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Q9HN97 (SYI_HALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. 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:VNG_2190G
OrganismHalobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) [Reference proteome] [HAMAP]
Taxonomic identifier64091 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium

Protein attributes

Sequence length1070 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_02003

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003

Cofactor

Zinc By similarity. HAMAP-Rule MF_02003

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02003

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02003.

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_02003

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference 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 – 10701070Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098577

Regions

Motif50 – 6011"HIGH" region HAMAP-Rule MF_02003
Motif606 – 6105"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6091ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HN97 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: EABADEAC91ECBDC3

FASTA1,070119,902
        10         20         30         40         50         60 
MSGFGDVPDQ YDPAGVEERV FSYWEAVDAY EQTVDHRADA ETFFFVDGPP YTSGAAHMGT 

        70         80         90        100        110        120 
TWNKTLKDAY IRYHRMQGYD VTDRPGYDMH GLPIETKVEE QLGFESKKDI QEFGEEAFIE 

       130        140        150        160        170        180 
ECKRFADDNL DGLQSDFQSF GVWMDWDNPY KTVDPSYMEA AWWAFSEVHD NGLVERGQRS 

       190        200        210        220        230        240 
ISQCPRCETA IANNEVEYED VTDPSIYVRF DLDDREGSLV VWTTTPWTIP ANQFVAVDED 

       250        260        270        280        290        300 
GDYQQVRATT PDGETDVLYV ASECVEDVLS AGGYSDHEIV ADHSGSDLIG WSYTPPLADA 

       310        320        330        340        350        360 
VPANPTDADG THEVYHGDWV EADRTGLVHS APGHGEEDFE RGAELDLPVF CPVGEDGVYT 

       370        380        390        400        410        420 
DAGGKYAGAF VRDANDDIIA DLEARDAMLA SQTVEHSYGH CWRCDTGIIQ IVTDQWFITI 

       430        440        450        460        470        480 
TDVKDELLAN MDTSEWHPEW ARDNRFRDFV ENAPDWNVSR QRYWGIPVPI WTPEDWSGDA 

       490        500        510        520        530        540 
EDVLVVGTRE ELAALADQDV DPASVDLHKP TVDDITITED GTEYTRVPDV FDVWLDSSVA 

       550        560        570        580        590        600 
SWGTLNYPEQ EDDFDELWPA DLIMEAHDQT RGWFWSQLGM GTAALGDVPY EEVLMHGYAN 

       610        620        630        640        650        660 
MPDGRGMSKS KGITIEPNEV IDEYGADPMR MFLLSVTPQG DDMSFSWDET ENMQRDLNIL 

       670        680        690        700        710        720 
WNVFRFPRPY MALDDFDANV PAAFGGDDAG VGIADADLET VDEWLLSRLQ HVKADATAHW 

       730        740        750        760        770        780 
EDFEQHRALD AVLEFVVEDL SRYYVQVVRE RMWEDDASAS KTAAYATMQR VLLEVVALLA 

       790        800        810        820        830        840 
PYAPFVTEEL YSHLTGDRGY DTVHMADWPT VEESLRAPAL EADVAVLRAA EEAGSHARQQ 

       850        860        870        880        890        900 
AGRKLRWPVT RVVVDAAEDS VVDALDAHGD LLADRLNTRA IEVVEPGAAW DELAYSARAD 

       910        920        930        940        950        960 
MSELGPAFGD DAGAVMNALN DARVTDRDID ALAEQVAADL GRDDIELTTE MVEFVEETPE 

       970        980        990       1000       1010       1020 
HVAGAAFETE TAAGTVYVDT ELNEDVESEG YAREVVRRVQ EMRKEMDLAM DAEIRLDVLV 

      1030       1040       1050       1060       1070 
FDERVGELVA RHEPLITAET RARELGEVED GHREEWDVEG TTMILEVEAV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004437 Genomic DNA. Translation: AAG20324.1.
PIRH84369.
RefSeqNP_280844.1. NC_002607.1.

3D structure databases

ProteinModelPortalQ9HN97.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING64091.VNG2190G.

Proteomic databases

PaxDbQ9HN97.
PRIDEQ9HN97.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG20324; AAG20324; VNG_2190G.
GeneID1448627.
KEGGhal:VNG2190G.

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMATEGIDQT.
PhylomeDBQ9HN97.
ProtClustDBPRK06039.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02003. Ile_tRNA_synth_type2.
InterProIPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
IPR023586. Ile-tRNA-ligase_type2.
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. SSF47323. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYI_HALSA
AccessionPrimary (citable) accession number: Q9HN97
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 76 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