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A8AW24 (SYI_STRGC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:SGO_0681
OrganismStreptococcus gordonii (strain Challis / ATCC 35105 / CH1 / DL1 / V288) [Complete proteome] [HAMAP]
Taxonomic identifier29390 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length930 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 – 930930Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000088560

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif595 – 5995"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8881Zinc By similarity
Metal binding8911Zinc By similarity
Metal binding9081Zinc By similarity
Metal binding9111Zinc By similarity
Binding site5541Aminoacyl-adenylate By similarity
Binding site5981ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8AW24 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 0B7AED6F835C95F2

FASTA930105,189
        10         20         30         40         50         60 
MKLKETLNLG KTDFPMRAGL PTKEPVWQKE WEEAKLYQRR QELNQGKPHF TLHDGPPYAN 

        70         80         90        100        110        120 
GNIHVGHAMN KISKDIIVRS KSMSGFYAPY IPGWDTHGLP IEQVLAKQGV KRKEMDLVEY 

       130        140        150        160        170        180 
LKLCREYALS QVDKQREDFK RLGVSGDWEN PYVTLTPDYE AAQIRVFGEM AKKGYIYRGA 

       190        200        210        220        230        240 
KPVYWSWSSE SALAEAEIEY HDLLSTSLYY ANRVKDGKGV LDTDTYIVVW TTTPFTITAS 

       250        260        270        280        290        300 
RGLTVGADID YVLVQPAGES RKFVVASELL NSLSEKFGWA DVQVLATYRG QELNHIVTVH 

       310        320        330        340        350        360 
PWDTAVDELV ILGDHVTTDS GTGIVHTAPG FGEDDYNVGV ANGLEVAVTV NERGIMMENA 

       370        380        390        400        410        420 
GPEFAGQFYD KVVPTVIEKL GDLLLAQEEI SHSYPFDWRT KKPIIWRAVP QWFASVSKFR 

       430        440        450        460        470        480 
QEILDEIEKV KFHSEWGKVR LYNMIRDRGD WVISRQRAWG VPLPIFYAED GTPIMTVETI 

       490        500        510        520        530        540 
EHVAQLFEEH GSIIWWERDA KDLLPEGFTH PGSPNGEFKK ETDIMDVWFD SGSSWNGVVV 

       550        560        570        580        590        600 
NRPELKYPAD LYLEGSDQYR GWFNSSLITS VANHGVAPYK QILSQGFALD GKGEKMSKSL 

       610        620        630        640        650        660 
GNTIAPSDVE KQFGAEILRL WVTSVDSSND VRISMDILSQ VSETYRKIRN TLRFLIANTS 

       670        680        690        700        710        720 
DFNPAEDTVA YEELRSVDKY MTVRFNQLVK TIRDAYADFE FLTIYKALVN FINVDLSAFY 

       730        740        750        760        770        780 
LDFAKDVVYI EGAKSLERRQ MQTVFYDILV KITKLLTPIL PHTAEEIWSY LEFEAEDFVQ 

       790        800        810        820        830        840 
LSELPEAETF ANQEEILNTW AAFMDFRGQA QKALEEARNA KVIGKSLEAH LTIYPNEVVK 

       850        860        870        880        890        900 
TLLGAVDSNV AQLLIVSELT IAEGGAPEGA VSFEDVAFTV ERAAGEVCDR CRRIDPTTAE 

       910        920        930 
RNYHAVICDH CASIVEENFA DAVAEGFETK 

« Hide

References

[1]"Genome-wide transcriptional changes in Streptococcus gordonii in response to competence signaling peptide."
Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.
J. Bacteriol. 189:7799-7807(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Challis / ATCC 35105 / CH1 / DL1 / V288.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000725 Genomic DNA. Translation: ABV09656.1.
RefSeqYP_001449984.1. NC_009785.1.

3D structure databases

ProteinModelPortalA8AW24.
SMRA8AW24. Positions 1-917.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING467705.SGO_0681.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV09656; ABV09656; SGO_0681.
GeneID5598687.
KEGGsgo:SGO_0681.
PATRIC19659325. VBIStrGor124371_0670.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycSGOR467705:GH3R-680-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_STRGC
AccessionPrimary (citable) accession number: A8AW24
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 23, 2007
Last modified: May 14, 2014
This is version 52 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