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Q2RK59 (SYI_MOOTA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 67. 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:Moth_0863
OrganismMoorella thermoacetica (strain ATCC 39073) [Reference proteome] [HAMAP]
Taxonomic identifier264732 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella

Protein attributes

Sequence length930 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 – 930930Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022092

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif596 – 6005"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8961Zinc By similarity
Metal binding8991Zinc By similarity
Metal binding9161Zinc By similarity
Metal binding9191Zinc By similarity
Binding site5551Aminoacyl-adenylate By similarity
Binding site5991ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2RK59 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: F09E475EDD3423AE

FASTA930106,238
        10         20         30         40         50         60 
MDYSKTLNLP RTDFPMRANL PQREPEILKF WEENDIYGKV QEANRGKPKF ILHDGPPYAN 

        70         80         90        100        110        120 
GHLHLGHTLN KILKDIIIKY HSMNGYDAPY VPGWDTHGLP IEQQAIKNLG LNRHAVDVVE 

       130        140        150        160        170        180 
FRNRCRDYAL KYVNIQREEF KRLGVRGDWE HPYLTLEPEY EAIQIGIFGE MAKKGYIYKG 

       190        200        210        220        230        240 
LKPVYWCTDC ETALAEAEVE YGEERSPSIY VKFPVADARG LFEPRGSSIV IWTTTPWTLP 

       250        260        270        280        290        300 
ANVAIALHPE FKYVLIQVGE ERLLMAAELV RPVLELLGVK DYQVVATFTG SELEGVVCRN 

       310        320        330        340        350        360 
PLMDRDSVVI LGEHVTLEQG TGCVHTAPGH GLEDYEVGMR YHLPVLSPLD DRGRFTEEGG 

       370        380        390        400        410        420 
QFAGLFIDEA NKAVVKELEA RGALLHFGFI KHQYPHCWRC KHPIIFRATE QWFASIEGFR 

       430        440        450        460        470        480 
QEALEAIKKV KWIPSWGEDR IYNMVADRSD WCISRQRTWG VPIPIFYCAN CGREIINDAT 

       490        500        510        520        530        540 
ISHLQELFRK HGSNVWFARE AGELVPPGLK CPECGSKEFR KETDIMDVWF DSGSSHAAVL 

       550        560        570        580        590        600 
ATRPELAWPA DLYLEGSDQH RGWFNSSLST AVATRGRAPY RQVLTHGFLV DEEGRKMSKS 

       610        620        630        640        650        660 
LGNGIDPADV IRQRGADVLR LWVASADYRR DVAASENIMR QITEAYRKIR NTCRFLLANL 

       670        680        690        700        710        720 
ADFDPGKDQV PREEMLELDR WAMNRLQRLI ARVTMAYDDY EFHVVYHTIH NFCAVDLSAV 

       730        740        750        760        770        780 
YLDIIKDRLY TWPAASKGRR SAQTVLYETI NVLVRLLTPI LAFTTEEIWR YLPGEDDRPI 

       790        800        810        820        830        840 
SVQLAGWPQV KTEFLDDELE EKWKRILQVR DVVARALERA RQEQDLGNSL NAAVHLYPDA 

       850        860        870        880        890        900 
DMYQFLKPLG DELATIMIVS RVDLHQPGEE APAGSLEAPE LPGLRVYVTG APGQKCERCW 

       910        920        930 
MVSETVGQDT DHPTLCRRCA TVVKEMYMNG 

« Hide

References

[1]"The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum)."
Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C., Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.
Environ. Microbiol. 10:2550-2573(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39073.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000232 Genomic DNA. Translation: ABC19180.1.
RefSeqYP_429723.1. NC_007644.1.

3D structure databases

ProteinModelPortalQ2RK59.
SMRQ2RK59. Positions 1-926.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264732.Moth_0863.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC19180; ABC19180; Moth_0863.
GeneID3831750.
KEGGmta:Moth_0863.
PATRIC22638876. VBIMooThe6753_0926.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycMTHE264732:GH0A-899-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_MOOTA
AccessionPrimary (citable) accession number: Q2RK59
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 24, 2006
Last modified: April 16, 2014
This is version 67 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