Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8R9L3 (SYI_THETN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. 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:TTE1594
OrganismThermoanaerobacter tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) (Caldanaerobacter subterraneus subsp. tengcongensis) [Complete proteome] [HAMAP]
Taxonomic identifier273068 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeCaldanaerobacter

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
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_0000098493

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif600 – 6045"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8991Zinc By similarity
Metal binding9021Zinc By similarity
Metal binding9191Zinc By similarity
Metal binding9221Zinc By similarity
Binding site5591Aminoacyl-adenylate By similarity
Binding site6031ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8R9L3 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 9CB12C99B76D09C7

FASTA932108,136
        10         20         30         40         50         60 
MDYNKTLNLP KTDFPMKANL PVREPEILKK WEEMDIYRRV LEKNKGKEKY ILHDGPPYAN 

        70         80         90        100        110        120 
GDIHIGTAMN KVLKDIVVKY KTMRGYDSPY VPGWDTHGLP IEQQVIKILG VKRHEMNPVE 

       130        140        150        160        170        180 
FRKVCKDFAF SQIERQRQQF KRLGVRGDWE KPYLTLDPEY EAKQIEVFGE MAKRGYIYKG 

       190        200        210        220        230        240 
LKPVYWCPSC ETALAEAEIE YFDETSDSIY VKFRVRDDLG KFKGIVEDLS NVYFVIWTTT 

       250        260        270        280        290        300 
TWTIPANLAI ALNPEFDYSL TKFGDEVYII AKDMIEEVRK ETGLGDYEIL ATFKGKELEG 

       310        320        330        340        350        360 
MKAVHPIYNR DSIVVLGEHV TLDAGTGCVH TAPGHGEEDF LVGQEYGLEA LNPIDEKGYF 

       370        380        390        400        410        420 
TDKAPGYEGL YYAEANKVIK EDLRKANALL AEKKITHSYP HCWRCKSPIL FRATEQWFAS 

       430        440        450        460        470        480 
VEGFREEALK AIKEVNWYPA WGEERITNMV RDRKDWCISR QRVWGVPIPI FYCENCGKPL 

       490        500        510        520        530        540 
INDETINAVK ELFRQKGSDA WFEMSAEEIL PEGIKCECGS TKFRKETDIM DVWFDSGSSH 

       550        560        570        580        590        600 
AAVLETHPDL KWPAELYLEG SDQHRGWFQS SLLTAVATRG KAPYKNVLTH GFVVDGEGRK 

       610        620        630        640        650        660 
MSKSLGNVVD PAEVIQEYGA DVLRLWVVSA DYTADMRTSP EILKQIAEVY RKIRNTARFL 

       670        680        690        700        710        720 
LGNLYDFDPD KDMLPYEELL EIDKWALYRL NRLVKQLTES FDKYEFYDFF HPVHNFCVVD 

       730        740        750        760        770        780 
MSSLYLDILK DRLYTYPAKS KERKAAQTTL YIILDTLVKL MAPVLAFTSE EIWWHMKHDR 

       790        800        810        820        830        840 
NNNFESVQLA DWPQVKEEYD NPYIIEKWEK LFDIRKDISK ALEIARSEKK IGHSLDAQVD 

       850        860        870        880        890        900 
IYPSSELYEF FKGFEDLQYV FIVSKVVLHD PQEVAPENAY VSEDYDLKIT VTRAPGEKCE 

       910        920        930 
RCWMYSETVG TIKEHPTICA RCASHIEEQL KV 

« Hide

References

[1]"A complete sequence of the T. tengcongensis genome."
Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R. expand/collapse author list , Wang J., Yu J., Yang H.
Genome Res. 12:689-700(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 15242 / JCM 11007 / NBRC 100824 / MB4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008691 Genomic DNA. Translation: AAM24798.1.
RefSeqNP_623194.1. NC_003869.1.

3D structure databases

ProteinModelPortalQ8R9L3.
SMRQ8R9L3. Positions 1-929.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273068.TTE1594.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM24798; AAM24798; TTE1594.
GeneID996077.
KEGGtte:TTE1594.
PATRIC23897890. VBITheTen82880_1594.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

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_THETN
AccessionPrimary (citable) accession number: Q8R9L3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: June 1, 2002
Last modified: April 16, 2014
This is version 78 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