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Q9V072 (SYI_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. 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:PYRAB09190
ORF Names:PAB0616
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length1067 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 – 10671067Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098588

Regions

Motif49 – 5911"HIGH" region HAMAP-Rule MF_02003
Motif625 – 6295"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6281ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9V072 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: B7A8C50C93924D82

FASTA1,067126,109
        10         20         30         40         50         60 
MIKEPEFREY DPKKLEEKVE KFWSENEIYR KVKELRKDGP KYYFLDGPPY VSGAIHLGTA 

        70         80         90        100        110        120 
WNKIIKDMII RFRTMQGYNV WRQPGYDMHG LPIEVKVEQA LGLKTKKEIE EKIGVENFIK 

       130        140        150        160        170        180 
KCKEFALNNL KIMTEQFKML GIWMDWDNPY MTIKNEYIES AWFTLKRAWE KGLLEKDKRV 

       190        200        210        220        230        240 
LHWCPRCETA LAEHEVRGEY KLRKDPSIYV KFPVEGKENE YLLIWTTTPW TLPANLAVSA 

       250        260        270        280        290        300 
HPDYDYVKVK VEFNGREEYW ILAKALVDKV LGEIGVKGEV VEEFKGRELE GLRYVHILMD 

       310        320        330        340        350        360 
EYPRQKEFKE KYEWAHRVIL ADFVTLEEGT GLVHTAPGHG EEDFEVGQKY GLPVYSPLDD 

       370        380        390        400        410        420 
QGKYTEGKWK GIYVKEADPK IIEHLREKGY LVKAGEIEHK YPHCWRCKTP LIFRATDQWF 

       430        440        450        460        470        480 
LKISKVKDKI IKENDEKVTW YPDWVKIRFD NGVRDSGDWV ISRQRYWGIP LPIWQSEDGE 

       490        500        510        520        530        540 
IYVVGSWREL VELAVAIEVN GERIELPESY EEKLKVIEEK LGPEDLHRPY VDAFIIKVNG 

       550        560        570        580        590        600 
KDMRRVKDVV DVWFDSGIAS WASLGYPRNK ELFEKLWPAD FIVEGEDQVT KWFYSQQAAS 

       610        620        630        640        650        660 
IVAFDTVPYR RVAMHGYVLD EKGDKMSKSL GNIIRPEEVV ERAGRDTFRF YMLWATNPWE 

       670        680        690        700        710        720 
NLKFSWKGVE QVRRMLNILW NVYVLASTYM SLDNFDPRKL NPDELPFREE DKWILSRVNS 

       730        740        750        760        770        780 
LISEVENGIE SFYLTKATRA LYNFVVEDLS RWYVRLIRKR LWVEGEDPDK LAAYYTLWKV 

       790        800        810        820        830        840 
FDVLLRLLAP FTPYIAEEIY QNLIRPFTNV ESVHMLDWPK VDEKAIDEEL EREMEFIRRI 

       850        860        870        880        890        900 
VEAGSAARQR AKIKLRYPVR RIIIETEDET VKKAVERLNR ILRDQLNAKE VKVGRVEREL 

       910        920        930        940        950        960 
TIKPNFAKLG PEFKGDAKII AKWINENGRE LYEKGELTVE IDGKTFHLTR EHIIVEEKLP 

       970        980        990       1000       1010       1020 
DFFVSEEFEG GRVFVDKTLT RELIAEGLAR EFVRRIQEMR KRLDLDVNDR IIVTIETTDE 

      1030       1040       1050       1060 
NVELLKENLD YIMRETRADK IVFGKAKGYV VEWPEVQAKI GIEKVEE 

« Hide

References

« Hide 'large scale' references
[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
[2]"Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
Gao J., Wang J.
Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248285 Genomic DNA. Translation: CAB49833.1.
HE613800 Genomic DNA. Translation: CCE70327.1.
PIRH75139.
RefSeqNP_126602.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9V072.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272844.PAB0616.

Proteomic databases

PRIDEQ9V072.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB49833; CAB49833; PAB0616.
GeneID1496271.
KEGGpab:PAB0616.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAGARDWCI.
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.
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. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_PYRAB
AccessionPrimary (citable) accession number: Q9V072
Secondary accession number(s): G8ZI86
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 92 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