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Q0K7A0 (SYI_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:H16_A3046
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length964 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 – 964964Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022111

Regions

Motif66 – 7611"HIGH" region HAMAP-Rule MF_02002
Motif637 – 6415"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9271Zinc By similarity
Metal binding9301Zinc By similarity
Metal binding9471Zinc By similarity
Metal binding9501Zinc By similarity
Binding site5961Aminoacyl-adenylate By similarity
Binding site6401ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0K7A0 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 082E30A7D7350B97

FASTA964108,212
        10         20         30         40         50         60 
MPDDKRAKPE KSKYPVNLLD TPFPMRGDLP KREPQWVKQW QDKQLYKKIR AARKGAKKFV 

        70         80         90        100        110        120 
LHDGPPYANG DIHIGHAVNK VLKDMIIKAR GLTGLDAVYV PGWDCHGMPI EIQIEKKFGK 

       130        140        150        160        170        180 
GLPVQEVQAK ARAYATEQIK RQMMDFERLG VLGDWDHPYL TMNYSNEADE LRALGKIMEK 

       190        200        210        220        230        240 
GYVFRGLKPV NWCFDCGSAL AEAEVEYKDK VDLSIDVGFP FAQADKLAHA FKVPFEQLDG 

       250        260        270        280        290        300 
KPGWIVIWTT TPWTIPSNQA LNVHPEVEYA LVETPRGYLI LATERVEEQL KVYGLEGKVV 

       310        320        330        340        350        360 
ATTTGAALSE IRFHHPLAKM DAGYDRLSPV YLGDYVTTDT GSGIVHSAPA YGVEDFQSCK 

       370        380        390        400        410        420 
AHGMADSDII SPVMGNGVYA GTLPLFGGLS IWDANPKIVE VLQASGNLFN SHKYTHSYMH 

       430        440        450        460        470        480 
CWRHKTPIIY RATSQWFAGM DVDPADENGK TGPTLRETAL AGIDATEFFP AWGKQRLHNM 

       490        500        510        520        530        540 
IANRPDWTLS RQRQWGVPMA FFLHKETGAL HPRTPQLLEE VARRVEQHGI EAWQTLDPAE 

       550        560        570        580        590        600 
LLGDEASQYE KNRDTLDVWF DSGTTHWSVI RGSHRDDLYD PSADEADGRL ADLYLEGSDQ 

       610        620        630        640        650        660 
HRGWFHSSLL TASMLYGKPP YKALLTHGFT VDGEGRKMSK SIGNTVSPQD ISNKMGAEII 

       670        680        690        700        710        720 
RLWVASTDYS GELSISDEIL KRVVEGYRRI RNTLRFLLSN LSDYDHARHA LPASEWLEID 

       730        740        750        760        770        780 
RYAVALTAQL QKEVLSHYEA YEFHPVVSKL QTFCSEDLGG FYLDVLKDRL YTTAPDSKAR 

       790        800        810        820        830        840 
RAAQNALYHI TQAMLHWMAP FLSFTAEEAW QIFAHGTEHT DTIFTSTYYA IPEVDDGADD 

       850        860        870        880        890        900 
LLQKWHTLRE VRAEVTKQLE AVRVEGEIGS SLQAELTIQA GGPVLDALQS LGDDLRFVLL 

       910        920        930        940        950        960 
TSSAKVTHAP EAGDLLVTVT PSTHAKCERC WHYRADVGHN PDHPTLCGRC DSNLFGAGEH 


RSHA 

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References

[1]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260479 Genomic DNA. Translation: CAJ94121.1.
RefSeqYP_727489.1. NC_008313.1.

3D structure databases

ProteinModelPortalQ0K7A0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING381666.H16_A3046.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ94121; CAJ94121; H16_A3046.
GeneID4250185.
KEGGreh:H16_A3046.
PATRIC35235637. VBIRalEut6770_3447.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAERLMLHQ.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-3010-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_CUPNH
AccessionPrimary (citable) accession number: Q0K7A0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: May 14, 2014
This is version 62 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