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Q18GW3 (SYI_HALWD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:HQ_2671A
OrganismHaloquadratum walsbyi (strain DSM 16790 / HBSQ001) [Complete proteome] [HAMAP]
Taxonomic identifier362976 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloquadratum

Protein attributes

Sequence length1059 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
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 – 10591059Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_1000022149

Regions

Motif47 – 5711"HIGH" region HAMAP-Rule MF_02003
Motif606 – 6105"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6091ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q18GW3 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: E2353B1F064CE233

FASTA1,059119,617
        10         20         30         40         50         60 
MDEVDDQYTP ADVETAIETY WDDTNAYEAT KEAHADDPSF FFVDGPPYTS GQMHLGTAWN 

        70         80         90        100        110        120 
KTLKDAIIRY KRMTGHHVTD RPGYDMHGLP IEVKVEEELG FETKRDIEEY GMESFIEECK 

       130        140        150        160        170        180 
RFAVDNRKAM DEDFQSIGVW MDWDNPYETL SPEYMEAAWW AFQQVDDRGL VERGKRSVSY 

       190        200        210        220        230        240 
CPRCQTAIAA NEVEYDEITS PSIYVRFPLS NKEGSLVIWT TTPWTIPANT FVAVDKDLTY 

       250        260        270        280        290        300 
QAVRAEQGDD SEVLYIAESC VEDVLKQGRY DDYTVVEEYS GDELTGWEYD HPLADQVQTY 

       310        320        330        340        350        360 
ADFAGAGEVY TAEYVEADRT GLVHSAPGHG QEDFARGQEL DLETFVPVDG RGEFTEAAGQ 

       370        380        390        400        410        420 
YTGTFVRDAN DEIINDLDEE GVLLSSGTHE HRYGHCWRCD TDIIFLATDQ WFITVTDIKD 

       430        440        450        460        470        480 
ELLDNINDSE WYPQWARDNR FRDFVADAPD WNVSRQRYWG IPLPIWESVD DADTGDNSTS 

       490        500        510        520        530        540 
DDWIVIGTRE ELAERADQDV NPAEIDLHRP AVDPLTITEN GSRYERVPDV FDVWIDSSVA 

       550        560        570        580        590        600 
SWGTIDYPGE TDAYDELWPA DFIVEAHDQT RGWFWSQLGM GTAATGQVPY EEVMMHGFAN 

       610        620        630        640        650        660 
DENGRKMSKS RGNIVTPEEA IDRAGRDPLR AYLLSHDQQG VDLSFEWDGL GEMQSTLNIF 

       670        680        690        700        710        720 
WNVFRFPLPY MDLDGYDPAT ADLSEGSMNI VDEWVLSRLQ SVKATTRAAW EEYEIDTAVN 

       730        740        750        760        770        780 
TILEFITDDV SRFYIKAIRE RMWADEDSAS KRGAYATLST VLDETIRLLA PIAPYLTEQM 

       790        800        810        820        830        840 
YQHLNGSETT VHALSYPSVD PEWQNETLES EMAVLRDVEE AAANARQQGG RKLRWPVPRV 

       850        860        870        880        890        900 
IVEAEDDSIA DAVESLSGLL ADRVNTEAIE TVTQFDELIE RAQPEMSVIG PEFGADAQRV 

       910        920        930        940        950        960 
MDAIEGGSRE ILTEGVTIDG VQYEITDEMI TFDAEPPAYI SAADFDGGTV YVDTSLTESI 

       970        980        990       1000       1010       1020 
EAEGYARDVI RRIQQMRKEL ALDVDTEIQT AVDVADDRVA DLVAQQRDVV ATETRTNAFV 

      1030       1040       1050 
DNIDRASENG QALIEEWDVE GVTVTIGVAP LKAQLSDQS 

« Hide

References

[1]"The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity."
Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F., Pfeiffer F., Oesterhelt D.
BMC Genomics 7:169-169(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 16790 / HBSQ001.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM180088 Genomic DNA. Translation: CAJ52782.1.
RefSeqYP_658388.1. NC_008212.1.

3D structure databases

ProteinModelPortalQ18GW3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362976.HQ2671A.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ52782; CAJ52782; HQ_2671A.
GeneID4194153.
KEGGhwa:HQ2671A.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMARYVEGKW.

Enzyme and pathway databases

BioCycHWAL362976:GJSR-1772-MONOMER.

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.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. 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. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_HALWD
AccessionPrimary (citable) accession number: Q18GW3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 25, 2006
Last modified: May 14, 2014
This is version 62 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