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Q5WFI3 (SYI_BACSK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. 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:ABC2342
OrganismBacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]
Taxonomic identifier66692 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length923 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 – 923923Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098348

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif594 – 5985"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8881Zinc By similarity
Metal binding8911Zinc By similarity
Metal binding9081Zinc By similarity
Metal binding9111Zinc By similarity
Binding site5531Aminoacyl-adenylate By similarity
Binding site5971ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WFI3 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: E25EFE72971B29FD

FASTA923104,537
        10         20         30         40         50         60 
MDYKQTLLMP KTAFPMRGNL PNSEPKRQEQ WEEMDIYKQV QERTEGRPYF VLHDGPPYAN 

        70         80         90        100        110        120 
GDIHMGHALN KIIKDFIVRY KSMSGFHAPY VPGWDTHGLP IETALTKNKK VDRKSMSIAD 

       130        140        150        160        170        180 
FRKLCEEYAL EQINSQRQQF MRLGVRGDWW KPYITLEKEF EAEQIKVFGK MAKKGYIYKG 

       190        200        210        220        230        240 
KKPVYWSPSS ESALAEAEIE YYDKRSASIY VAFQVADGKG VLPEDAALVI WTTTPWTIPA 

       250        260        270        280        290        300 
NLGITVHPQL EYSVVRTGGR SFVVASGLLE HVQTELSWED VVVEKTVTGK ELDYIVCRHP 

       310        320        330        340        350        360 
FYDRDSIVMN GEHVTLDAGT GCVHTAPGHG VDDFVVGQKY GLDVLCPIDD KGIMTSEAPG 

       370        380        390        400        410        420 
FEGEFYDNIN KMVTEKLEAV GALLKLGFIT HSYPHDWRTK KPVIFRATSQ WFASIANIRK 

       430        440        450        460        470        480 
ELLQAVANTE WIPAWGETRL HNMVRDRGDW CISRQRAWGV PIPVFYGEDG TEIVSEETIE 

       490        500        510        520        530        540 
HVSNLFREHG SNVWFEREAK DLLPPGFTSP HSPNGHFTKE TDIMDVWFDS GSSHQGVLRE 

       550        560        570        580        590        600 
RNDLVFPADL YFEGSDQYRG WFNSSLSTSV AINGVAPYKG VLSHGFVMDG EGKKMSKSLG 

       610        620        630        640        650        660 
NIVVPNTVMK QLGADILRLW VASVDYQADS RVSDSILKQV AETYRKIRNT FRFLLGNLHD 

       670        680        690        700        710        720 
FDPKINAVPR DQLTGVHAFL LVRLNELTKR MHEGYNEYQF LNVYNHFRNF CTVELSSFYM 

       730        740        750        760        770        780 
DISKDTLYIE HADHPERRAF QTVMYEVVTA LTKLIAPILP HTADEVWENI PGVSEQSVQL 

       790        800        810        820        830        840 
TDMPTAEELS GTDELKAHWQ AFMDIRADVL KALEVARNEK VIGKSLQASL TLYPNKQARA 

       850        860        870        880        890        900 
LLEATEGLKK LFIVSNVQIA NEGDEVPAAA QQFADVAVLV EKAEGETCER CWQVSNTVGA 

       910        920 
DEKHPTLCLS CAQTVTNHYN DVV 

« Hide

References

[1]"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KSM-K16.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006627 Genomic DNA. Translation: BAD64877.1.
RefSeqYP_175838.1. NC_006582.1.

3D structure databases

ProteinModelPortalQ5WFI3.
SMRQ5WFI3. Positions 2-878.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING66692.ABC2342.

Proteomic databases

PRIDEQ5WFI3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD64877; BAD64877; ABC2342.
GeneID3201308.
KEGGbcl:ABC2342.
PATRIC18924272. VBIBacCla58185_2499.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycBCLA66692:GHMP-2410-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_BACSK
AccessionPrimary (citable) accession number: Q5WFI3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: November 23, 2004
Last modified: April 16, 2014
This is version 74 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