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Q0IDA5 (SYI_SYNS3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 61. 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:sync_0333
OrganismSynechococcus sp. (strain CC9311) [Complete proteome] [HAMAP]
Taxonomic identifier64471 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length968 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 – 968968Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022135

Regions

Motif68 – 7811"HIGH" region HAMAP-Rule MF_02002
Motif625 – 6295"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9381Zinc By similarity
Metal binding9411Zinc By similarity
Metal binding9581Zinc By similarity
Metal binding9611Zinc By similarity
Binding site5841Aminoacyl-adenylate By similarity
Binding site6281ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0IDA5 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: B761E5BA2DE8B901

FASTA968108,080
        10         20         30         40         50         60 
MTQQTGQDAD QRPSYKDTLN LLETGFGMRA NAIHREPELQ AFWKEKGIDL DLGRNNPGPV 

        70         80         90        100        110        120 
FTLHDGPPYA NGALHMGHAL NKVLKDIINK HRLMQGRKVR FVPGWDCHGL PIELKVLQAM 

       130        140        150        160        170        180 
NQEQRQALTP IKLRKKAAAY AHKQVAGQRA GFQRWGIWAD WDHPYLTLQK DYEAAQIDVF 

       190        200        210        220        230        240 
GTMALKGHIY RGLKPVHWSP SSRTALAEAE LEYPDGHTSP SVYVGFPVVD LPESLRSKLN 

       250        260        270        280        290        300 
AQGLDVPAAS DTLSQCLQVA IWTTTPWTLP ANLAVSVNDR LDYCLADDGN GQLLIVAAEL 

       310        320        330        340        350        360 
CDSIASKLER PLQAKATVKG ADLAGITYSH PLLERRSAIV VGGEYITTES GTGLVHTAPG 

       370        380        390        400        410        420 
HGVDDFNTGR KHGLPVLCPV DEAGTLTAEA GPFEGLNVLK DANAKIIAAL EDSGSLLLQE 

       430        440        450        460        470        480 
SYSHRYPYDW RTKKPTIFRA TEQWFASVEG FRTEALTAID GVQWLPASGR NRIESMVSER 

       490        500        510        520        530        540 
GDWCISRQRT WGVPIPVFYQ RETGEVLLNS DSIAHVKALI AEHGADIWWE KDEVDLLPSS 

       550        560        570        580        590        600 
HKAEAHLWRK GTDTMDVWFD SGSSWASVSS QRDGLSYPAD LYLEGSDQHR GWFQSSLLTS 

       610        620        630        640        650        660 
VAVNGTAPYR TVLTHGFALD EKGRKMSKSL GNVVDPMVII EGGKNQKQEP AYGADVLRLW 

       670        680        690        700        710        720 
VSSVDYSADV PIGAGILRQL SDVYRKVRNT SRYLLGNLHD FIPSRDAISI SDLPLLDRWM 

       730        740        750        760        770        780 
LQRTATVLDQ ISEAFERYEF FRFFQLLQNF CVADLSNFYL DIAKDRLYVS APNDKRRRSC 

       790        800        810        820        830        840 
QTVMALIIER LAAAIAPVLC HMAEDIWQNI PYPTGTESVF LSGWPSVPEE WRDDSLRDPM 

       850        860        870        880        890        900 
QELRELRAAV NKVLEECRSK RKLGSSLEAA VRLEARTPAL QDALQWLQSK GDQEVDGLRD 

       910        920        930        940        950        960 
WLLVSQLQIG GEPWAELLAS DDNELAVIEV ALSRGQKCER CWHYEADIGQ YSDHPGLCGR 


CVSVLERR 

« Hide

References

[1]"Genome sequence of Synechococcus CC9311: insights into adaptation to a coastal environment."
Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H., Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S., Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R., Paulsen I.T.
Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC9311.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000435 Genomic DNA. Translation: ABI45549.1.
RefSeqYP_729567.1. NC_008319.1.

3D structure databases

ProteinModelPortalQ0IDA5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING64471.sync_0333.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI45549; ABI45549; sync_0333.
GeneID4260647.
KEGGsyg:sync_0333.
PATRIC23791520. VBISynSp88089_0342.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSSP64471:GIVP-333-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_SYNS3
AccessionPrimary (citable) accession number: Q0IDA5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: April 16, 2014
This is version 61 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