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

A9BDK6 (SYI_PROM4) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 51. 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:P9211_02611
OrganismProchlorococcus marinus (strain MIT 9211) [Complete proteome] [HAMAP]
Taxonomic identifier93059 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length969 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 – 969969Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189186

Regions

Motif68 – 7811"HIGH" region HAMAP-Rule MF_02002
Motif626 – 6305"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9391Zinc By similarity
Metal binding9421Zinc By similarity
Metal binding9591Zinc By similarity
Metal binding9621Zinc By similarity
Binding site5851Aminoacyl-adenylate By similarity
Binding site6291ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9BDK6 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 9C4CAAB0CD942EAF

FASTA969109,816
        10         20         30         40         50         60 
MTKETRQGEQ NRPSYKESLN LLKTSFGMRA NATLREPELQ NFWADKGIDL ELGLANKGPS 

        70         80         90        100        110        120 
FTLHDGPPYA NGALHMGHAL NKVLKDIINK FHIMRGHKVH FVPGWDCHGL PIELKVLQTL 

       130        140        150        160        170        180 
SNKERQALTP IQLRKKAAAY ASKQVKGQME GFKRWGIWGN WNKPYLTLQK EYESAQVKLF 

       190        200        210        220        230        240 
GQMVLKGYIY RGLKPVHWSP SSRTALAEAE LEYPEAHTSP SVYVAFSVIH LPQSLSENLI 

       250        260        270        280        290        300 
KQGLELPGDE VELSKRLKVC IWTTTPWTLP ANAAVSVNSN LDYSFVRHEE KGQILIFATE 

       310        320        330        340        350        360 
LLEEVSEILG ISFKQVANAK GESLKGILYK HPLYERTAPI VLGGSYITTQ SGTGLVHTAP 

       370        380        390        400        410        420 
GHGIDDFKTG LQNNLEVFCP VDEKGIFTSE AGKFEGLNVL KDANKEIISS LEISGSLLKE 

       430        440        450        460        470        480 
LPYVHKYPYD WRTKKPTIFR ATEQWFASVE GFREDALKAI DDVEWLPESG RNRIQSMVRE 

       490        500        510        520        530        540 
RGDWCISRQR TWGIPIPVFY KKNTNEILLN KETIDHIENL FAQYGADIWW EFDESKLLPP 

       550        560        570        580        590        600 
SLASESHHWQ KGVDTMDVWF DSGSSWASVS CQRDELGYPA DLYLEGTDQH RGWFQSSLLT 

       610        620        630        640        650        660 
SVAVNGHAPY KKVLTHGFAL DENGRKMSKS LGNIIDPTVI INGGTNKKTD PAYGADVLRL 

       670        680        690        700        710        720 
WVSSVDYSVD VPIGSNILKQ LSDVYRKVRN TSRYLLGNLH DFDPKKNSVD IDNLPILDKW 

       730        740        750        760        770        780 
MLNRTAEVID EITLAFEKYE FSRFFQLLQS FCTVDLSNFY LDIAKDRLYV SAPDDPRRRA 

       790        800        810        820        830        840 
CQTVMALIIE KLAGLISPVL CHMAEDIWQN IPYQLSEESV FKRGWPVSPS NWKRASLTEP 

       850        860        870        880        890        900 
ISLIRELRTS VNRVLEGCRN RQELGSSLEA GLRLEITNQG LLDAIDFLAK NGDHDVDCIR 

       910        920        930        940        950        960 
DWFLVSQLQI GGEPWAEVLI SQQFELGVIE ISNARGYKCE RCWHYEQDIG SCSEHPTLCG 


RCVTVMNRL 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9211.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000878 Genomic DNA. Translation: ABX08192.1.
RefSeqYP_001550146.1. NC_009976.1.

3D structure databases

ProteinModelPortalA9BDK6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93059.P9211_02611.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX08192; ABX08192; P9211_02611.
GeneID5731556.
KEGGpmj:P9211_02611.
PATRIC22985966. VBIProMar136502_0279.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPMAR93059:GHJV-265-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_PROM4
AccessionPrimary (citable) accession number: A9BDK6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: January 15, 2008
Last modified: April 16, 2014
This is version 51 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