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A6LK77 (SYI_THEM4) 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:Tmel_0461
OrganismThermosipho melanesiensis (strain BI429 / DSM 12029) [Complete proteome] [HAMAP]
Taxonomic identifier391009 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermosipho

Protein attributes

Sequence length908 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 – 908908Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022137

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif588 – 5925"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8761Zinc By similarity
Metal binding8791Zinc By similarity
Metal binding8961Zinc By similarity
Metal binding8991Zinc By similarity
Binding site5471Aminoacyl-adenylate By similarity
Binding site5911ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A6LK77 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: A10220901D34034F

FASTA908105,172
        10         20         30         40         50         60 
MDYKETLNLP STEFSMRANL VKKEPEMIKK WHEMDDYNLI LKSREGKPKF VLHDGPPYAN 

        70         80         90        100        110        120 
GNIHIGTATN KILKDIVIRY KTMRGYYAPY VPGWDTHGLP IEHRVSVEMG EKIKGMSPVE 

       130        140        150        160        170        180 
IRQKCKEFAL HFVDVQREQF KRLGVRGDWD NPYLTLDPKY EKHILNIFKT LVKNGNVYRG 

       190        200        210        220        230        240 
NKPVYWCPTC KTALAEAEVE YHDHSSPSIY VKFELEKNTY IVIWTTTPWT LPANVAIAVH 

       250        260        270        280        290        300 
PEYDYVKIKV GNEYWIVAEG LLNKFAAETE IEYSVVEKFK GKDLEHKKAK HPFMNRESLI 

       310        320        330        340        350        360 
VLADYVTLED GTGCVHTAPG HGAEDYLTGI KYNLPVLSPV NEEGVFTKDA GKYAGLKIWD 

       370        380        390        400        410        420 
ANKVIIEDLE KLGVLIKSQK IEHSYPHCWR CKNPVIFRAT PQWFISVDRN GLREKVLEEI 

       430        440        450        460        470        480 
KKVEWHPKWG ENRITAMVKE RPDWTISRQR VWGTPIPAIK CKECGEVFLD EKVIDNFVNI 

       490        500        510        520        530        540 
VEEKGTDAWF ELSEDELIPE GVKCPKCGKN SFEKTYDTLD VWIDSGCSFE AVIRSKGEKF 

       550        560        570        580        590        600 
PVDLYLEGDD QHRGWFQSSI FMSVAHTNIA PYKSVVTHGF IKDEHGRKMS KSLGNVIDPK 

       610        620        630        640        650        660 
EIVDKYGADI LRLWVSSIDF FDNIRVGKNI IQQQVETYKK LRNTLRYLLG NLNDFEENMI 

       670        680        690        700        710        720 
VPFEKLLPLD KWALGRLQEV ISQVTEHFEK YEYSKVYSLL NRYCTVELSA TYLDIIKDRI 

       730        740        750        760        770        780 
YVEAKGSIYR RSAQTVMYYI LQSLIKMLAP ILVFTAEEAY QLSPFKKYET VHLEYWPEVK 

       790        800        810        820        830        840 
EEYIDNQIME DFKMILLIRD DVLKALEEAR KQDIIGHSLD AKVTIEGLND NVQMIIEKHK 

       850        860        870        880        890        900 
DYLSEIFIVS DVEIGNGQTK GEFVSVTVEK AKGEKCQRCW KYSEDVGKDD TYKDVCPRCA 


AVLKGERK 

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References

[1]"Complete sequence of Thermosipho melanesiensis BI429."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BI429 / DSM 12029.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000716 Genomic DNA. Translation: ABR30328.1.
RefSeqYP_001305713.1. NC_009616.1.

3D structure databases

ProteinModelPortalA6LK77.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391009.Tmel_0461.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR30328; ABR30328; Tmel_0461.
GeneID5297673.
KEGGtme:Tmel_0461.
PATRIC23922081. VBITheMel19269_0486.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycTMEL391009:GHM1-485-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_THEM4
AccessionPrimary (citable) accession number: A6LK77
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 24, 2007
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