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Q3K6L5 (SYI_PSEPF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. 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:Pfl01_4852
OrganismPseudomonas fluorescens (strain Pf0-1) [Complete proteome] [HAMAP]
Taxonomic identifier205922 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length943 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_02002

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02002

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_02002

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02002

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02002.

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_02002

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 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 – 943943Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022108

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif608 – 6125"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9061Zinc By similarity
Metal binding9091Zinc By similarity
Metal binding9261Zinc By similarity
Metal binding9291Zinc By similarity
Binding site5671Aminoacyl-adenylate By similarity
Binding site6111ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3K6L5 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 6B46ACE3C698942C

FASTA943105,507
        10         20         30         40         50         60 
MTDYKATLNL PDTAFPMKAG LPQREPQILQ RWDSIGLYGK LREIGKDRPK FVLHDGPPYA 

        70         80         90        100        110        120 
NGTIHIGHAL NKILKDMIIR SKTLSGFDAP YVPGWDCHGL PIEHKVEVTH GKNLGADKTR 

       130        140        150        160        170        180 
ELCRAYATEQ IEGQKTEFIR LGVLGDFANP YKTMNFKNEA GEIRALAEIV KGGFVFKGLK 

       190        200        210        220        230        240 
PVNWCFDCGS ALAEAEVEYE NKKSSTIDVA FPIADEAKLA AAFGLPSLAK PAAIVIWTTT 

       250        260        270        280        290        300 
PWTIPANQAL NVHPEFTYAL VDIGDKLLVL AEELVESCLT RYGVEGTVLA TAPGSALELI 

       310        320        330        340        350        360 
NFRHPFYDRL SPVYLADYVE LGAGTGVVHS APAYGVDDFV TCKKYGMVND DILNPVQSNG 

       370        380        390        400        410        420 
VYVPSLEFFG GQFIWKANPA IVDKLTEVGA LLHTTVIEHS YMHCWRHKTP LIYRATAQWF 

       430        440        450        460        470        480 
IGMDKEPVSG DTLRVRSLKA IEDTKFVPAW GQARLHSMIA NRPDWCISRQ RNWGVPIPFF 

       490        500        510        520        530        540 
LNKESGELHP RTVELMEEVA KRVEVEGIEA WFKLDAAELL GDEAPQYDKI SDTLDVWFDS 

       550        560        570        580        590        600 
GTTHWHVLRG SHPMGHETGP RADLYLEGSD QHRGWFHSSL LTGCAIDNHA PYRELLTHGF 

       610        620        630        640        650        660 
TVDESGRKMS KSLGNVIAPQ KVNDTLGADI MRLWVASTDY SGEMAVSEQI LQRSADAYRR 

       670        680        690        700        710        720 
IRNTARFLLS NLTGFNPATD LLPAEDMLAL DRWAVDRTLL LQRELQEHYG EYRFWNVYSK 

       730        740        750        760        770        780 
IHNFCVQELG GFYLDIIKDR QYTTGADSKA RRSCQTALFH ISEALVRWIA PILAFTADEL 

       790        800        810        820        830        840 
WQYLPGERNE SVMLNTWYEG LTELPEGFEL GREYWDRIME VKVAVNKEME IQRAAKAVGG 

       850        860        870        880        890        900 
NLQAEVTLFA EDALTADLAK LSNELRFVLI TSTATVAPFV QAPADAVATE VSGLKLKIVK 

       910        920        930        940 
SAFPKCARCW HCREDVGVNP EHPEICGRCV DNIDGAGEVR HYA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000094 Genomic DNA. Translation: ABA76589.1.
RefSeqYP_350580.1. NC_007492.2.

3D structure databases

ProteinModelPortalQ3K6L5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205922.Pfl01_4852.

PTM databases

PhosSiteP0906691.

Proteomic databases

PRIDEQ3K6L5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA76589; ABA76589; Pfl01_4852.
GeneID3716852.
KEGGpfo:Pfl01_4852.
PATRIC19891898. VBIPseFlu44242_4864.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycPFLU205922:GJBD-4931-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02002. Ile_tRNA_synth_type1.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
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.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 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_PSEPF
AccessionPrimary (citable) accession number: Q3K6L5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 8, 2005
Last modified: May 14, 2014
This is version 73 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