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

P46207 (SYI_AQUPY) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. 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
OrganismAquifex pyrophilus
Taxonomic identifier2714 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length529 AA.
Sequence statusFragment.
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.

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile).

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

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.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
Gene Ontology (GO)
   Biological_processisoleucyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

aminoacyl-tRNA editing activity

Inferred from electronic annotation. Source: InterPro

isoleucine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›529›529Isoleucine--tRNA ligase
PRO_0000098342

Regions

Motif523 – 5275"KMSKS" region

Sites

Binding site4821Aminoacyl-adenylate By similarity
Binding site5261ATP By similarity

Experimental info

Non-terminal residue11
Non-terminal residue5291

Sequences

Sequence LengthMass (Da)Tools
P46207 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: FB6C40D69E26DDD8

FASTA52961,379
        10         20         30         40         50         60 
DTHGLPIERA VEKELSKKKI RKESLPKTEF RKLCREYANR YVNIQKEEFI RLGVLGDWEN 

        70         80         90        100        110        120 
PYLTMSPEYE ATEIRELGKF FEKGLAYRSK KPVYWCIYDK TAEGQAEVEY YEKEDPSIYV 

       130        140        150        160        170        180 
KFPLKKEIEG KKAYAVIWTT TPWTLPANLG IMVKEDADYS LVEVEGEVWI VAKELLENFF 

       190        200        210        220        230        240 
KNIGKTYTRV LKDVKGRDLV GLEYEHPFVD RDELKGYLSE ETLKNMWRIY PSEFVSLDTG 

       250        260        270        280        290        300 
TGLVHMAPGH GQEDYTVGKR YNLEPYAPLD DSGRFVEPAP EFIRGVRVFD ANKLIIALLK 

       310        320        330        340        350        360 
EKGYLVHEAR IRHSYPHCWR CKNPVIFRAT PQWFIGMDIE YEGKTLSGES LEEIEKVKWI 

       370        380        390        400        410        420 
PEYGKNRIKS MVENRPDWCI SRQRFWGVPI TVFYCENCGE VIKDKEVFER IASLVEKHPG 

       430        440        450        460        470        480 
GTDVWFEKSP EEILPEGYKC PKCGGTSFRK EEDILDVWFD SGCSHASVIR PLGFEKADLY 

       490        500        510        520 
LEGSDQHRGW FQASLLESVG SYGEAPYRSV LTHGFIVDEQ GRKMSKSLV 

« Hide

References

[1]"Root of the universal tree of life based on ancient aminoacyl-tRNA synthetase gene duplications."
Brown J.R., Doolittle W.F.
Proc. Natl. Acad. Sci. U.S.A. 92:2441-2445(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L37096 Genomic DNA. Translation: AAA87287.1.
PIRI39658.

3D structure databases

ProteinModelPortalP46207.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP46207.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
InterProIPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF50677. SSF50677. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYI_AQUPY
AccessionPrimary (citable) accession number: P46207
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 79 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