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Q9AAA5 (SYI_CAUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 80. 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:CC_0701
OrganismCaulobacter crescentus (strain ATCC 19089 / CB15) [Reference proteome] [HAMAP]
Taxonomic identifier190650 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter

Protein attributes

Sequence length969 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

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
Nucleotide-binding
   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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 969969Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098374

Regions

Motif70 – 8011"HIGH" region HAMAP-Rule MF_02002
Motif642 – 6465"KMSKS" region HAMAP-Rule MF_02002

Sites

Binding site6011Aminoacyl-adenylate By similarity
Binding site6451ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9AAA5 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: C7CEE8311F59B174

FASTA969108,637
        10         20         30         40         50         60 
MADDATTARD YRETVFLPDT PFPMRAGLPK KEPEILEGWA ALSEKGLYGA VRQKRQAAGA 

        70         80         90        100        110        120 
PLFVFHDGPP YANGAIHIGH ALNKILKDFV VRSRFALGYD VDYVPGWDCH GLPIEWKIEE 

       130        140        150        160        170        180 
QFRAKGRRKD EVPAEEFRRE CRAYAGGWIE AQKTEFQRLG VLGDWWNRYA TMDFTSEAKI 

       190        200        210        220        230        240 
VEEFHKFLAT GQLYRGSKPV MWSPVERTAL ADAEIEYHDH VSPTIWVKFP VVQGSDAAVG 

       250        260        270        280        290        300 
AKLVIWTTTP WTIPANRAVS YNPDIPYSVF EVTALEEGLE FEPWAKPGDR LIIADKLAED 

       310        320        330        340        350        360 
VFKAAKVASW KTVEAVDCEG MVLAHPLADL DSHYGYAVPM LAGDHVTDDA GTGFVHTAPG 

       370        380        390        400        410        420 
HGADDYQVWL AHGHREIPDT VDPDGAYYPH VALFAGLKVL ETEGKKVGKF GPANGAVMEK 

       430        440        450        460        470        480 
LIEAGNLLAR GRVEHSYPHS WRSKAPVIFR NTPQWFIRMD HAVDSLDGKT LREVAVQAIA 

       490        500        510        520        530        540 
DTAFYPDGGR NRIGAMVETR PDWLISRQRN WGTPLAMFVD KHTGHPLNDP EVNARILAAI 

       550        560        570        580        590        600 
REGGADAWFT RPDADFLGAH DPAQYEKITD ILDVWFDSGC THAFTIEGRA DSAWPADLYL 

       610        620        630        640        650        660 
EGSDQHRGWF QSSLLEGCGT RGRAPYKAVV THGFTMDENG EKMSKSRGNT IEPQTITKES 

       670        680        690        700        710        720 
GAEILRLWTA MVDYQEDQRI GKTILATTTD AYRKLRNTMR YLLGALAGFD EEERVTDYDQ 

       730        740        750        760        770        780 
FPALEKYILH RLWELDGQVR EAYQSYRFSD VIRPLIEFCQ GDLSALYFDV RRDSLYCDRP 

       790        800        810        820        830        840 
DALKRRAYRT ALDYVFDRLT IWLAPLASFT MEEAWTTRFP EAGPVAYRVM PERVDAWRND 

       850        860        870        880        890        900 
AEAARWAKVE KVTSVVTGAL EVERREKRIG SALEAAPVVH FADEDLLAAF EGLDAGEVFR 

       910        920        930        940        950        960 
TSSATLVAGD AGAFRVDEVK GVSVDPNKAE GKKCARSWRI LPEVGTDPRY PELSLRDADA 


VAYWDAGRG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005673 Genomic DNA. Translation: AAK22686.1.
PIRB87336.
RefSeqNP_419518.1. NC_002696.2.

3D structure databases

ProteinModelPortalQ9AAA5.
SMRQ9AAA5. Positions 58-878.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK22686; AAK22686; CC_0701.
GeneID941463.
KEGGccr:CC_0701.
PATRIC21298350. VBICauCre124313_0710.

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycCAULO:CC0701-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_CAUCR
AccessionPrimary (citable) accession number: Q9AAA5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: June 1, 2001
Last modified: June 11, 2014
This is version 80 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