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

Q3ZY20 (SYI_DEHMC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. 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:cbdbA1012
OrganismDehalococcoides mccartyi (strain CBDB1) [Complete proteome] [HAMAP]
Taxonomic identifier255470 [NCBI]
Taxonomic lineageBacteriaChloroflexiDehalococcoidiaDehalococcoidalesDehalococcoidaceaeDehalococcoides

Protein attributes

Sequence length1014 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 – 10141014Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098541

Regions

Motif48 – 5811"HIGH" region HAMAP-Rule MF_02003
Motif628 – 6325"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6311ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3ZY20 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: FAC5A5AA9D9830A7

FASTA1,014116,166
        10         20         30         40         50         60 
MFKAVNPRQN FPQMEEEILK IWQDKGIFKK SIENRRDGKR FTLYEGPPTA NGRPGIHHVL 

        70         80         90        100        110        120 
SRVFKDVIPR YKVMKGYYAP RIGGWDTHGL PVELEVEKEL GFTSKNDIEK YGIAEFNTRC 

       130        140        150        160        170        180 
RSSVFKYVSE WNKLTERIAY WVDLDNAYIT MDNKYIESGW WALKQMWDKG LVYQGHRVTP 

       190        200        210        220        230        240 
HCPRCGTSLS SHEVAQGYKD NTEDPSVFVK FEINHESLAQ TGLGQKWVNP SDKPLYLLAW 

       250        260        270        280        290        300 
TTTPWTLPAN TALAVSATDE YAILDMADYY MVLAKPRLSS LKLTENPIVG ECLGSDLKGL 

       310        320        330        340        350        360 
TYKPLFDPRE FGISVKNMQD NSEIDALEPL SYPVITTSYV SMDDGTGIVH TAPAYGELDY 

       370        380        390        400        410        420 
ESGVKYGLKF VHHVDLQGRI TGNYPFAGKF VKEADKDISR NLKERGLMFR NERMHHTYPF 

       430        440        450        460        470        480 
CWRCDSPLIY YAKQSWYIRT TAVRDELIKG NQQINWYPEH IKDGRFGDWL ENNIDWAFSR 

       490        500        510        520        530        540 
ERYWGTPVPI WRCEKCGQTE CVGGIDELKA KPNFKGMQEK LDIHRPYADE WTYDCAKCGG 

       550        560        570        580        590        600 
NMKRVTEVMD CWYDSGAMPV AQYHYPFEPE SRTIASDGRF PADYICEAVD QTRGWFYSLH 

       610        620        630        640        650        660 
AISTLIFGRP CYQNVICLGH ILDERGEKMS KSKNNVIQPA AVLDKYGADA VRWYFYTAAP 

       670        680        690        700        710        720 
PGNARRFSEK LVGEVTRQFL LMLWNIYSFF VTYANIDNFT PSEKYLAGEV PELDRWILSE 

       730        740        750        760        770        780 
LNQLVLDVDK GLDNYDPTQA GRRIEDFVGY LSNWYVRRSR RRFWKSENDA DKLSAYQALY 

       790        800        810        820        830        840 
TCLVTLSKLL APFTPFVAEE LYQNLVLLVD QSALESVHLT DFPVADKALI DEQLDNEIRL 

       850        860        870        880        890        900 
VMKVSSMGRS ARSKAALKVR QPLAEVRVVL SSPAERTGLM RLAEQVLEEL NVKALVAEEP 

       910        920        930        940        950        960 
GTAIPQENYV ASTEGAYTVA VYTGLSPELL AEGSAREIVH RLQTMRKSAE FEIADYINTH 

       970        980        990       1000       1010 
YQADEYLESV IRTHAEYIKK ETLSNQIVNG NAPEGAYTES LDIDGHPLSL WVVR 

« Hide

References

[1]"Genome sequence of the chlorinated compound-respiring bacterium Dehalococcoides species strain CBDB1."
Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.
Nat. Biotechnol. 23:1269-1273(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CBDB1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ965256 Genomic DNA. Translation: CAI83123.1.
RefSeqYP_308039.1. NC_007356.1.

3D structure databases

ProteinModelPortalQ3ZY20.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING255470.cbdb_A1012.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI83123; CAI83123; cbdbA1012.
GeneID3623543.
KEGGdeh:cbdb_A1012.
PATRIC21612063. VBIDehSp125902_0851.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAKWIISEI.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycDSP255470:GJXW-878-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.
InterProIPR002300. 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. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYI_DEHMC
AccessionPrimary (citable) accession number: Q3ZY20
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: September 27, 2005
Last modified: May 14, 2014
This is version 63 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