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Q2S9T9 (SYI_HAHCH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 67. 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:HCH_05933
OrganismHahella chejuensis (strain KCTC 2396) [Complete proteome] [HAMAP]
Taxonomic identifier349521 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHahellaceaeHahella

Protein attributes

Sequence length941 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 – 941941Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022075

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif605 – 6095"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9041Zinc By similarity
Metal binding9071Zinc By similarity
Metal binding9241Zinc By similarity
Metal binding9271Zinc By similarity
Binding site5641Aminoacyl-adenylate By similarity
Binding site6081ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2S9T9 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 2C175D4B31DA6BFB

FASTA941106,642
        10         20         30         40         50         60 
MSDYKHTLNL PQTDFPMRGN LPQREPDMLK RWGDIELYEK IREEFKGREK FILHDGPPYA 

        70         80         90        100        110        120 
NGNIHLGHAV NKILKDIIVK SKTVAGYDAP YVPGWDCHGL PIEHKVETMI GRAGDKVGYK 

       130        140        150        160        170        180 
EFRRKCREYA LEQVAKQRED FIRLGVFGDW FKPYLTLDFK TEADIIRALG KIATSGHLQK 

       190        200        210        220        230        240 
GYKPVYWSVV GGSALAEAEV EYKDKTSNSI DVSYPAENEQ DLLSAFADAS GEGAVSIVIW 

       250        260        270        280        290        300 
TTTPWTLPAS LAVSLGAEID YALTQCSVDG RPQRWIVAEK MLESVMARCG VEDYQVVGRC 

       310        320        330        340        350        360 
TGQDLEGKTF LHPFYKRSIP ALLGDHVTLD AGTGVVHTAP DHGMEDFAVC NKYGIETINP 

       370        380        390        400        410        420 
LDDRGVYRDN VELFAGEHVY KVDDHVIEVL KERGRLLSHG KITHSYAHCW RTKTPLIYRA 

       430        440        450        460        470        480 
TPQWFISMDK QGLRDQALAE IKLVRWVPSW GQNRIEAMIE QSPDWCISRQ RTWGVPIAFF 

       490        500        510        520        530        540 
VHKETQELHP DTARLVEEVA KQVEKTGIDA WWDINAEDLL GADAQNYEKV TDTLDVWFDS 

       550        560        570        580        590        600 
GVTHSAVLEQ REELGQFPAD LYLEGSDQHR GWFQSSLKTA VAIKGKAPYR QVLTHGFTVD 

       610        620        630        640        650        660 
EKGHKMSKSL GNGIEPQEVM NKLGADILRL WVAATDYSAE MVLSKNILER TADSYRRIRN 

       670        680        690        700        710        720 
TSRFLLANIN DFDPVKDMVA MDDLLALDRW IVDRAWLLQE ELKKAYEQYN FVQVYQKVHN 

       730        740        750        760        770        780 
FCSVELGSFY LDVIKDRQYT MKLDSLGCRS AQTAQYHVIE ALVRWIAPIL SFTAEEIWSY 

       790        800        810        820        830        840 
IPGQRAESIF LETFYEGLQP LAEGSEMGRD YWSRLLRVRT SVNKALEEAR NAGKVKGSLT 

       850        860        870        880        890        900 
TEVSLFATPE MQHDLNALGE ELRFVFITSG ASVFGVEDAS ESNSVATETE GLRVGIRSSE 

       910        920        930        940 
HKKCGRCWHH REDVGAHGSH EDLCGRCIEN IDGSGEERKY A 

« Hide

References

[1]"Genomic blueprint of Hahella chejuensis, a marine microbe producing an algicidal agent."
Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., Oh T.K., Kim J.F.
Nucleic Acids Res. 33:7066-7073(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KCTC 2396.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000155 Genomic DNA. Translation: ABC32585.1.
RefSeqYP_437010.1. NC_007645.1.

3D structure databases

ProteinModelPortalQ2S9T9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349521.HCH_05933.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC32585; ABC32585; HCH_05933.
GeneID3842782.
KEGGhch:HCH_05933.
PATRIC22092096. VBIHahChe29232_5388.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycHCHE349521:GHAL-5730-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_HAHCH
AccessionPrimary (citable) accession number: Q2S9T9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 24, 2006
Last modified: June 11, 2014
This is version 67 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