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Q6YR34 (SYI_ONYPE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. 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:PAM_184
OrganismOnion yellows phytoplasma (strain OY-M) [Complete proteome] [HAMAP]
Taxonomic identifier262768 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesAcholeplasmatalesAcholeplasmataceaeCandidatus PhytoplasmaCandidatus Phytoplasma asteris

Protein attributes

Sequence length900 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 – 900900Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098433

Regions

Motif59 – 6911"HIGH" region HAMAP-Rule MF_02002
Motif591 – 5955"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8761Zinc By similarity
Metal binding8791Zinc By similarity
Metal binding8921Zinc By similarity
Metal binding8951Zinc By similarity
Binding site5501Aminoacyl-adenylate By similarity
Binding site5941ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6YR34 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 023BA5BF424BF031

FASTA900104,373
        10         20         30         40         50         60 
MTTNYKTTLL MPKTDFPMKG NLGKNEINIQ KHWQKLDLYQ KKLQQNQDNN PFILHDGPPY 

        70         80         90        100        110        120 
ANGNIHMGHA LNKILKDFIV RFRSMQGFYT PLIPGWDTHG LPIEAAVLKK TSKNAFTRKP 

       130        140        150        160        170        180 
LLDKCQEFAL ENVNNQKHQF QRLGILGDWQ NPYLTLDKTF VSDQVRIFGQ MVDKGLIFKA 

       190        200        210        220        230        240 
LKPIHWSPTL ESALAEAELE YHNHQSPSVY VAFSMKKLDI FDNVALVIWT TTPWTLPANV 

       250        260        270        280        290        300 
AIAVHPEKEY QLIEVLQKRY LVGTKNIPFL QKVFAWNKEN IKVVATFEGK TLEHLTYQNH 

       310        320        330        340        350        360 
LVSKFGKIIL SQHVLDGEGT GLVHIAPGHG LDDFLVGQKY NLDVVCSIDK KGMMTDVSKY 

       370        380        390        400        410        420 
QGLFYTKANE AIISDLEKDH SLLKADVILH SYPHDWRTKK PVISLALPQW FVSIKKIKSL 

       430        440        450        460        470        480 
LLEETQKVKW IPRWGELKMT NMITNREDWN ISRQRTWGVP IPIFYTETHQ PILDLKLINH 

       490        500        510        520        530        540 
VADLFEQHGM DIWYEWDVKK LLPENYINPQ SPNNLFTKEL DIMDVWFDSG TSYSVFKKRN 

       550        560        570        580        590        600 
QVLQSDVYLE GSDQYRGWFN SSLITSVATQ NQAPYKTVIT HGFVFDGEGK KMSKSLGNVI 

       610        620        630        640        650        660 
DPLTVAEQKG ADIIRLWVAN TNYNLDVRIN PSILKQVEDL YRKIRNTFRF MLGNLDNFKK 

       670        680        690        700        710        720 
DTNYIAFEQR TFIHQAMMLD FEEVLKNVLH SYDTYNFEGV LRHLFPFITN KISAFYLDFA 

       730        740        750        760        770        780 
KDILYIEKED HKERKMIQST IYDLLLSLLQ VLTPIIPHTT SEVYGFFPFA VEKDIYLEKM 

       790        800        810        820        830        840 
PQLKARPTSH LLLEYHKFLT LRKNVLQYLE KARQSGLINS SLQAHITLSL TQEEMHALDV 

       850        860        870        880        890        900 
LQIKDQLHQL FIVSKVTLQL KDTFDVKVAK ASGYACQRCW NVVITKPLTP LCTRCQNILK 

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References

[1]"Reductive evolution suggested from the complete genome sequence of a plant-pathogenic phytoplasma."
Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S., Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.
Nat. Genet. 36:27-29(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OY-M.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006628 Genomic DNA. Translation: BAD04269.1.
RefSeqNP_950436.1. NC_005303.2.

3D structure databases

ProteinModelPortalQ6YR34.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262768.PAM_184.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD04269; BAD04269; PAM_184.
GeneID2673552.
KEGGpoy:PAM_184.
PATRIC22809860. VBIOniYel86799_0253.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycMORG262768:GHF5-191-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_ONYPE
AccessionPrimary (citable) accession number: Q6YR34
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 73 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