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Q3ITY7 (SYI_NATPD) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 61. 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:NP_0610A
OrganismNatronomonas pharaonis (strain ATCC 35678 / DSM 2160) (Halobacterium pharaonis) [Complete proteome] [HAMAP]
Taxonomic identifier348780 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeNatronomonas

Protein attributes

Sequence length1061 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 – 10611061Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098585

Regions

Motif50 – 6011"HIGH" region HAMAP-Rule MF_02003
Motif604 – 6085"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6071ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3ITY7 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 2B24147A2FCB2EA2

FASTA1,061120,589
        10         20         30         40         50         60 
MSRFAEVDDQ YDPDAVEDRV FDYWDEVDAY ERTVEHRADG EDFFFVDGPP YTSGSAHMGT 

        70         80         90        100        110        120 
TWNKTLKDAY IRYHRMRGYN VTDRPGYDMH GLPIETKVEE RLGFDNKKDI EEFGEQNFID 

       130        140        150        160        170        180 
ECKSFAEEQL EGLQEDFKSF GVWMDWDDPY KTVDPEYMEA AWWGFSKAHD RDLVEQGQRS 

       190        200        210        220        230        240 
ISQCPRCETA IANNEVEYDH VEDPSIYVKF PLAEREGHLV IWTTTPWTVP ANTFVAVDEE 

       250        260        270        280        290        300 
MTYQAIEVDT GDGTETLYVG EPCVEDVVDH GGYEDYEVVG EHEGSDLVGW RYEHPLREEV 

       310        320        330        340        350        360 
PEAPAFEGAL EVYGADYVEA DRTGLVHSAP GHGEVDFERG QELGLSVFCP VGPDGVYEDA 

       370        380        390        400        410        420 
AGDYAGQFVK DADAAIMDDL EAKGLLLSRG TVNHDYGHCW RCDTPIIQMV TDQWFITVTD 

       430        440        450        460        470        480 
IKDELLANME ESEWFPQEAR DNRFRSFIEE SPDWNVSRQR YWGIPIPIWT PDDWSGDVEE 

       490        500        510        520        530        540 
AIVVSTREEL AERVDQDIDP ESVDLHKDTV DDLTITADGT TYTRVPDVFD VWLDSSVASW 

       550        560        570        580        590        600 
GTLGYPGNED DFEELWPADL IMEAHDQTRG WFWSQLGMGS AALGEAPYET VLMHGWALAE 

       610        620        630        640        650        660 
DGRKMSKSIG NIVAPQEAID RHGADPMRLF LLTQNPQGDD MRFSWDEMEN RQRDLNILWN 

       670        680        690        700        710        720 
VFRFPLPYMR LDDFDPDAVA LDEAALETVD EWVLSRLSTV TAEMTDHWEN FRQDKALDEL 

       730        740        750        760        770        780 
LAFIVEDVSR FYIQVVRERM WEEETSESKL AAYATLHHVL VETTKLLAPY APFVAEEIYG 

       790        800        810        820        830        840 
TLTGDGGHET VHMADWPDPD ERFRDPQLET DVDIVAAVEE AGSNARQQAE RKLRWPVTRV 

       850        860        870        880        890        900 
VVAADDDRAA EAVDRHRDLL RDRLNAREIE LVEPGSDWEE LSYTARADMS VLGPTFGDEA 

       910        920        930        940        950        960 
GEVMNAINAV SVTDTAVEAL EAAVETELGR DIELTDEMVS FNTETPEGVE GTAFTVDGDD 

       970        980        990       1000       1010       1020 
RGVVYVDTAL TEDIESEGYA REVIRRVQEM RKDLDLDIEA EIRVDLDIAD ERVATLVDEH 

      1030       1040       1050       1060 
EGLIADEVRA AEFADLNAGH ERVWDVESTD ITITIDPVSE R 

« Hide

References

[1]"Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis."
Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J., Oesterhelt D.
Genome Res. 15:1336-1343(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35678 / DSM 2160.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR936257 Genomic DNA. Translation: CAI48396.1.
RefSeqYP_325965.1. NC_007426.1.

3D structure databases

ProteinModelPortalQ3ITY7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING348780.NP0610A.

Proteomic databases

PRIDEQ3ITY7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI48396; CAI48396; NP_0610A.
GeneID3702863.
KEGGnph:NP0610A.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAGARDWCI.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycNPHA348780:GJX0-315-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.
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. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYI_NATPD
AccessionPrimary (citable) accession number: Q3ITY7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: November 8, 2005
Last modified: April 16, 2014
This is version 61 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