Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

C5B7M4

- SYI_EDWI9

UniProt

C5B7M4 - SYI_EDWI9

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Edwardsiella ictaluri (strain 93-146)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 40 (01 Oct 2014)
      Sequence version 1 (28 Jul 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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).UniRule annotation

    Catalytic activityi

    ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile).UniRule annotation

    Cofactori

    Binds 1 zinc ion per subunit.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei572 – 5721Aminoacyl-adenylateUniRule annotation
    Binding sitei616 – 6161ATPUniRule annotation
    Metal bindingi911 – 9111ZincUniRule annotation
    Metal bindingi914 – 9141ZincUniRule annotation
    Metal bindingi931 – 9311ZincUniRule annotation
    Metal bindingi934 – 9341ZincUniRule annotation

    GO - Molecular functioni

    1. aminoacyl-tRNA editing activity Source: InterPro
    2. ATP binding Source: UniProtKB-HAMAP
    3. isoleucine-tRNA ligase activity Source: UniProtKB-HAMAP
    4. zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. isoleucyl-tRNA aminoacylation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciEICT634503:GCMY-674-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isoleucine--tRNA ligaseUniRule annotation (EC:6.1.1.5UniRule annotation)
    Alternative name(s):
    Isoleucyl-tRNA synthetaseUniRule annotation
    Short name:
    IleRSUniRule annotation
    Gene namesi
    Name:ileSUniRule annotation
    Ordered Locus Names:NT01EI_0679
    OrganismiEdwardsiella ictaluri (strain 93-146)
    Taxonomic identifieri634503 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEdwardsiella
    ProteomesiUP000001485: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 948948Isoleucine--tRNA ligasePRO_1000216235Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi634503.NT01EI_0679.

    Structurei

    3D structure databases

    ProteinModelPortaliC5B7M4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi58 – 6811"HIGH" regionAdd
    BLAST
    Motifi613 – 6175"KMSKS" region

    Domaini

    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)).UniRule annotation

    Sequence similaritiesi

    Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0060.
    HOGENOMiHOG000246402.
    KOiK01870.
    OMAiKPVHWCL.
    OrthoDBiEOG644ZM1.

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    3.40.50.620. 2 hits.
    3.90.740.10. 1 hit.
    HAMAPiMF_02002. Ile_tRNA_synth_type1.
    InterProiIPR001412. 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]
    PANTHERiPTHR11946:SF9. PTHR11946:SF9. 1 hit.
    PfamiPF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 1 hit.
    PF06827. zf-FPG_IleRS. 1 hit.
    [Graphical view]
    PRINTSiPR00984. TRNASYNTHILE.
    SUPFAMiSSF47323. SSF47323. 1 hit.
    SSF50677. SSF50677. 1 hit.
    TIGRFAMsiTIGR00392. ileS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    C5B7M4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDYKNTLNL PETGFPMRGD LAKREPGMLQ HWYEQDLYGI IRNAKQGKKS    50
    FILHDGPPYA NGSIHIGHSV NKILKDIIIK SKGLSGYDSP YIPGWDCHGL 100
    PIELKVEQLI GKPGEKYSAA EFREQCRAYA AEQVAGQKAD FIRLGVLGDW 150
    EHPYLTMDYG TEANIIRALA RIVDNGHLMK GAKPVHWCPD CGSSLAEAEV 200
    EYYDKVSPSI DVRFAAVDKA QVLAKFGVSE AKGDVNVVIW TTTPWTLPAN 250
    RAVALHPELE YQLVQVEGEC LILAADLVES VMKRAGIDYW QVLGSCKGEA 300
    LELLHFCHPF MNFDVPIIMG DHVTLDAGTG AVHTAPGHGP DDYVVGQKYG 350
    LEIANPVGSN GCYLPGTHPV LDGLFVFKAN DIVIDLLKDS GALLHVEKLT 400
    HSYPCCWRHK SPIIFRATPQ WFISMDRQGL RSQSLAEIDR IERQGLDEQN 450
    LSGWIPAWGK ARIESMVANR PDWCISRQRT WGVPMAMLVH KETQELHPRT 500
    TELMEMVAKR VEQAGIQAWW DLDIRDLLGD EADQYEKVPD TLDVWFDSGS 550
    TSYSVVDARP EFNGHSPDMY LEGSDQHRGW FMSSLMISVA MKGKAPYRQV 600
    LTHGFTVDGQ GRKMSKSVGN VVSPQQVMNK LGGDILRLWV ASTDYTSEMA 650
    VSDEILKRSA DAYRRIRNTA RFLLANLNGF DPCKDMVKPE DMVVLDRWAV 700
    GCAKQAQDEI IAAYENYDFH EVVQRLMQFC SVEMGSFYLD IIKDRQYTAK 750
    ADSVARRSCQ TALYHIAEAL VRWMAPILSF TADEVWGYLP GDRAQFVFTE 800
    EWYQGLFGLD AAEQMNDAFW AELLKVRGEV NRVIEQARND KKVGGSLEAA 850
    ITLYADEALA TQLDSLQDEL RFVLITSAAR VQPLVQATAD AVASELAGLK 900
    VGLGKADGSK CPRCWHYSTA IGQDAAHPQL CPRCVTNVAG QGEERKFA 948
    Length:948
    Mass (Da):105,791
    Last modified:July 28, 2009 - v1
    Checksum:i2399B079470C2A0C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001600 Genomic DNA. Translation: ACR67901.1.
    RefSeqiYP_002932136.1. NC_012779.2.

    Genome annotation databases

    EnsemblBacteriaiACR67901; ACR67901; NT01EI_0679.
    GeneIDi7962013.
    KEGGieic:NT01EI_0679.
    PATRICi21834582. VBIEdwIct114273_0611.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001600 Genomic DNA. Translation: ACR67901.1 .
    RefSeqi YP_002932136.1. NC_012779.2.

    3D structure databases

    ProteinModelPortali C5B7M4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 634503.NT01EI_0679.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACR67901 ; ACR67901 ; NT01EI_0679 .
    GeneIDi 7962013.
    KEGGi eic:NT01EI_0679.
    PATRICi 21834582. VBIEdwIct114273_0611.

    Phylogenomic databases

    eggNOGi COG0060.
    HOGENOMi HOG000246402.
    KOi K01870.
    OMAi KPVHWCL.
    OrthoDBi EOG644ZM1.

    Enzyme and pathway databases

    BioCyci EICT634503:GCMY-674-MONOMER.

    Family and domain databases

    Gene3Di 1.10.730.10. 1 hit.
    3.40.50.620. 2 hits.
    3.90.740.10. 1 hit.
    HAMAPi MF_02002. Ile_tRNA_synth_type1.
    InterProi IPR001412. 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 ]
    PANTHERi PTHR11946:SF9. PTHR11946:SF9. 1 hit.
    Pfami PF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 1 hit.
    PF06827. zf-FPG_IleRS. 1 hit.
    [Graphical view ]
    PRINTSi PR00984. TRNASYNTHILE.
    SUPFAMi SSF47323. SSF47323. 1 hit.
    SSF50677. SSF50677. 1 hit.
    TIGRFAMsi TIGR00392. ileS. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete genome sequence of Edwardsiella ictaluri 93-146."
      Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C., Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.
      Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 93-146.

    Entry informationi

    Entry nameiSYI_EDWI9
    AccessioniPrimary (citable) accession number: C5B7M4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 40 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3