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P56456 (SYI_HELPY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:HP_1422
OrganismHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]
Taxonomic identifier85962 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length920 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
Reference 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 – 920920Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098398

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif610 – 6145"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8951Zinc By similarity
Metal binding8981Zinc By similarity
Metal binding9101Zinc By similarity
Metal binding9131Zinc By similarity
Binding site5691Aminoacyl-adenylate By similarity
Binding site6131ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P56456 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: E6AFE8C21D84C69A

FASTA920106,079
        10         20         30         40         50         60 
MEEYKDTLNL NTTTFSMKGN LSVNEPKTYA KWQEQQAFKR MQARKDNHGD FTLHDGPPYA 

        70         80         90        100        110        120 
NGHLHLGHAL NKILKDIVVK REYFKGKKIY YTPGWDCHGL PIEQQILERL EKEKTSLENP 

       130        140        150        160        170        180 
TLFREKCRDH AKKFLEIQKN EFLQLGVLGD FEDPYKTMDF KFEASIYRAL VEVAKKGLLK 

       190        200        210        220        230        240 
ERHKPIYWSY ACESALAEAE VEYKMKKSPS IFVAFGLKKE SLEKLKVKKA SLVIWTTTPW 

       250        260        270        280        290        300 
TLYANVAIAL KKDAVYALTQ KGYLVAKALH EKLAALGVVD NEITHEFNSN DLEYLVATNP 

       310        320        330        340        350        360 
LNQRDSLVAL GEHVGLEDGT GAVHTAPGHG EEDYYLGLRY NLEVLMSVDE KGCYDEGIIH 

       370        380        390        400        410        420 
NQLLDESYLG EHVFKAQKRI IEQLGDSLLL EQEIEHSYPH CWRTHKPVIY RATTQWFILM 

       430        440        450        460        470        480 
DEPFIQNDGS QKTLREVALD AIEKVEFVPS SGKNRLKTMI ENRPDWCLSR QRKWGVPLAF 

       490        500        510        520        530        540 
FIDKRTNKPC FESEVLEHVA NLFEKKGCDV WWEYSVKDLL PPSYQEDAKH YEKIMHILDV 

       550        560        570        580        590        600 
WFDSGSTFKA VLEDYHGEKG QSPSDVILEG SDQHRGWFQS SLLIGCVLNN QAPFKKVITH 

       610        620        630        640        650        660 
GFIVDEKGEK MSKSKGNVVS LDKLLKTHGS DVVRLWVAFN DYQNDLRVSQ TFFTQTEQHY 

       670        680        690        700        710        720 
KKFRNTLKFL LANFSDMDLK NLERPHNFSP LDHFMLETLE TISAGVNSAF EEHDFVKGLN 

       730        740        750        760        770        780 
ILMAFVTNEL SGIYLDACKD SLYCDSKNNE KRQAIQMVLL ATASKLCYFL APILTHTIEE 

       790        800        810        820        830        840 
VLEHSQALRI FLQAKDVFDL KDISVSEKLH LKEFKKPENF EAVLALRSAF NEELDRLKKE 

       850        860        870        880        890        900 
GVIKNSLECA IEVKEKALDE NLVEELLMVS FVGIAKEKLS ETPAFTLFKA PFYKCPRCWR 

       910        920 
FKSELENTPC KRCEQVLKER 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000511 Genomic DNA. Translation: AAD08464.1.
PIRF64697.
RefSeqNP_208213.1. NC_000915.1.

3D structure databases

ProteinModelPortalP56456.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-3571N.
IntActP56456. 3 interactions.
MINTMINT-187219.
STRING85962.HP1422.

Proteomic databases

PRIDEP56456.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD08464; AAD08464; HP_1422.
GeneID899873.
KEGGhpy:HP1422.
PATRIC20594243. VBIHelPyl33062_1491.

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAERLMLHQ.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycHPY:HP1422-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_HELPY
AccessionPrimary (citable) accession number: P56456
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: May 14, 2014
This is version 97 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

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries