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Q9PL20 (SYI_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 90. 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:TC_0288
OrganismChlamydia muridarum (strain MoPn / Nigg) [Complete proteome] [HAMAP]
Taxonomic identifier243161 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length1036 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_02003

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003

Cofactor

Zinc By similarity. HAMAP-Rule MF_02003

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02003

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02003.

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_02003

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 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 – 10361036Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098527

Regions

Motif46 – 5611"HIGH" region HAMAP-Rule MF_02003
Motif589 – 5935"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site5921ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PL20 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 69E6B05FD54D5E8D

FASTA1,036118,950
        10         20         30         40         50         60 
MDNEDKVSFP AKEEKVLTFW KEQNIFQKTL ENRDGSPTFS FYDGPPFATG LPHYGHLLAG 

        70         80         90        100        110        120 
TIKDVVCRYA TMDGHYVPRR FGWDCHGVPV EYEVEKSLGL TEPGAIDRFG IANFNEECRK 

       130        140        150        160        170        180 
IVFRYVDEWK YFVDRIGRWV DFSATWKTMD LSFMESVWWV FHSLYKQGLV YEGTKVVPFS 

       190        200        210        220        230        240 
TKLGTPLSNF EAGQNYKEVD DPSVVAKFAL QDDQGILLAW TTTPWTLVSN MALAVHPGLT 

       250        260        270        280        290        300 
YVRIQDKESG EEYILGQESL ARWFPDRESY KWIGQLSGES LVGRRYCPLF PYFQDQQDRG 

       310        320        330        340        350        360 
AFRVIPADFI EESEGTGVVH MAPAFGEADF FACQEHNVPL VCPVDNQGCF TSEVTDFVGE 

       370        380        390        400        410        420 
YIKFADKGIA RRLKNENKLF YQGTIRHRYP FCWRTDSPLI YKAVNSWFVS VEKVKHKMLK 

       430        440        450        460        470        480 
ANESIHWTPG HIKHGRFGKW LEGARDWAIS RNRYWGTPIP IWRSEDGELL VIRSIQELEE 

       490        500        510        520        530        540 
LSGQKIVDLH RHFIDEIVIH KNGKSFHRIP YVFDCWFDSG AMPYAQNHYP FERAEETEAR 

       550        560        570        580        590        600 
FPADFIAEGL DQTRGWFYTL TVIAAALFDQ PAFKNVIVNG IVLAEDGNKM SKRLNNYPSP 

       610        620        630        640        650        660 
KKIMDTYGAD ALRLYLLNSV VVKAEDLRFS DKGVEAVLKQ VLLPLSNALA FYKTYAELYG 

       670        680        690        700        710        720 
FSPNETTDLE LAEIDRWILS SLYSLVGKTR ENMAQYDLHA AVSPFIDFIE DLTNWYIRRS 

       730        740        750        760        770        780 
RRRFWESEDS PDRRAAFATL YEVLMVFSKI IAPFIPFTAE DMYQQLRVET DPESVHLCDF 

       790        800        810        820        830        840 
PHVVLEKILP DLEKKMQDIR EIVALGHSLR KEHKLKVRQP LQHMYIVGAK ERMAALAQVD 

       850        860        870        880        890        900 
SLIGEELNVK EVHFCSETPE YVTTLVKPNF RSLGKRVGNR LPEIQKALAG LSQEQIQAFM 

       910        920        930        940        950        960 
HNGFMVLSLG EETISLNEED ITVSWEAAPG FVARSSASFV AILDCQLTSP LIMEGIAREI 

       970        980        990       1000       1010       1020 
VNKINTMRRN GKLHVSDRIA IRLHAPKIVQ EAFSQYEEYI CEETLTTSVS FIDDKEGEEW 

      1030 
DVNGHAVSLS LEVIGH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002160 Genomic DNA. Translation: AAF39156.1.
PIRF81719.
RefSeqNP_296667.1. NC_002620.2.

3D structure databases

ProteinModelPortalQ9PL20.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243161.TC0288.

Proteomic databases

PRIDEQ9PL20.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF39156; AAF39156; TC_0288.
GeneID1246458.
KEGGcmu:TC_0288.
PATRIC20371978. VBIChlMur19118_0315.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAKESHFDE.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycCMUR243161:GHYU-302-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02003. Ile_tRNA_synth_type2.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
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]
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_CHLMU
AccessionPrimary (citable) accession number: Q9PL20
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 90 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