Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A5CX61 (SYI_VESOH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 54. 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:COSY_0322
OrganismVesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA) [Complete proteome] [HAMAP]
Taxonomic identifier412965 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriasulfur-oxidizing symbionts

Protein attributes

Sequence length955 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 – 955955Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022140

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif593 – 5975"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9181Zinc By similarity
Metal binding9211Zinc By similarity
Metal binding9381Zinc By similarity
Metal binding9411Zinc By similarity
Binding site5521Aminoacyl-adenylate By similarity
Binding site5961ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A5CX61 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 5D73688DC5DC10A2

FASTA955109,700
        10         20         30         40         50         60 
MSDYKSSLNL PSTQFSMKAN LANREGKFLK KWQNDRLYDQ IRKQNQGKPK FVLHDGPIYA 

        70         80         90        100        110        120 
NGDIHIGHAV NKVLKDIIVK SKSLSGFDAP YVPGWDCHGL PIELNVEKEY GKVGIKIDVN 

       130        140        150        160        170        180 
TFRYKCREYA DHQVMRQSQD FQRLGILSDW DNPYLTKDFK YEADVVRALG QVVKNGHVYK 

       190        200        210        220        230        240 
GHKPLHWCTE CGSALAEAEV EYKNKQSEAI DVKFRIIEDS VFNVKKPVSV VIWTTTPWTL 

       250        260        270        280        290        300 
PANEAVALHS ELNYVLVDIG SEYLLLSQSL VVNSISRYDI KVTIGERMFS SSELEGLKVQ 

       310        320        330        340        350        360 
HPFYDKQVPI ILGDHVTIDS GTGAVHIAPA HGQEDFIAGL KYNLPIDCPV DAKGVFFKEI 

       370        380        390        400        410        420 
LLLGGQFIFK ANASVIRILK ETNTLVKHES LTHSYPHCWR HKTPIIFRIT SQWFISMQQN 

       430        440        450        460        470        480 
GLRDIVNSEI QKVQWIPHWS KKRIELMVDN RPDWCISRQR FWGVPITLFV HKKTGELHPN 

       490        500        510        520        530        540 
TQMLFVCIAN RIEQEGIEAW FKSDTKDFIG DDVNDYDKIT DILDVWFDSG MSHFVVLKVR 

       550        560        570        580        590        600 
KELSNVADLY LEGSDQHRGW FQSSLISSVA INKKAPYKNV LTHGFVVDKD GKKMSKSLGN 

       610        620        630        640        650        660 
IISPQKIVNN VGADILRLWI ASTDYTGEMT VSDEILKRSA DSYRRIRNTM RFMLANMNGF 

       670        680        690        700        710        720 
TQKNLVDTKA MLDLDRWIVA KTQKIQEAII ENYDTYQFHY IVKSINNFCS NDLGGFYLDI 

       730        740        750        760        770        780 
IKDRQYTTQK DSPARRSAQT ALYHITQMMV RWLSPILSFT SEEIWQELAP NKKSIFLQEW 

       790        800        810        820        830        840 
YLQVDTIDNV VFDDGIIYGT MISSHISQEQ REGLEKSDDI FTSINIVRII SPTIRQAIEK 

       850        860        870        880        890        900 
LRKDKVLGAS LEAEVDIYCN LKVKEKLSKF GEELRFMFIT SDVRLHSFEE KPNNAIEVDS 

       910        920        930        940        950 
DVLQQVAIVV VKSEHSKCVR CWHHRKDVGS NNKYLELCCR CVENVDGDGE VRKFA 

« Hide

References

[1]"Reduced genome of the thioautotrophic intracellular symbiont in a deep-sea clam, Calyptogena okutanii."
Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M., Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., Sato T., Kato C., Kitagawa M., Kato I., Maruyama T.
Curr. Biol. 17:881-886(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HA.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009247 Genomic DNA. Translation: BAF61447.1.
RefSeqYP_001219171.1. NC_009465.1.

3D structure databases

ProteinModelPortalA5CX61.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING412965.COSY_0322.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF61447; BAF61447; COSY_0322.
GeneID5172097.
KEGGvok:COSY_0322.
PATRIC32020463. VBICanVes128383_0317.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCVES412965:GHZZ-321-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.
InterProIPR002300. 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. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYI_VESOH
AccessionPrimary (citable) accession number: A5CX61
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: April 16, 2014
This is version 54 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