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)

B5Y235

- SYI_KLEP3

UniProt

B5Y235 - SYI_KLEP3

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Klebsiella pneumoniae (strain 342)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 1 (25 Nov 2008)
      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 sitei561 – 5611Aminoacyl-adenylateUniRule annotation
    Binding sitei605 – 6051ATPUniRule annotation
    Metal bindingi901 – 9011ZincUniRule annotation
    Metal bindingi904 – 9041ZincUniRule annotation
    Metal bindingi921 – 9211ZincUniRule annotation
    Metal bindingi924 – 9241ZincUniRule 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

    BioCyciKPNE507522:GI0B-4736-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:KPK_4735
    OrganismiKlebsiella pneumoniae (strain 342)
    Taxonomic identifieri507522 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella
    ProteomesiUP000001734: 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 – 938938Isoleucine--tRNA ligasePRO_1000189173Add
    BLAST

    Proteomic databases

    PRIDEiB5Y235.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi507522.KPK_4735.

    Structurei

    3D structure databases

    ProteinModelPortaliB5Y235.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi58 – 6811"HIGH" regionAdd
    BLAST
    Motifi602 – 6065"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.

    B5Y235-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDYKSTLNL PETGFPMRGD LAKREPGMLA RWTDDDLYGI IRAAKKGKKT    50
    FILHDGPPYA NGSIHIGHSV NKILKDIIVK SKGLTGYDSP YVPGWDCHGL 100
    PIELKVEQQY GKPGEKFTAA EFRSKCREYA AEQIDGQRKD FIRLGVLGDW 150
    SRPYLTMDFK TEANIIRALG KIIGNGHLHK GAKPVHWCVD CRSALAEAEV 200
    EYYDKTSPSI DVAFHAVDKA AVLAKFGVAD VNGPVSLVIW TTTPWTLPAN 250
    RAISLSPEFD YALVQVDGQA LILAKDLVES VMKRVGATDY TILAAVQGSE 300
    LELMRFKHPF LDFDVPAILG DHVTLDAGTG AVHTAGGHGP DDYTISQKYG 350
    LEIANPVGPD GAYLPGTYPS LDGINVFKAN DIIVEMLRDS GALLHVEKMQ 400
    HSYPCCWRHK SPIIFRATPQ WFVSMDQKGL RAQSLKEIKG VQWIPDWGQA 450
    RIESMVANRP DWCISRQRTW GVPMSLFVHK ETHELHPRTL ELMEEVAKRV 500
    EVDGIQAWWD LDSRDILGDD ADSYEKVPDT LDVWFDSGST HSSVVDVRPE 550
    FAGHAADMYL EGSDQHRGWF MSSLMISTAM KGKAPYRQVL THGFTVDGQG 600
    RKMSKSIGNT VSPQDVMNKL GADILRLWVA STDYTGEMAV SDEILKRAAD 650
    SYRRIRNTAR FLLANLNGFD PAKDMVKPEE MVVLDRWAVG CAQAAQEDIL 700
    KAYESYDFHE VVQRLMRFCS IEMGSFYLDI IKDRQYTAKA DSVARRSCQT 750
    ALFHIVEALV RWMAPIMSFT ADEIWGYLPG DREKYVFTGE WYKGLFGLAD 800
    DEAMNDGFWD ELLKVRGEVN KVIEQARADK KVGGSLEAAV TLYADADLAA 850
    KLNALGDELR FVLLTSGANV ADYAQAPADA WQSDLLKGLK VVLSKAEGEK 900
    CPRCWHYTSD VGKVAEHAEI CGRCVSNVAG NGEQRKFA 938
    Length:938
    Mass (Da):104,446
    Last modified:November 25, 2008 - v1
    Checksum:i98AC25E8115A448E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000964 Genomic DNA. Translation: ACI10800.1.
    RefSeqiYP_002240526.1. NC_011283.1.

    Genome annotation databases

    EnsemblBacteriaiACI10800; ACI10800; KPK_4735.
    GeneIDi6935267.
    KEGGikpe:KPK_4735.
    PATRICi20442615. VBIKlePne121904_4649.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000964 Genomic DNA. Translation: ACI10800.1 .
    RefSeqi YP_002240526.1. NC_011283.1.

    3D structure databases

    ProteinModelPortali B5Y235.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 507522.KPK_4735.

    Proteomic databases

    PRIDEi B5Y235.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACI10800 ; ACI10800 ; KPK_4735 .
    GeneIDi 6935267.
    KEGGi kpe:KPK_4735.
    PATRICi 20442615. VBIKlePne121904_4649.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci KPNE507522:GI0B-4736-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 the N2-fixing broad host range endophyte Klebsiella pneumoniae 342 and virulence predictions verified in mice."
      Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H., Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y., Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W., Methe B.A.
      PLoS Genet. 4:E1000141-E1000141(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 342.

    Entry informationi

    Entry nameiSYI_KLEP3
    AccessioniPrimary (citable) accession number: B5Y235
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 46 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