPQKIVNN LGADVLRLWI ASTDYTSEMT VGDEILKRSA DSYRRIRNTM RFMLANMQAF 

       670        680        690        700        710        720 
NPVEHLLDNK QMLDLDKWIV AKTANLQTQI IKAYEQYNFH HVVQLILNFC SNDLGGFYLD 

       730        740        750        760        770        780 
VIKDRQYTTQ ANSLARRSAQ SALHHITEAM VRWLAPILSF TAEEIWQNMP SEKNTSIFLA 

       790        800        810        820        830        840 
SWYQDLTFGY ENKAIDITRE ISPFIRKQME GMRGEKIIGS SLESEIDIYC ETDIFSTLSQ 

       850        860        870        880        890        900 
LDDELRFIFI TSYIRIHSLN EKNDDCIKAI EGVFIKVSKS RHEKCVRCWH HREDVGNNAK 

       910        920 
HPELCGRCVE NVDGKGEIRK FA 

« Hide

References

[1]"The Calyptogena magnifica chemoautotrophic symbiont genome."
Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J., Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M., Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.
Science 315:998-1000(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000488 Genomic DNA. Translation: ABL02116.1.
RefSeqYP_903587.1. NC_008610.1.

3D structure databases

ProteinModelPortalA1AW09.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING413404.Rmag_0340.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL02116; ABL02116; Rmag_0340.
GeneID4554628.
KEGGrma:Rmag_0340.
PATRIC32000323. VBICanRut45856_0386.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKKRIELM.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycCRUT413404:GHM7-353-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 nameSYI_RUTMC
AccessionPrimary (citable) accession number: A1AW09
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 58 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