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A7GX26 (SYI_CAMC5) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 49. 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:Ccur92_04640
ORF Names:CCV52592_0977
OrganismCampylobacter curvus (strain 525.92) [Complete proteome] [HAMAP]
Taxonomic identifier360105 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length919 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 – 919919Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022053

Regions

Motif59 – 6911"HIGH" region HAMAP-Rule MF_02002
Motif611 – 6155"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8931Zinc By similarity
Metal binding8961Zinc By similarity
Metal binding9081Zinc By similarity
Metal binding9111Zinc By similarity
Binding site5701Aminoacyl-adenylate By similarity
Binding site6141ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A7GX26 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: C211CC0ADD97716E

FASTA919104,842
        10         20         30         40         50         60 
MDYKDTLLLP ATDFPMRGDL PKNEPIRLKS WYEERKIYEK MKSKRAGAAK NFAIHDGPPY 

        70         80         90        100        110        120 
ANGHLHIGHA LNKILKDIIT KTHYFFGENV RYVPGWDCHG LPIEQQVEVK LGDKKKELSK 

       130        140        150        160        170        180 
TQIRELCRAH AREFIDIQRE EFKALGIIGD FENPYMTMKF EFEADIYRSL CEIAKKGLLI 

       190        200        210        220        230        240 
ERSKPVYWSW AAKSALAEAE VEYEDKEDYS IYVAFELDSD ALAKLGVKLA KAVIWTTTPW 

       250        260        270        280        290        300 
TLPANQAISL KPDEIYVLTS ENLIFAKPLL ESLVNLGLTK GEILKEFVSN ELENTHAINP 

       310        320        330        340        350        360 
LNDRKSRFLL GDHVLMDGGT GLVHTAPGHG EDDYYICLRY GFKEILMPVD DGGLYDETLK 

       370        380        390        400        410        420 
AHSLLRADVV DSFVGMHIFK ANEKIIELLG ENLLHVSKFT HSYPFCWRTH KPVIYRATKQ 

       430        440        450        460        470        480 
WFIAMDEPKL GGKTLREVAR GELENVKFYP SVGIKRIGSM IENRPDWCIS RQRDWGVPIA 

       490        500        510        520        530        540 
FFRRKDTKEP IFEPKILEHI AKIFEQKGAD AWWDMSVEEL LAPDSGFEAK NLEKVMDILD 

       550        560        570        580        590        600 
VWFDSGSTWH AVLNSKNYDA GSYPADMYLE GSDQHRGWFQ SSLLVSTAIN SHAPYKNILT 

       610        620        630        640        650        660 
HGFTVDENGQ KMSKSKGNVV APQDVAKSYG VEILRLWVGL SDYSSDLKIS ENILKQVSEQ 

       670        680        690        700        710        720 
YRKIRNTIRF LLANVNDLET IGTDFGFLDQ WILGRAKRVF DEASKCFRAY DFSKGFNLLL 

       730        740        750        760        770        780 
NFLSADLSGI YLDICKDRLY CDAKDSPRRR SAQSAMAIIT KSLLPLIAPT LTYTVDEVMD 

       790        800        810        820        830        840 
YAPAIIKGDA KDAFDLVYEP INFDFDVEDE LLFASREKFF ELIDALKKDK KIKSTLELVL 

       850        860        870        880        890        900 
ETTSSKILDY DSVERADIYM VSDVHRYSGN EGLGEFEIDG EKFKIVLSDA SKCPRCWKFN 

       910 
AIIDGSTCER CSEVLNSVC 

« Hide

References

[1]"Genome sequence of Campylobacter curvus 525.92 isolated from human feces."
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 525.92.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000767 Genomic DNA. Translation: EAT99831.1.
RefSeqYP_001407768.1. NC_009715.1.

3D structure databases

ProteinModelPortalA7GX26.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360105.CCV52592_0977.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEAT99831; EAT99831; CCV52592_0977.
GeneID5406413.
KEGGccv:CCV52592_0977.
PATRIC20031348. VBICamCur47627_0493.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCCUR360105:GJ9P-505-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.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 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_CAMC5
AccessionPrimary (citable) accession number: A7GX26
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 11, 2007
Last modified: April 16, 2014
This is version 49 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