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Q7VP34 (SYI_HAEDU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. 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:HD_0272
OrganismHaemophilus ducreyi (strain 35000HP / ATCC 700724) [Complete proteome] [HAMAP]
Taxonomic identifier233412 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length935 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 – 935935Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098394

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif600 – 6045"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8981Zinc By similarity
Metal binding9011Zinc By similarity
Metal binding9181Zinc By similarity
Metal binding9211Zinc By similarity
Binding site5591Aminoacyl-adenylate By similarity
Binding site6031ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VP34 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 7050B5D1ACFFAF54

FASTA935105,766
        10         20         30         40         50         60 
MTDYKDTLNL PETGFPMRGD LAKREPAMLK NWYDKNLYQQ IRQTSKGKKT FILHDGPPYA 

        70         80         90        100        110        120 
NGNLHLGHAV NKILKDIIMK SKTASGFDTP YVPGWDCHGL PIELKVESIV GKPNEKISAA 

       130        140        150        160        170        180 
EFRQACREYA NEQVDRQKAD FIRMGVLGDW DNPYLTMNFN TEASIIRTLA KVIANGHLYK 

       190        200        210        220        230        240 
GSKPVHWCLD CGSSLAEAEV EYEDKVSPSI YVRFKACDET AIETLFNAKG NGPISAIIWT 

       250        260        270        280        290        300 
TTPWTMPSNR AIAIHPELEY ALVQLADERV ILATELVESV AKAIEAESFD ILATVKGETL 

       310        320        330        340        350        360 
QLLRFHHPFY AFDVPFIFGD HVTTEGGTGL VHTAPDHGTD DFIIARKNNI EMAGLIGNDG 

       370        380        390        400        410        420 
KFKSDVEFFA GLAVFESNEK VIEKLKETGA LLKLARIKHS YPHCWRHKTP IIFRATPQWF 

       430        440        450        460        470        480 
IGMEKQGLRA QALAEIKTVR WIPNWGEARI DTMVANRPDW CISRQRTWGV PMAMFVHNET 

       490        500        510        520        530        540 
EELHPRTLDI LELVAQRVEQ QGIQAWWDLD PTEVLGEDAQ HYHKVPDTLD VWFDSGSTYA 

       550        560        570        580        590        600 
SVVEQRPEFN GQTADMYLEG SDQHRGWFMS SLMLASATNG KAPYQQVLTH GFVVDEKGRK 

       610        620        630        640        650        660 
MSKSIGNVIV PSEVWNKNGA DILRLWVAST DYTAEMKVSH GILNSAGDAY RRIRNTARFL 

       670        680        690        700        710        720 
LSNLNGFIPA RDEVKPNEMI ALDRWAVSCA LEAQNDIIEA YEHYQFHTVV QRLMRFCSIE 

       730        740        750        760        770        780 
MGSFYLDIIK DRQYTTKADS LARRSCQTAL WHIAEALVRW IAPILSFTAD EIWSHLPTVE 

       790        800        810        820        830        840 
GRSEFVFTEQ FYSQLFTLNC HDKLDDNYWQ QLINIRAEVN RVLEQARNEK TIGAGLEAKV 

       850        860        870        880        890        900 
TVYANDEMLP LLHQLGNELR FVLITSQAIV KPLSEADVAE GELAGLAVKV ERAEGEKCPR 

       910        920        930 
CWHFATDIGT HAEHNAICGR CVENVAGKGE VRRFA 

« Hide

References

[1]"The complete genome sequence of Haemophilus ducreyi."
Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 35000HP / ATCC 700724.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017143 Genomic DNA. Translation: AAP95253.1.
RefSeqNP_872864.1. NC_002940.2.

3D structure databases

ProteinModelPortalQ7VP34.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233412.HD0272.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP95253; AAP95253; HD_0272.
GeneID1490272.
KEGGhdu:HD0272.
PATRIC20177107. VBIHaeDuc133973_0221.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycHDUC233412:GH5F-250-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_HAEDU
AccessionPrimary (citable) accession number: Q7VP34
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 74 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