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C1DCX2 (SYI_LARHH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 41. 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:LHK_00614
OrganismLaribacter hongkongensis (strain HLHK9) [Complete proteome] [HAMAP]
Taxonomic identifier557598 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeLaribacter

Protein attributes

Sequence length957 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 – 957957Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000216239

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif635 – 6395"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9201Zinc By similarity
Metal binding9231Zinc By similarity
Metal binding9401Zinc By similarity
Metal binding9431Zinc By similarity
Binding site5941Aminoacyl-adenylate By similarity
Binding site6381ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
C1DCX2 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: F4891ED2EA3BB86F

FASTA957106,364
        10         20         30         40         50         60 
MDLKKTVNLL DTPFPMRGDL ARREPGWLAQ WQAQQRYQKL RKIAAGRPKF ILHDGPPYAN 

        70         80         90        100        110        120 
GDIHIGHAVN KILKDIIVRS KTQAGFDAPY VPGWDCHGLP IEHQIEKLVK GDKKAIEAAP 

       130        140        150        160        170        180 
SIHARITEYR KANGLDAKAT DLPASFIREL CREYAGLQVE RQKKDFIRLG VLGEWDNPYR 

       190        200        210        220        230        240 
TMSFRSEADE IRALGKLYQQ GYLFKGLKPV YWCFDCGSAL AEAEVEYQDK TSPTIDVAFA 

       250        260        270        280        290        300 
SAEPEKLAAA FGLSALPAGK TASAVIWTTT PWTIPANQAL NVHPDFDYGL YDTEKGLLIL 

       310        320        330        340        350        360 
AADLAKGALE RFGLTGVEVA RCKGQALDRL TFRHPFYDRV SPVYVGDYVT LDAGTGIVHS 

       370        380        390        400        410        420 
APAYGLEDFD SCRKNGMPND AILNPVTSDG TYVDSLPFFG GLHIWKANPL IVEKLAEVGA 

       430        440        450        460        470        480 
LMHTSPLSHS YPHCWRHKTP VVYRATTQWF VGMDREVAGS TLRQRALKGV DDTAFFPAWG 

       490        500        510        520        530        540 
QARLHAMIAN RPDWCVSRQR NWGVPIPFFL DKQTGEPHPR TPELLEAVAR KVEEQGINAW 

       550        560        570        580        590        600 
FELDPAELLG EDAARFDKMK DTLDVWFDSG TTHFHVLRGT HAEQLAYPAD LYLEGSDQHR 

       610        620        630        640        650        660 
GWFHSSLLTG CALDGRAPYN QLLTHGFVVD GQGRKMSKSV GNVIAPQKIN DSLGADILRL 

       670        680        690        700        710        720 
WVASTDYSGE LAISDTILKG TTDSYRRLRN TIRFLLANLS DFNPATDALP VSELTELDRY 

       730        740        750        760        770        780 
ALVLAQRLHA GVAEDCYPRY AFHTAMQAIV GYCTDDLGAF WLDIIKDRLY TTKADSKARR 

       790        800        810        820        830        840 
SAQTALWHVT RSLLSLLAPV LCFTADEAWQ ALTGEAEDSP VYHTWHELPV VADAEALAAR 

       850        860        870        880        890        900 
WDVLRALRAQ INKDIETLRE AGAVGSSLQA EVDIEADAGL YPLLNALGDE LKFVLIVSRV 

       910        920        930        940        950 
GVVPGPETRI RVSASGEQKC ERCWHYHPTV GENAEAPTLC ARCYDNIFGQ GESRSYA 

« Hide

References

[1]"The complete genome and proteome of Laribacter hongkongensis reveal potential mechanisms for adaptations to different temperatures and habitats."
Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L., Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J., Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.
PLoS Genet. 5:E1000416-E1000416(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HLHK9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001154 Genomic DNA. Translation: ACO73607.1.
RefSeqYP_002794616.1. NC_012559.1.

3D structure databases

ProteinModelPortalC1DCX2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557598.LHK_00614.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO73607; ACO73607; LHK_00614.
GeneID7756237.
KEGGlhk:LHK_00614.
PATRIC22298325. VBILarHon49832_0585.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycLHON557598:GHO5-622-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. 2 hits.
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_LARHH
AccessionPrimary (citable) accession number: C1DCX2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: July 9, 2014
This is version 41 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