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Q88V89 (SYI_LACPL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 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:lp_2187
OrganismLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) [Reference proteome] [HAMAP]
Taxonomic identifier220668 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length932 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
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 – 932932Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098403

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif597 – 6015"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8911Zinc By similarity
Metal binding8941Zinc By similarity
Metal binding9111Zinc By similarity
Metal binding9141Zinc By similarity
Binding site5561Aminoacyl-adenylate By similarity
Binding site6001ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q88V89 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 559234B1D9AD149E

FASTA932106,318
        10         20         30         40         50         60 
MRVKETLNLG KTKFKMRGNL PVKEVERQNV WAENKVYEQR QKLNEGKPSF ILHDGPPYAN 

        70         80         90        100        110        120 
GDIHMGHALN KITKDFIVRY KSMNGFRAPY VPGWDTHGLP IEQKLKQAGY DRKKMTDNEF 

       130        140        150        160        170        180 
RELCRKYALE QVDRQRDEFK RLGVAGEWDN PYLTLKPEFE AAQVRVFGAF AKRHLIYRGQ 

       190        200        210        220        230        240 
KPVFWSWSSE SALAEAEVEY HDVTSPSAFY GEHVIDGKGV LDDDTYMVVW TTTPWTIPAS 

       250        260        270        280        290        300 
EGITIDASFD YVVVQPAGEN RKFVLAAELL DENAERFGWE DVQVLKTVKG AELENILCEH 

       310        320        330        340        350        360 
PFDNSRHLVT MLGDFVTLDS GTGLVHTAPG YGEDDYRIGK QYDLPIFAPV DDKGFLTAEA 

       370        380        390        400        410        420 
GDDFAGVFYD DANKIALDKL KAAGLLLKYM PYEHSYPFDW RTKKPIIFRA TPQWFASVGD 

       430        440        450        460        470        480 
MRDEILKSMD DVEFFPEWGK KRLYNMIRDR GDWVISRQRV WGVPLPIFYA EDGTAIMDEV 

       490        500        510        520        530        540 
TINHVADLFG KYGSNVWFER DAKDLLPDGY TNEHSPNGTF TKETDIMDVW FDSGSSHQGV 

       550        560        570        580        590        600 
LAERSYLDYP ADLYLEGSDQ YRGWFNSSLI TSVAVSGHAP YKQVLSQGFT LDNQGRKMSK 

       610        620        630        640        650        660 
SLGNTIAPAD VIKQMGAEIV RMWVASVDTS SDVRVSMESF KQVADSYKKF RNTVRFMLGN 

       670        680        690        700        710        720 
TADFDPKANR VAYEDLASVD QYMETRLNEF VAETKDHYDH YDFLDIYKKL INFLTVDLSN 

       730        740        750        760        770        780 
FYLDIAKDIM YIDAEDSHSR RSMQTVFYDV LVALTKLFTP MLPHTTEEIW PFLKEPEEFA 

       790        800        810        820        830        840 
QLAEMPAVQN YANSDELMAQ WTRFMDLRSN VLKALEEARD AKLIGKSLEA HLDLYVDDDT 

       850        860        870        880        890        900 
QAFLDHLNTN VRQMLMVSAL DLHALSDAPE DAETFGDTLA IKVGHADGDV CDRCRMVKTD 

       910        920        930 
VGSDEAYPML CARCAAIVRE NYPESVTTGL EA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL935263 Genomic DNA. Translation: CCC79407.1.
RefSeqYP_004889921.1. NC_004567.2.

3D structure databases

ProteinModelPortalQ88V89.
SMRQ88V89. Positions 1-920.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING220668.lp_2187.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCC79407; CCC79407; lp_2187.
GeneID1063600.
KEGGlpl:lp_2187.
PATRIC22250415. VBILacPla27411_1848.

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAERLMLHQ.

Enzyme and pathway databases

BioCycLPLA220668-WGS:GSPK-1868-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_LACPL
AccessionPrimary (citable) accession number: Q88V89
Secondary accession number(s): F9UQB8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: June 1, 2003
Last modified: July 9, 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