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Q46XM7 (SYI_CUPPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. 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:Reut_A2745
OrganismCupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134)) [Complete proteome] [HAMAP]
Taxonomic identifier264198 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length963 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.

Sequence caution

The sequence AAZ62106.1 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
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 – 963963Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098452

Regions

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

Sites

Metal binding9261Zinc By similarity
Metal binding9291Zinc By similarity
Metal binding9461Zinc By similarity
Metal binding9491Zinc By similarity
Binding site5961Aminoacyl-adenylate By similarity
Binding site6401ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q46XM7 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: E3CFF0F4E3D78986

FASTA963108,201
        10         20         30         40         50         60 
MSDDKRAKPE KSKYPVNLLD TTFPMRGDLP KREPQWVKQW QDKQLYKKIR AARKGAKKFV 

        70         80         90        100        110        120 
LHDGPPYANG DIHIGHAVNK VLKDMIVKAR GLSGLDAVYV PGWDCHGMPI EIQIEKQFGK 

       130        140        150        160        170        180 
GLPVQEVQAK ARAYATEQIK RQMVDFERLG VLGDWGHPYL TMNYSNEADE LRALGKIMEK 

       190        200        210        220        230        240 
GYVFRGLKPV NWCFDCGSAL AEAEVEYKDK VDLSIDVGFP FAETDKLAHA FKLSIEQLNA 

       250        260        270        280        290        300 
KPGWIVIWTT TPWTIPSNQA LNVHPEVEYA LVDTPRGYLI LATERVEEQL KIYELEGKVV 

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

       370        380        390        400        410        420 
AHGMSDHDII SPVMGNGVYA GTLPLFGGLS IWDANPKIVE VLKASGNLFN SHKYTHSYMH 

       430        440        450        460        470        480 
CWRHKTPIIY RATSQWFAGM DVDPVEQDGK AVPTLRETAL AGIEATEFYP SWGKQRLHNM 

       490        500        510        520        530        540 
IANRPDWTLS RQRQWGVPMA FFVHKETGAL HPRTAELLEE VARRVEQHGI EAWQTLDPKD 

       550        560        570        580        590        600 
LLGDEADQYE KNRDTLDVWF DSGTTHWTVI RGSHRDDLYD PSADEADGRL ADLYLEGSDQ 

       610        620        630        640        650        660 
HRGWFHSSLL TASMLYGKPP YKALLTHGFT VDGEGRKMSK SVGNTVSPQD IANKMGAEII 

       670        680        690        700        710        720 
RLWVASTDYS GELSISDEIL KRVVESYRRI RNTLRFLLSN LSDYDHSKHA LPASEWLEID 

       730        740        750        760        770        780 
RYAVALTERL QKEVLSHYDS YEFHPVVAKL QTFCSEDLGG FYLDVLKDRL YTTAADSKAR 

       790        800        810        820        830        840 
RAAQNALYHI TQAMLHWMAP FLSFTAEEAW QVFAHGTGHT DTIFTSTYYT LPEVDQADDL 

       850        860        870        880        890        900 
LQKWHSLREV RAEVTKQLEA VRVEGAIGSS LQAEVNIQAG GPVLAALQSL EDDLRFVLLT 

       910        920        930        940        950        960 
SAATVTPAPE AGDLLVTVTA STHAKCERCW HYRADVGQNP DHPTLCGRCD SNLFGAGEHR 


SHA 

« Hide

References

[1]"Complete sequence of chromosome 1 of Ralstonia eutropha JMP134."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JMP134 / LMG 1197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000090 Genomic DNA. Translation: AAZ62106.1. Different initiation.
RefSeqYP_296950.1. NC_007347.1.

3D structure databases

ProteinModelPortalQ46XM7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264198.Reut_A2745.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ62106; AAZ62106; Reut_A2745.
GeneID3612451.
KEGGreu:Reut_A2745.
PATRIC20231166. VBIRalEut24049_3416.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycCPIN264198:GIW3-2792-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_CUPPJ
AccessionPrimary (citable) accession number: Q46XM7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: May 14, 2014
This is version 65 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