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Q6L206 (SYI_PICTO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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:PTO0411
OrganismPicrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828) [Complete proteome] [HAMAP]
Taxonomic identifier263820 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesPicrophilaceaePicrophilus

Protein attributes

Sequence length1024 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 – 10241024Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098586

Regions

Motif52 – 6211"HIGH" region HAMAP-Rule MF_02003
Motif590 – 5945"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site5931ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6L206 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6B23F804B7AAFF9F

FASTA1,024120,191
        10         20         30         40         50         60 
MKATLYENIN VNKSMIDINN EILNYWKENH IDENIIKSNR NLKPFAFLEG PPTANGRPHV 

        70         80         90        100        110        120 
GHLMTRAVKD TVMRYKYMTG HDILRRTGGW DCHGLPVELE AEKHFGFKNK KDIENFGIEK 

       130        140        150        160        170        180 
FNQYCRDSVF RYIDEWNIVD DLVGFWVDKE NSYITLKNDY MESEWWALKT LYENNLLVKD 

       190        200        210        220        230        240 
YKIVPYCPRC GTSLSSHEVA QGYKNVDDPS VFVKFAEKGR KNRYFIAWTT TPWTLPSNEF 

       250        260        270        280        290        300 
LVVNPDMDYS LIESDGFEYY LLSSKVESLF NDYKLIKTFK GRDLEGIEYE QLMPFLEKPE 

       310        320        330        340        350        360 
NAFRVVAASF VTAEDGTGIV HAAPAFGADD FEIGKRFSVE ILNPVDQDGR FNEKLPWSGL 

       370        380        390        400        410        420 
FVTDANKSII NYLKENNLLF KAETMKHDYP FCYRCGTRLL YYPLDTWFIK VSLIRKKLLE 

       430        440        450        460        470        480 
NNEKINWVPD YLKNGRFGNF LEEAKDWALS RDRYWGTPLP IWRCNKNHYL AIGSRDDLLK 

       490        500        510        520        530        540 
YGGYIPEDLH RPYIDDVVLK CPECGSEMHR ESYVIDTWFD SGSASYAAMH YPFSKDFTKS 

       550        560        570        580        590        600 
HFPVDFITEA IDQTRGWFYT LHVVASLLFD ENAYKNVVSI SHILDENGQK MSKSKGNFIA 

       610        620        630        640        650        660 
AIDFLNDYGA DAARMFFFTG APWNSKSVNK KLIGEITRKN LSTLLNVYSF FASNANIDEY 

       670        680        690        700        710        720 
RFTEIKEPEN LLDRWMLSRL NTTIIKVREN MDNYNIHTAL RYIEDLISEL SNVYLRLSRK 

       730        740        750        760        770        780 
RFWEGNLDDS KERAYSTLYY TLRETIKMMA PITPFFSEYL YQKLSPGMPS VHMESYPEAI 

       790        800        810        820        830        840 
ERFIDNDLEN EMEHAIEIME LSRRTRQELN IKGRQPVKEI LIYSDIKLRD DIIDIISPEL 

       850        860        870        880        890        900 
NAESIRFIKS DEMPLKITVR ADISKVAKLL KSRINDFNLY LERNNDLVYR ELKSKGKINF 

       910        920        930        940        950        960 
DGIYLTDDMF IMNEEVNGNY GFNKDERSGI YLFINREIDN DLLLEGYARE IIRRIQVMRK 

       970        980        990       1000       1010       1020 
DLNLEYSEKI KTYIDADEDI RSAVERYMEK IKNETLSSEI LFKNDPEARA WDIDDKTVYI 


KIVK 

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References

[1]"Genome sequence of Picrophilus torridus and its implications for life around pH 0."
Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C., Schepers B., Dock C., Antranikian G., Liebl W.
Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017261 Genomic DNA. Translation: AAT42996.1.
RefSeqYP_023189.1. NC_005877.1.

3D structure databases

ProteinModelPortalQ6L206.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING263820.PTO0411.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT42996; AAT42996; PTO0411.
GeneID2844251.
KEGGpto:PTO0411.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMANANIDEY.

Enzyme and pathway databases

BioCycPTOR263820:GHA3-426-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.
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]
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.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_PICTO
AccessionPrimary (citable) accession number: Q6L206
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 70 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