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Q0I1V8 (SYI_HISS1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. 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:HS_0186
OrganismHistophilus somni (strain 129Pt) (Haemophilus somnus) [Complete proteome] [HAMAP]
Taxonomic identifier205914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus

Protein attributes

Sequence length937 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 – 937937Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022074

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif602 – 6065"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9001Zinc By similarity
Metal binding9031Zinc By similarity
Metal binding9201Zinc By similarity
Metal binding9231Zinc By similarity
Binding site5611Aminoacyl-adenylate By similarity
Binding site6051ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0I1V8 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: C0E8BBD52F459F68

FASTA937105,861
        10         20         30         40         50         60 
MTDYKNTLNL PETGFPMRGD LAKREPDMLK NWYDKNLYQK VREASKGKKT FILHDGPPYA 

        70         80         90        100        110        120 
NGTLHLGHAV NKILKDIIMK SKTALGFDTP YVPGWDCHGL PIELKVEGLV GKPNEKISAA 

       130        140        150        160        170        180 
EFRQACRDYA KEQVEGQKAD FIRMGVLGDW DNPYLTMNFE TEAEIIRTLG KVIQNGHLYK 

       190        200        210        220        230        240 
GSKPVHWCLD CASSLAEAEV EYEDKVSPSI YVRFAAVSAA EVEEKFNALG KGQGALSAVI 

       250        260        270        280        290        300 
WTTTPWTLPS NRAIAVNAEL EYQLVQLGNE RVILATELVQ TVQNALGIEQ IQILGSAKGG 

       310        320        330        340        350        360 
DLELIRFNHP FYDFSVPMIL GDHVTVDGGT GLVHTAPDHG QDDFVVSKKY GLEMAGLVAN 

       370        380        390        400        410        420 
DGKFISSTPF FAGKGVFEAN DLVLEKLKET GALLKLERIK HSYPHCWRHK TPIIFRATPQ 

       430        440        450        460        470        480 
WFIGMETQDL RIKALSEIKS VRWIPSWGEA RIDKMVANRP DWCISRQRTW GVPMTMFVHN 

       490        500        510        520        530        540 
ETEELHPRTL ELLEDIAKRV EKAGIQAWWD LDPAELLGEE AKTYHKVPDT LDVWFDSGST 

       550        560        570        580        590        600 
YASVVEQRPE FNGKSTDMYL EGSDQHRGWF MSSLMLSTAT NNKAPYKQVL THGFTVDEKG 

       610        620        630        640        650        660 
RKMSKSLGNV IVPSEVWNKN GADILRLWVA STDYTGEIAV SHKILNSAGD TYRRIRNTAR 

       670        680        690        700        710        720 
FLLANLNGFD PKNDLVNPEE MISLDRWAVS CALEAQNEIK EAYDNYQFHT VVQRLMRFCS 

       730        740        750        760        770        780 
IEMGSFYLDI IKDRQYTTKA DSLARRSCQT ALWHISEALV RWIAPILSFT ADEIWGYLPK 

       790        800        810        820        830        840 
LDNRAEFVFT EEFYDGLFGL DESDKLDDTY WQQLLKVRAE VNRVLEQARN DKLIGAGLEA 

       850        860        870        880        890        900 
KVTVYASEEI RPLLEQLGNE LRFVLITSQV VVKPLSKADV AESELTGLAV KVERADGEKC 

       910        920        930 
PRCWHFATDI GSNKEHSHIC GRCIENVEGN GEQRQFA 

« Hide

References

[1]"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129Pt.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000436 Genomic DNA. Translation: ABI24464.1.
RefSeqYP_718393.1. NC_008309.1.

3D structure databases

ProteinModelPortalQ0I1V8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205914.HS_0186.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI24464; ABI24464; HS_0186.
GeneID4239697.
KEGGhso:HS_0186.
PATRIC20280280. VBIHaeSom53361_0198.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycHSOM205914:GJ7V-192-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_HISS1
AccessionPrimary (citable) accession number: Q0I1V8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: May 14, 2014
This is version 63 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