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Q03QI3 (SYI_LACBA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. 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:LVIS_1441
OrganismLactobacillus brevis (strain ATCC 367 / JCM 1170) [Complete proteome] [HAMAP]
Taxonomic identifier387344 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length937 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
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 – 937937Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022081

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif597 – 6015"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8951Zinc By similarity
Metal binding8981Zinc By similarity
Metal binding9151Zinc By similarity
Metal binding9181Zinc By similarity
Binding site5561Aminoacyl-adenylate By similarity
Binding site6001ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q03QI3 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: E4C032D9680F36D3

FASTA937105,621
        10         20         30         40         50         60 
MRVKDTLNLG KTKFKMRGNL PVKEVDRQKA WAENKMYEAR QKLNEGKPTF ILHDGPPYAN 

        70         80         90        100        110        120 
GPIHMGHALN KISKDIIVRY KSMSGFRAPY VPGWDTHGLP IEQQLTKAGY DRKKMSTAEF 

       130        140        150        160        170        180 
RDLCREYALK QVDQQREGFK RLGVSAEWDN PYLTLKPEFE AAEVRVFGEM AKRGLIYKGK 

       190        200        210        220        230        240 
KPVYWSWSSE SAMAEAEVEY HDVTSPSAFY GEQVVDGKGV LDTDTYLVVW TTTPWTIPGS 

       250        260        270        280        290        300 
EGITIDAGIE YAVVKPANDD RKFVLAADLV DQNAEMFGWE DVQVIKTVMG QDLDNVTAQH 

       310        320        330        340        350        360 
PFIADRKLVV MLGDFVTTES GTGLVHTAPG LGEDDFNVGA LYHLPVLVPV DDKGYMTAEA 

       370        380        390        400        410        420 
GADFAGVFYE DANQIALDKL KAANALLKYM PYEHSYPFDW RTKKPVIFRA TPQWFASVDK 

       430        440        450        460        470        480 
IRDEILAQLK DVKFQPDWGQ RRLANMIKDR GDWVISRQRV WGVPLPIFYG EDGEAIITPE 

       490        500        510        520        530        540 
TVDHVADLFA EYGSNIWFKR EAKDLLPDGF TSEHSPNGEF TKETDIMDVW FDSGTSHQGV 

       550        560        570        580        590        600 
LAERDYLDFP ADLYLEGSDQ YRGWFNSSLI TSVAATGKAP YKQVVSQGFT LDKDGHKMSK 

       610        620        630        640        650        660 
SLGNTIAPDE IISKMGADIV RLWVTSVDSS ADVRVSTEAF VKISDSYKKL RNTMRYLLAN 

       670        680        690        700        710        720 
TSDFDPQTDA IAVDDLQPVD RHMLYQLNEF AKSVRAHYDH YDFLNIYKEL INFVVSDLSA 

       730        740        750        760        770        780 
FYLDFAKDIL YIEAADSPVR RSMQTVFYQI AVSLTKLITP ILPHTAEEIW DFLKEPEDFV 

       790        800        810        820        830        840 
QLAEMPAVLE LTDANEQPDD GHQSAWDHFM TLRSHVLKAL EEARDAKLIG KAAEAHLDLY 

       850        860        870        880        890        900 
VDEETKRLLD QLNVNVQQIL LVSGLDVASL DQAPADALTF DHLAVKVTPA AGEVCDRCRL 

       910        920        930 
TKEDVGSDSA YPHFCARCAA IVRQNFPETA TEGFDEN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000416 Genomic DNA. Translation: ABJ64539.1.
RefSeqYP_795570.1. NC_008497.1.

3D structure databases

ProteinModelPortalQ03QI3.
SMRQ03QI3. Positions 1-924.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING387344.LVIS_1441.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ64539; ABJ64539; LVIS_1441.
GeneID4413669.
KEGGlbr:LVIS_1441.
PATRIC22201819. VBILacBre134470_1378.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycLBRE387344:GJ8S-1441-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.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 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_LACBA
AccessionPrimary (citable) accession number: Q03QI3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: May 14, 2014
This is version 60 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