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A5F8Z3

- SYI_VIBC3

UniProt

A5F8Z3 - SYI_VIBC3

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (12 Jun 2007)
      Previous versions | rss
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    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 sitei567 – 5671Aminoacyl-adenylateUniRule annotation
    Binding sitei611 – 6111ATPUniRule annotation
    Metal bindingi912 – 9121ZincUniRule annotation
    Metal bindingi915 – 9151ZincUniRule annotation
    Metal bindingi932 – 9321ZincUniRule annotation
    Metal bindingi935 – 9351ZincUniRule 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

    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:VC0395_A0214, VC395_0699
    OrganismiVibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
    Taxonomic identifieri345073 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000000249: Chromosome 2, UP000001630: Chromosome I

    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 – 949949Isoleucine--tRNA ligasePRO_1000073712Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi345073.VC0395_A0214.

    Structurei

    3D structure databases

    ProteinModelPortaliA5F8Z3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi58 – 6811"HIGH" regionAdd
    BLAST
    Motifi608 – 6125"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.

    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.

    A5F8Z3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEYKDTLNL PETGFPMRGD LAKREPEMLQ RWYQEDLYGA IRQAKKGKKS    50
    FVLHDGPPYA NGDIHIGHAL NKILKDVIIK SKTLSGFDAP YIPGWDCHGL 100
    PIELMVEKKV GKPGQKVTAA EFREKCREYA AGQVEGQKES FKRLGILGEW 150
    DKPYRTMDFV TEANIIRALG KIADNGHLLK GFKPVHWCTD CGSALAEAEV 200
    EYKNKVSPSI DVRFKAADEA AVLAKFGLAA GHEGKGDVSI VIWTTTPWTL 250
    PANRAVCLRA DLEYVLIQVE GEQPERIIVA SELAKSVMDR AGIEHFHNLG 300
    FATGADLELV QFQHPFYSFT VPAILGDHVT TDSGTGVVHT APGHGQEDFA 350
    VGQQYGLEVA NPVGSNGVYL PDTELFAGQH VFKANDSVLE VLKEKGALLH 400
    HHAYEHSYPH CWRHKTPIIF RATPQWFVSM EQAGLREQAL TAIKGVHWMP 450
    DWGQSRIEGM VAGRPEWCIS RQRTWGVPIA LFVHKETAEL HPNSADLIEK 500
    VAQLVEQKGI QAWWDLDTAE LLGAEDAANY EKVLDTLDVW FDSGVTHSAV 550
    VDARQEFNGA EADMYLEGSD QHRGWFQSSL ISSVAMKSKA PYKEVLTHGF 600
    VVDGQGRKMS KSIGNVVAPQ DVTNKLGADI LRLWVASTDY TGEVAVSDEI 650
    LKRSADAYRR IRNTARFFLA NLNGFNPTTD IIPVEDMVAL DRWAVGRALA 700
    AQQEIIQAYQ DYNLHAVVQR LMNFCSIEMG SFYLDVIKDR QYTAKRGGHA 750
    QRSCQTALFF IVEALVRWMA PIMSFTADEI WNAMPAQQAD GSARDKFVFT 800
    TEWFDGLFGL AEGEELNNAF WNDIQKVRGS VNKLLENARN EKLIGGSLQA 850
    ELVLFADDAL ASKLAKLGDE LRFVLLTSKA VVKPLAEKSE AAQATDIDGL 900
    FVQVNKTEAE KCDRCWHHTP DVGTIAGHTT ICGRCVSNVE GEGEVRKFA 949
    Length:949
    Mass (Da):105,413
    Last modified:June 12, 2007 - v1
    Checksum:i5B4212359E2AD71A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000627 Genomic DNA. Translation: ABQ21661.1.
    CP001235 Genomic DNA. Translation: ACP08717.1.
    RefSeqiYP_001216177.1. NC_009457.1.
    YP_002818953.1. NC_012582.1.

    Genome annotation databases

    EnsemblBacteriaiABQ21661; ABQ21661; VC0395_A0214.
    ACP08717; ACP08717; VC395_0699.
    GeneIDi5137625.
    7774718.
    KEGGivco:VC0395_A0214.
    vcr:VC395_0699.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000627 Genomic DNA. Translation: ABQ21661.1 .
    CP001235 Genomic DNA. Translation: ACP08717.1 .
    RefSeqi YP_001216177.1. NC_009457.1.
    YP_002818953.1. NC_012582.1.

    3D structure databases

    ProteinModelPortali A5F8Z3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 345073.VC0395_A0214.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ21661 ; ABQ21661 ; VC0395_A0214 .
    ACP08717 ; ACP08717 ; VC395_0699 .
    GeneIDi 5137625.
    7774718.
    KEGGi vco:VC0395_A0214.
    vcr:VC395_0699.

    Phylogenomic databases

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

    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. Heidelberg J.
      Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 39541 / Classical Ogawa 395 / O395.
    2. "A recalibrated molecular clock and independent origins for the cholera pandemic clones."
      Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
      PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 39541 / Classical Ogawa 395 / O395.

    Entry informationi

    Entry nameiSYI_VIBC3
    AccessioniPrimary (citable) accession number: A5F8Z3
    Secondary accession number(s): C3LXZ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: June 12, 2007
    Last modified: October 1, 2014
    This is version 54 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

    Documents

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

    External Data

    Dasty 3