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Q8ZWU4 (SYI_PYRAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:PAE1617
OrganismPyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827) [Reference proteome] [HAMAP]
Taxonomic identifier178306 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length981 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 – 981981Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098587

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
Q8ZWU4 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 6F7A1242CC105D41

FASTA981114,759
        10         20         30         40         50         60 
MPHGDLPLPP SYRPHEVKKA VEEFWRRNRI FEKWKSWRGG PKFTFLEGPP TTNGMPHVGH 

        70         80         90        100        110        120 
IRGRTYKDVV IRFYRLLGYD VWVQGGWDMQ GMPVEWEVEK KLKLRSKKDI EQFGLEKFAL 

       130        140        150        160        170        180 
ECNSLVEEYL AYWREWGTKR LGLWLDLENA YETRQPHYLQ YAWRIVKRAH ELGLLTEDYR 

       190        200        210        220        230        240 
VLWFCPRCET SLSDHEVALG YDEREDPSIY VKFRVEGGVD EYLVIWTTTP WTIVDNEAVA 

       250        260        270        280        290        300 
VHPDYVYAKV EVEVGGRREY WWLAEALVPS LMAKFGIKTW RVVETKKGVE LAGVRYIHPL 

       310        320        330        340        350        360 
AEEVPERASR PHQVVTAEFV TLEQGTGLVH IAPGHGPEDF ELAKKYGLPV TNSVEINGIY 

       370        380        390        400        410        420 
NELGGRYKGK HVYDVDKEVT RDLRSKGLLV FEEKIRHEYP HCWRCGSKLI LRADRQWFIA 

       430        440        450        460        470        480 
ISRIRDKMYA ELQKVNVVPT KLRDRFDIFV QNARDWNISR SRVWGTPLPV WRCKKDGRIL 

       490        500        510        520        530        540 
VIGSLEELKK LAKELPPVDD FKLVHRPWID QVKISAHDCD EWVREPYVMD VWLDSGIAWI 

       550        560        570        580        590        600 
AAVDGENNRD LWEKLFPYDF VTEGIDQTRG WFYSLLATSV LYTGRAPYKN VLIQGLILDK 

       610        620        630        640        650        660 
HGQKMSKSKG NVIWAKDLFE KYGADPVRLY ILSKVAPWED LSFDPDEVKY VIGDLNILWN 

       670        680        690        700        710        720 
VVKFADTYMS LDGFDAEKYP LSQWLEKGLE EDKWILSELN IMISEFTNFV KNFEFHKAAA 

       730        740        750        760        770        780 
LWREFVVETL SHRYIRLLRR RVWSEEPSPD KYAAYAVLHD VLKKVLILGS ILVPFITEYL 

       790        800        810        820        830        840 
WQAYVRKYEK NAPESVHLAQ YPAAGSYDKE LIYAYRELFA VFSALAEARN KAGIKLRWPI 

       850        860        870        880        890        900 
REAYVNGAKY AERYTELLKY LGNVKEVKVG RRPDYLCVKE GELEVCVPDK IEPELYYEAL 

       910        920        930        940        950        960 
ARELIRRIQV MRKETGLEIS DEIHVVVETN SDDIKKAVEQ YRDYIARETR AVKLIIDAVS 

       970        980 
QGKEWDISGE KVKIEIRKAQ A 

« Hide

References

[1]"Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum."
Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I., Miller J.H.
Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009441 Genomic DNA. Translation: AAL63605.1.
RefSeqNP_559423.1. NC_003364.1.

3D structure databases

ProteinModelPortalQ8ZWU4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING178306.PAE1617.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL63605; AAL63605; PAE1617.
GeneID1465853.
KEGGpai:PAE1617.

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMARYVEGKW.

Enzyme and pathway databases

BioCycPAER178306:GCEO-1146-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_PYRAE
AccessionPrimary (citable) accession number: Q8ZWU4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2002
Last modified: May 14, 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