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A7I1S7 (SYI_CAMHC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 50. 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:CHAB381_0906
OrganismCampylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A) [Complete proteome] [HAMAP]
Taxonomic identifier360107 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length921 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 – 921921Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022055

Regions

Motif59 – 6911"HIGH" region HAMAP-Rule MF_02002
Motif610 – 6145"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8961Zinc By similarity
Metal binding8991Zinc By similarity
Metal binding9111Zinc By similarity
Metal binding9141Zinc By similarity
Binding site5691Aminoacyl-adenylate By similarity
Binding site6131ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A7I1S7 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: FEB0BE766577CAF5

FASTA921106,166
        10         20         30         40         50         60 
MDYKDTLFLP TTDFAMRGNL PQNEPKRFKA WYNERKVYEK MKAKRQSAGV SFNLHDGPPY 

        70         80         90        100        110        120 
ANGHLHIGHA LNKILKDIIV KTHYFAGENV RYVPGWDCHG LPIEQQIEIK LGGKKNETSK 

       130        140        150        160        170        180 
TKIREMCRAH AREFINIQRD EFKDMGIIGD WDDPYITMKF KFEAEIYKGL CEIAKKGLLI 

       190        200        210        220        230        240 
ERSKPVFWSW AAGSALAEAE VEYKDKEDYS IYIAFDLSDE ANKKIGAKGA KAVIWTTTPW 

       250        260        270        280        290        300 
TIPANQAICL NPDEIYVLTS ENFIFAKHLL ENLVQKGISK GKIVKEFASG ELENLYAKNP 

       310        320        330        340        350        360 
LNDRPSKFIL GEHVLMDGGT GLVHTAPGHG EDDYYVSLKY GIETIMPVDD AGKYDETIKT 

       370        380        390        400        410        420 
KKLFRDNVVD EFVGMHIFKA NEKIVELLGD AVVSVGKFTH SYPYCWRTHK PVIYRATKQW 

       430        440        450        460        470        480 
FIAMDKPFKD GKTLREVALN ALKEVKFYPE VGRNRITSMI ENRPDWCISR QRDWGVPIAF 

       490        500        510        520        530        540 
FRDKATKEPI FDDEILNNIY EIFKEKGADA WWELDIGELL PKNCKYEAKN LEKVVDILDV 

       550        560        570        580        590        600 
WFDSGSTWRA VLKSGDYDAG EFRADMYLEG SDQHRGWFQS SLLVSSAINE TAPYKSILTH 

       610        620        630        640        650        660 
GFTVDEKGQK MSKSVGNVIA PQEVAKKYGV EIMRLWVGLS DYSSDLKISD NILKQVSEQY 

       670        680        690        700        710        720 
RKIRNTIRFL LANVSDLKEI ETNNFTMLDK WILSKANIAF EETNRAFRNY DFSKGFSVLL 

       730        740        750        760        770        780 
NFLSADLSGI YLDVCKDRLY CDELDSSRRR SAQSTMVLIT RTLLPLIAPT LTYTVDEVME 

       790        800        810        820        830        840 
FAPEIVKNGK KDAFDLVYEP LEFEDFKKNE TGELFIESRA KFFEIIDTLK KEKKIKSTLE 

       850        860        870        880        890        900 
LVLETSSNEI LSHDLDEICD WYMVSHMRSI ESRDFLAEFK VEDETFRLVL SDHHKCPRCW 

       910        920 
KFDAKNEDEL CPRCQKVLNV K 

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References

[1]"Complete genome sequence of Campylobacter hominis ATCC BAA-381, a commensal isolated from the human gastrointestinal tract."
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Nelson K.E.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000776 Genomic DNA. Translation: ABS51595.1.
RefSeqYP_001406468.1. NC_009714.1.

3D structure databases

ProteinModelPortalA7I1S7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360107.CHAB381_0906.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS51595; ABS51595; CHAB381_0906.
GeneID5409280.
KEGGcha:CHAB381_0906.
PATRIC20039946. VBICamHom81367_0869.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCHOM360107:GHCX-910-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_CAMHC
AccessionPrimary (citable) accession number: A7I1S7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 11, 2007
Last modified: April 16, 2014
This is version 50 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