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Q97AG7 (SYI_THEVO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. 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:TV0843
ORF Names:TVG0867938
OrganismThermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1) [Complete proteome] [HAMAP]
Taxonomic identifier273116 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length1028 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.

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 – 10281028Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098596

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
Q97AG7 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: ABBBCD972B46641F

FASTA1,028119,494
        10         20         30         40         50         60 
MQAQRYRLIE QGNTIMDIDN EILRYWNDHA INEKIFKKEG TKKFVFLEGP PTANGRPHIG 

        70         80         90        100        110        120 
HAMTRTIKDI VLRYNTMTGH KIYRRYGGWD CHGLPVELEA EKYFGFKTKS DIINYGVEKF 

       130        140        150        160        170        180 
NSYCRDSVFR YIDEWKTVDQ IIGFSIDHSG DYITLRNEYI ESEWYVLKYI YENGLLYKDY 

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

       250        260        270        280        290        300 
VVNPDIEYSL IEYNNAKYYV ASSRAQYIFK DFKVLKKMKG FELAGKGYEQ LLPFLDPPAG 

       310        320        330        340        350        360 
ALRVVTGDFV TDIDGSGIVH AAPAFGSDDY QIGKRENVPI LNPVDKNGRF SDERLPWYGK 

       370        380        390        400        410        420 
KVREANEDII VYLKNNGLLI KSEKYEHSYP FCYRCDTPLL YYPLDAWFIR VSSVRDKLVE 

       430        440        450        460        470        480 
NNEKIRWKPD YLKHGRFGNF LDEAKDWNLS RDRFWGTPLP VWRCRNNHVR FIGSRKEIEE 

       490        500        510        520        530        540 
MGATVPQDLH RPYIDEVKFV CPDCGEEMRR EPYVIDTWFD SGSATYAAMH YPFEDNFDPS 

       550        560        570        580        590        600 
SDLPVSFITE AIDQTRGWFY VLHVISTIMF NKNAYDSALS ISFILDEQGR KMSKSKGNSV 

       610        620        630        640        650        660 
FALDYLKQVA PDSLRLFFLY GAPWKSKNLD RKIIDEVSRR VISTLLNVYS FFAYNANIDG 

       670        680        690        700        710        720 
FEFKGILEAK DTLDKWLISK INTFIIESRR AYDDLDFHEV VRLSMDFVDN LSNFYLRLSR 

       730        740        750        760        770        780 
RRFWAEDVTE DKLAAYSTLY TAIMTCSKVL APIVPFVSDY LYLSLHGPYE SIHLDSFPEP 

       790        800        810        820        830        840 
DTSKIDHDLE KRMDQAYSVI ETVRRIRQEI NIKGRQPVKE ILLSGNIDPE IIPVVSQEVN 

       850        860        870        880        890        900 
AKEIRIVSSE QRPLKYTVDL KMETAAPILR SSVNSVREAL KSIDGKAAFD AVQNGGKLRV 

       910        920        930        940        950        960 
LDHELTGEML NISTIPDPDY GYSRDEKNGI DVFVNKRIDR NEYLEGLARE IVRRIQLMRK 

       970        980        990       1000       1010       1020 
EMNLDYTDRI NVWIDPVGDF SDAIDKFESY IKAETQCDSL NVGHTDDLRK WEIGDETIGI 


RIEKVVPK 

« Hide

References

[1]"Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium."
Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y., Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T., Yamamoto Y., Aramaki H., Makino K., Suzuki M.
Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000011 Genomic DNA. Translation: BAB59985.1.
RefSeqNP_111348.1. NC_002689.2.

3D structure databases

ProteinModelPortalQ97AG7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273116.TVN0829.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB59985; BAB59985; BAB59985.
GeneID1441935.
KEGGtvo:TVN0829.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMADWNLSRS.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycTVOL273116:GC31-856-MONOMER.

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_THEVO
AccessionPrimary (citable) accession number: Q97AG7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2001
Last modified: April 16, 2014
This is version 76 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