Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8P068 (SYI_STRP8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 74. 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:spyM18_1531
OrganismStreptococcus pyogenes serotype M18 (strain MGAS8232) [Complete proteome] [HAMAP]
Taxonomic identifier186103 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length933 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

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 933933Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098482

Regions

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

Sites

Binding site5541Aminoacyl-adenylate By similarity
Binding site5981ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8P068 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: C93E9EBD10AEAF28

FASTA933105,113
        10         20         30         40         50         60 
MKLKETLNLG KTAFPMRADL PNKEPQWQAA WEQAELYKKR QELNAGKPAF HLHDGPPYAN 

        70         80         90        100        110        120 
GNIHVGHALN KISKDIIVRS KSMSGFQAPY VPGWDTHGLP IEQVLAKQGI KRKEMDLAEY 

       130        140        150        160        170        180 
LEMCRQYALS QVDKQRDDFK RLGVSADWEN PYVTLDPQFE ADQIRVFGAM AEKGYIYRGA 

       190        200        210        220        230        240 
KPVYWSWSSE SALAEAEIEY HDIDSTSLYY ANKVKDGKGI LDTNTYIVVW TTTPFTVTAS 

       250        260        270        280        290        300 
RGLTVGPDMD YLVVKPAGSD RQYVVAEGLL DSLAGKFGWE SFETLASHKG ADLEYIVTEH 

       310        320        330        340        350        360 
PWDTDVEELV ILGDHVTLES GTGIVHTAPG FGEDDYNVGT KYKLEVAVTV DERGLMMENA 

       370        380        390        400        410        420 
GPDFHGQFYN KVTPIVIDKL GDLLLAQEVI NHSYPFDWRT KKPIIWRAVP QWFASVSDFR 

       430        440        450        460        470        480 
QDILDEIEKT TFHPSWGETR LYNMIRDRGD WVISRQRAWG VPLSIFYAED GTAIMTKEVT 

       490        500        510        520        530        540 
DHVADLFQEN GSIIWWQKEA KDLLPEGFTH PGSPNGEFTK ETDIMDVWFD SGSSWNGVMN 

       550        560        570        580        590        600 
ARENLSYPAD LYLEGSDQYR GWFNSSLITS VAVNGHAPYK AILSQGFVLD GKGEKMSKSK 

       610        620        630        640        650        660 
GNIISPNDVA KQYGADILRL WVASVDTDND VRVSMEILGQ VSETYRKIRN TLRFLIANTS 

       670        680        690        700        710        720 
DFNPATDTVA YADLGAVDKY MTIVFNQLVA TITDAYERYD FMAIYKAVVN FVTVDLSAFY 

       730        740        750        760        770        780 
LDFAKDVVYI EAANSLERRR MQTVFYDILV KITKLLTPIL PHTTEEIWSY LEYESEAFVQ 

       790        800        810        820        830        840 
LAEMPVAETF SAQEDILEAW SAFMTLRTQA QKALEEARNA KIIGKSLEAH LTIYASEEVK 

       850        860        870        880        890        900 
TLLTALDSDI ALLLIVSQLT IADLADAPAD AVAFEGIAFM VEHAIGEVCE RSRRIDPTTR 

       910        920        930 
MRSYNAFVCD HSAKIIEENF PEAVAEGFEE SGK 

« Hide

References

[1]"Genome sequence and comparative microarray analysis of serotype M18 group A Streptococcus strains associated with acute rheumatic fever outbreaks."
Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S., Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D., Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A., Veasy L.G., Musser J.M.
Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MGAS8232.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009949 Genomic DNA. Translation: AAL98099.1.
RefSeqNP_607600.1. NC_003485.1.

3D structure databases

ProteinModelPortalQ8P068.
SMRQ8P068. Positions 1-918.
ModBaseSearch...

Protein-protein interaction databases

STRING186103.spyM18_1531.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL98099; AAL98099; spyM18_1531.
GeneID994701.
KEGGspm:spyM18_1531.
PATRIC19749576. VBIStrPyo4396_1374.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKQVLTHG.
ProtClustDBPRK13804.

Enzyme and pathway databases

BioCycSPYO186103:GHJG-1319-MONOMER.

Family and domain databases

Gene3D3.40.50.620. 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.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. tRNAsyn_1a_bind. 1 hit.
SSF50677. ValRS_IleRS_edit. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_STRP8
AccessionPrimary (citable) accession number: Q8P068
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2002
Last modified: May 29, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families