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Q30ZF7 (SYI_DESDG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 68. 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:Dde_2142
OrganismDesulfovibrio desulfuricans (strain G20) [Complete proteome] [HAMAP]
Taxonomic identifier207559 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length934 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 – 934934Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000070885

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif606 – 6105"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9051Zinc By similarity
Metal binding9081Zinc By similarity
Metal binding9251Zinc By similarity
Metal binding9281Zinc By similarity
Binding site5651Aminoacyl-adenylate By similarity
Binding site6091ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q30ZF7 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 09591B35E2AE7F5F

FASTA934105,351
        10         20         30         40         50         60 
MSDYKKTLHL PVTKFPMKAN LTQKEPEMLK RWEQTDAYRI MYSTGATKEP FVLHDGPPYA 

        70         80         90        100        110        120 
NGNIHLGHAL NKIIKDIIIK SRNMQGHPSQ YVPGWDCHGL PIEHKVEQQL GEKKKTLPAH 

       130        140        150        160        170        180 
AVRRECRKYA TKYLDIQRKE FKRLGVMGQW DNPYLTMTPA YEAATARELV RFMEKGSVVR 

       190        200        210        220        230        240 
SKKPIYWCCS CETALAEAEV EYHDHTSPSI FVRFPMPDAR VAEILGTDPA STSIVIWTTT 

       250        260        270        280        290        300 
PWTIPDNMAV AVHPEFEYAV VKNDGQHYVL AAELAASCAE TFGWENPQTV RTVTGAALEG 

       310        320        330        340        350        360 
LVARHPIYNR ESPVVLADYV TLDSGTGCVH TAPGHGREDY ETGLRYGLEI YSPMNDEGRF 

       370        380        390        400        410        420 
LDSVEFFAGL NVFEANPKVI EKLAELGNLL AQAKIKHSYP HCWRCKQPVI FRATTQWFIS 

       430        440        450        460        470        480 
MEANGLREKA LKAIRNDVDW IPAWGEERIY SMVENRPDWC ISRQRLWGVP IIALLCESCD 

       490        500        510        520        530        540 
EAWYDTEWAA GIVEKFANHP TGCDYWFETD LSQIVPEGLV CPKCGGTHWA KVKDILDVWF 

       550        560        570        580        590        600 
DSGTSFAAVV EQREECSFPA DMYLEGSDQH RGWFHSSLLA SVGTRGIPPY KAVLTHGYVV 

       610        620        630        640        650        660 
DGEGRKMSKS IGNGIAPQEI IDKYGAEILR MWVSSADYRE DVRISEEILS RLVDAYRRIR 

       670        680        690        700        710        720 
NTCRYLLGNL SDLSAADLLP VGQLESLDRF ALDIAMRAHK RVQAAYNDYE FHKVYHTLHN 

       730        740        750        760        770        780 
LCVSDLSAFY LDILKDRLYS SKADSKERRS AQTAVYHILM LLIRDMAPVL SFTAEEVYSY 

       790        800        810        820        830        840 
IPEALRPEAV TVFALREDDI PPMEMPAAER EDWEAFLAVR AEVTKAMEPV RKSGEIGHPL 

       850        860        870        880        890        900 
DAHVTLFMDD ALAAKLKATG ADLRACFIVS KVTVAPLAQA PEQAYTSEEL NGLRISIAKA 

       910        920        930 
PGQKCERCWI WSEELGSSSE HPSLCPRCTG VLCA 

« Hide

References

[1]"Complete genome sequence and updated annotation of Desulfovibrio alaskensis G20."
Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L., Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S., Nolan M. expand/collapse author list , Lapidus A.L., Palumbo A.V., Wall J.D.
J. Bacteriol. 193:4268-4269(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G20.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000112 Genomic DNA. Translation: ABB38939.1.
RefSeqYP_388634.1. NC_007519.1.

3D structure databases

ProteinModelPortalQ30ZF7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING207559.Dde_2142.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB38939; ABB38939; Dde_2142.
GeneID3757151.
KEGGdde:Dde_2142.
PATRIC21743215. VBIDesDes50040_2117.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycDALA207559:GH1L-1916-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_DESDG
AccessionPrimary (citable) accession number: Q30ZF7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 6, 2005
Last modified: April 16, 2014
This is version 68 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