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Q9HJT4 (SYI_THEAC) 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:Ta0879
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length1026 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_02003

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003

Cofactor

Zinc By similarity. HAMAP-Rule MF_02003

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02003

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02003.

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_02003

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.

Sequence caution

The sequence CAC12008.1 differs from that shown. Reason: Erroneous initiation.

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 – 10261026Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098595

Regions

Motif51 – 6111"HIGH" region HAMAP-Rule MF_02003
Motif591 – 5955"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site5941ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HJT4 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: 0FE6AA2C39E9B50F

FASTA1,026119,169
        10         20         30         40         50         60 
MQSLRFRQID PGMTLREIDS EILKYWKDKN ILEKILSKGG SKKFVFLEGP PTANGRPHIG 

        70         80         90        100        110        120 
HAMTRTIKDI VLRYNTMTDH KIYRRVGGWD CHGLPVELEA EKHFGFHTKS EIVNFGVEKF 

       130        140        150        160        170        180 
NQYCRESIFR YIDEWKQVDD LIGFSIDHNG DYITLRNDYM ESEWFALKTM YNSGLLYKDY 

       190        200        210        220        230        240 
TVVPYCPRCE TSLSSHEVAQ GYKDVKDPSV YVRFKSADEE NTYFVAWTTT PWTLPSNEFL 

       250        260        270        280        290        300 
VVNPDMEYSL VEAQGSRYYV ASSRAGYIFK EYREIRRMHG RDLVGKRYLQ LMPFLDPPSG 

       310        320        330        340        350        360 
SLKVVAGSFV TSEDGSGIVH AAPAFGADDY QIGKEEGVEI LNPVDKNGRF ADPRIPWNGK 

       370        380        390        400        410        420 
FVRDANEDII VYLKKNQMLL KSEKYEHSYP FCYRCDTPLL YYPLDAWFIA VSRIRDKLVE 

       430        440        450        460        470        480 
YNERINWKPD YLKHGRFGNF LGEAKDWNLS RDRFWGTPLP AWRCKNGHLV FVGSRKEIED 

       490        500        510        520        530        540 
LGGKVPEDLH RPYIDEVRFK CPTCGEEMSR EPYVIDTWFD SGSATYAASH YPFEKNFDPE 

       550        560        570        580        590        600 
TDVPVSFITE AIDQTRGWFY VLHVIATIMF NKNAYESALS INFILDAQGR KMSKSKGNSV 

       610        620        630        640        650        660 
YALDFLNEVP PDSLRLFFLY GAPWKSKNLD KKVIDEVSRK TLMTVLNVYS FFAYNANIDN 

       670        680        690        700        710        720 
FQWNGLQLSG NALDRYMVSK VNSFVRSSRD AYESLDFHEV VRASMEFVDD LSNFYLRLSR 

       730        740        750        760        770        780 
RRFWAEGFDD DKLSAYSTLY YALKAFSEVM APITPFFSDF IYLNLGGDKE SVHLEAFPEF 

       790        800        810        820        830        840 
DSTLMDEKLE SEMDRAYSVI ETVRRLRQEN SIKGRQPLRE ILIAGDMEES IIDVVKSELN 

       850        860        870        880        890        900 
AKDIKLIERD QEPIRLSADL RMDRAAPVLR SRVNAVRHKI RSMDGLEVQR QISEKGFVEI 

       910        920        930        940        950        960 
DGVRLDPDMV EISRVPDPNY AYSQTEKYGI DVFINKNIDR DGYLEGLARE LVRRIQVMRK 

       970        980        990       1000       1010       1020 
EMNLNYTDRI ITHLDLSDDF LEALNKHAEY IKNETQSDSI ITDKVEGMKL WEINGEPVRI 


KIDLAR 

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References

[1]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL445065 Genomic DNA. Translation: CAC12008.1. Different initiation.
RefSeqNP_394338.1. NC_002578.1.

3D structure databases

ProteinModelPortalQ9HJT4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273075.Ta0879.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC12008; CAC12008; CAC12008.
GeneID1456418.
KEGGtac:Ta0879.

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMADWNLSRS.
ProtClustDBPRK06039.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02003. Ile_tRNA_synth_type2.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
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.
[Graphical view]
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_THEAC
AccessionPrimary (citable) accession number: Q9HJT4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 74 of the entry and version 2 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