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B0K8R7 (SYI_THEP3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:Teth39_0874
OrganismThermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium thermohydrosulfuricum) [Complete proteome] [HAMAP]
Taxonomic identifier340099 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeThermoanaerobacter

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_1000189210

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
B0K8R7 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: 0BD53F63FE09E523

FASTA932107,851
        10         20         30         40         50         60 
MDYNKTLNLP RTDFPMKANL PTREPEILKR WEEMDIYHKT LEKNKGKEKY ILHDGPPYAN 

        70         80         90        100        110        120 
GDIHIGTAMN KVLKDIIVKY KTMRGYDAPY VPGWDTHGLP IEQQAIKTLG IKRHEVSPTE 

       130        140        150        160        170        180 
FRKVCRDFAF SQIEKQKAQF KRLGVRGDWD NPYLTLNPEY EAKQIEVFGE MAKKGYIYKG 

       190        200        210        220        230        240 
LKPVYWCPSC ETALAEAEIE YFDETSDSIY VKFRVKDDLG KFKGIVENLN NVYFVIWTTT 

       250        260        270        280        290        300 
TWTIPANLAI ALNPEFDYAL AKFGDEVYIM AKDMLDTVKK EANLSDYEIV AVFKGKDLEG 

       310        320        330        340        350        360 
MKATHPLYDR DSLIILGEHV TLEAGTGCVH TAPGHGEEDF LVGQEYGLEV LNPIDDKGYF 

       370        380        390        400        410        420 
TDKAPGYAGL YYEEANKVIK EDLKKANALV AETRITHSYP HCWRCKSPII FRATEQWFAS 

       430        440        450        460        470        480 
VEGFREEALK AIKEVNWYPS WGEERITNMV RDRRDWCISR QRVWGVPIPI FYCEKCGKPL 

       490        500        510        520        530        540 
INDDTINAVK KIFRQKGSDA WFEMSAEEIL PKGITCECGS TKFRKETDIM DVWFDSGSSH 

       550        560        570        580        590        600 
AAVLQTHPDL KWPAELYLEG SDQHRGWFQS SLLTSVATRG KAPYRNVLTH GFVVDGEGRK 

       610        620        630        640        650        660 
MSKSLGNGID PADVIKEYGA DILRLWTVSA DFTSDMRISQ EILKQMTEAY RKIRNTSKFL 

       670        680        690        700        710        720 
LSNLYDFDPD KDMLPYEELL EIDKWALFRL NRVVEELTEA FDKYEYYDFL HLVHTFCVVD 

       730        740        750        760        770        780 
MSSLYLDILK DRLYTYPATS KERRAAQTTL YIILDTLVRL IAPVLTFTSE EIWSYMKHDS 

       790        800        810        820        830        840 
QNNFESVQLA DWPQVQEKYN NPYIIEKWEK LFDIRKDISK ALEIARTDKK IGHSLEAQVD 

       850        860        870        880        890        900 
IYPSQELYDF FKGFNDLEYV FIVSKVVLHQ PEEPAPQNAY ESDDYNLKIV VTHAPGEKCE 

       910        920        930 
RCWMYSETVG TIKEHPTICA RCASHIEQQT QV 

« Hide

References

[1]"Complete sequence of Thermoanaerobacter pseudethanolicus 39E."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33223 / 39E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000924 Genomic DNA. Translation: ABY94530.1.
RefSeqYP_001664866.1. NC_010321.1.

3D structure databases

ProteinModelPortalB0K8R7.
SMRB0K8R7. Positions 1-928.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING340099.Teth39_0874.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY94530; ABY94530; Teth39_0874.
GeneID5873648.
KEGGtpd:Teth39_0874.
PATRIC23886404. VBIThePse6203_0915.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycTPSE340099:GH4W-906-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_THEP3
AccessionPrimary (citable) accession number: B0K8R7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 18, 2008
Last modified: May 14, 2014
This is version 53 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