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

A5UIA3 (SYI_HAEIG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:CGSHiGG_08385
OrganismHaemophilus influenzae (strain PittGG) [Complete proteome] [HAMAP]
Taxonomic identifier374931 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length941 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 – 941941Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022073

Regions

Motif59 – 6911"HIGH" region HAMAP-Rule MF_02002
Motif603 – 6075"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9041Zinc By similarity
Metal binding9071Zinc By similarity
Metal binding9241Zinc By similarity
Metal binding9271Zinc By similarity
Binding site5621Aminoacyl-adenylate By similarity
Binding site6061ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A5UIA3 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: C5869EF1754F8C9B

FASTA941106,490
        10         20         30         40         50         60 
MTVDYKNTLN LPETSFPMRG DLAKREPDML KNWYEKNLYQ KIRKASKGKK SFILHDGPPY 

        70         80         90        100        110        120 
ANGNIHIGHA VNKILKDIII KSKTALGFDS PYIPGWDCHG LPIELKVEGL VGKPNEKISA 

       130        140        150        160        170        180 
AEFRQKCREY AAEQVEGQKK DFIRLGVLGD WDNPYLTMNF DTEANIIRTL GKVIENGHLY 

       190        200        210        220        230        240 
KGSKPVHWCL DCGSSLAEAE VEYEDKVSPS IYVRFPAESA DEIEAKFSAQ GRGQGKLSAI 

       250        260        270        280        290        300 
IWTTTPWTMP SNRAIAVNAD LEYNLVQLGD ERVILAAELV ESVAKAVGIE HIEILGSVKG 

       310        320        330        340        350        360 
DDLELSRFHH PFYDFTVPVI LGDHVTTDGG TGLVHTAPDH GLDDFIVGKQ YDLPMAGLVS 

       370        380        390        400        410        420 
NDGKFISTTE FFAGKGVFEA NPLVIEKLQE VGNLLKVEKI KHSYPHCWRH KTPIIFRATP 

       430        440        450        460        470        480 
QWFIGMETQG LRQQALGEIK QVRWIPDWGQ ARIEKMVENR PDWCISRQRT WGVPMTLFVH 

       490        500        510        520        530        540 
KETEELHPRT LDLLEEVAKR VERAGIQAWW DLDEKELLGA DAETYRKVPD TLDVWFDSGS 

       550        560        570        580        590        600 
TYSSVVANRP EFNGQNIDMY LEGSDQHRGW FMSSLMLSTA TDSKAPYKQV LTHGFTVDGQ 

       610        620        630        640        650        660 
GRKMSKSIGN IVTPQEVMDK FGGDILRLWV ASTDYTGEMT VSDEILKRAA DSYRRIRNTA 

       670        680        690        700        710        720 
RFLLANLNGF DPKRDLVKPE EMVSLDRWAV ACALDAQNEI KDAYDNYQFH TVVQRLMRFC 

       730        740        750        760        770        780 
SVEMGSFYLD IIKDRQYTTK ADSLARRSCQ TALWHIAEAL VRWMAPILSF TADEIWQHLP 

       790        800        810        820        830        840 
QTESARAEFV FTEEFYQGLF GLGEDEKLDD AYWQQLIKVR SEVNRVLEIS RNNKEIGGGL 

       850        860        870        880        890        900 
EAEVTVYAND EYRALLAQLG NELRFVLITS KVDIKSLSEK PADLADSELE GIAVSVTRSN 

       910        920        930        940 
AEKCPRCWHY SDEIGVSPEH PTLCARCVEN VVGNGEVRHF A 

« Hide

References

[1]"Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
Genome Biol. 8:R103.1-R103.18(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PittGG.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000672 Genomic DNA. Translation: ABR00509.1.
RefSeqYP_001292892.1. NC_009567.1.

3D structure databases

ProteinModelPortalA5UIA3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374931.CGSHiGG_08385.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR00509; ABR00509; CGSHiGG_08385.
GeneID5227556.
KEGGhiq:CGSHiGG_08385.
PATRIC20187697. VBIHaeInf102487_1696.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycHINF374931:GJA4-1475-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_HAEIG
AccessionPrimary (citable) accession number: A5UIA3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: May 14, 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