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)

B7VJ87

- SYI_VIBSL

UniProt

B7VJ87 - SYI_VIBSL

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Vibrio splendidus (strain LGP32) (Vibrio splendidus (strain Mel32))
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 44 (01 Oct 2014)
      Sequence version 1 (10 Feb 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 sitei576 – 5761Aminoacyl-adenylateUniRule annotation
    Binding sitei620 – 6201ATPUniRule annotation
    Metal bindingi915 – 9151ZincUniRule annotation
    Metal bindingi918 – 9181ZincUniRule annotation
    Metal bindingi935 – 9351ZincUniRule annotation
    Metal bindingi938 – 9381ZincUniRule 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

    BioCyciVSPL575788:GH64-517-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:VS_0536
    OrganismiVibrio splendidus (strain LGP32) (Vibrio splendidus (strain Mel32))
    Taxonomic identifieri575788 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000009100: Chromosome 1

    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 – 952952Isoleucine--tRNA ligasePRO_1000189215Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi575788.VS_0536.

    Structurei

    3D structure databases

    ProteinModelPortaliB7VJ87.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi58 – 6811"HIGH" regionAdd
    BLAST
    Motifi617 – 6215"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.

    B7VJ87-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDYKDTLNL PETGFPMRGN LANREPEMLK RWYKEDLYGE IRKAKKGKKS    50
    FVLHDGPPYA NGDIHIGHAL NKILKDIIIK SKTLSGFDAP YIPGWDCHGL 100
    PIELMVEKKK GKPGQKISAA EFREECRKYA AGQVEGQKES FKRLGIMGEW 150
    DKPYRTMDFG TEANIIRSLG KIADKGHLLK GFKPVHWCTD CGSALAEAEV 200
    EYKDKVSPSI DVKFTAADEA ALLEKFTLAE GHAGQGEISI VIWTTTPWTL 250
    PANRAVCLRD DLEYVLIQVE ANGDQPAQRI VVASELAKDV MDRAGIEHFH 300
    NLGFATGADL ELSQFNHPFY NFTVPAVLGD HVTTDSGTGV VHTAPGHGQE 350
    DFVVGKKYNL EIANPVGSNG VYLPDTELFA GQHVFKANDS VLEVLKEKGA 400
    LLHHHAYEHS YPHCWRHKTP IIFRATPQWF ISMDQAGLRA KALESTKSVE 450
    WMPEWGQSRI EGMIEGRPEW CISRQRTWGV PIALFVHKET SELHPDSPAL 500
    IEKVAKLVEE KGIQAWWDVD AAELMGAEDA DKYEKVLDTL DVWFDSGVTH 550
    FSVVDSREEY NFPNEERTHS ADLYLEGSDQ HRGWFQSSLI SSIAMKDEAP 600
    YKQVLTHGFV VDGNGRKMSK SIGNVVAPKD VTNKLGADIL RLWVASTDYT 650
    NEVAVSDEIL KRSADAYRRI RNTARFFLAN LNGFNPETDL VPAEEMVALD 700
    RWAVGRAQAA QEEIVKAYGE YNTHGVTQRL MQFCSIEMGS FYLDVIKDRQ 750
    YTAKQGSHAQ RSCQTALYYI VEALVRWMAP IMSFTADEIW NEMPGERDTF 800
    VFTGEWFEGL FGLADDEELS NEFWTEIQSV RGAVNKLLED ARKEKTIGGA 850
    LQAEVTLYAD DALAAKINKL EDELRFVLIT SAAVVKPLSD KSDTAQATDV 900
    EGLYVEVAAT EAEKCDRCWH HTPDVGTIEG HEKICGRCVS NIDGEGEVRK 950
    FA 952
    Length:952
    Mass (Da):106,624
    Last modified:February 10, 2009 - v1
    Checksum:i845A0CA06B4F3C80
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FM954972 Genomic DNA. Translation: CAV17541.1.
    RefSeqiWP_012603276.1. NC_011753.2.
    YP_002416191.1. NC_011753.2.

    Genome annotation databases

    EnsemblBacteriaiCAV17541; CAV17541; VS_0536.
    GeneIDi7160168.
    KEGGivsp:VS_0536.
    PATRICi20151772. VBIVibSpl48387_1900.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FM954972 Genomic DNA. Translation: CAV17541.1 .
    RefSeqi WP_012603276.1. NC_011753.2.
    YP_002416191.1. NC_011753.2.

    3D structure databases

    ProteinModelPortali B7VJ87.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 575788.VS_0536.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAV17541 ; CAV17541 ; VS_0536 .
    GeneIDi 7160168.
    KEGGi vsp:VS_0536.
    PATRICi 20151772. VBIVibSpl48387_1900.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci VSPL575788:GH64-517-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. "Vibrio splendidus str. LGP32 complete genome."
      Mazel D., Le Roux F.
      Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LGP32.

    Entry informationi

    Entry nameiSYI_VIBSL
    AccessioniPrimary (citable) accession number: B7VJ87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 44 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