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Q39DM8

- SYI_BURS3

UniProt

Q39DM8 - SYI_BURS3

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Burkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194))
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (22 Nov 2005)
      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 sitei581 – 5811Aminoacyl-adenylateUniRule annotation
    Binding sitei625 – 6251ATPUniRule annotation
    Metal bindingi908 – 9081ZincUniRule annotation
    Metal bindingi911 – 9111ZincUniRule annotation
    Metal bindingi928 – 9281ZincUniRule annotation
    Metal bindingi931 – 9311ZincUniRule 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

    BioCyciBSP269483:GHLS-2731-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:Bcep18194_A5844
    OrganismiBurkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194))
    Taxonomic identifieri482957 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
    ProteomesiUP000002705: 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 – 945945Isoleucine--tRNA ligasePRO_1000022048Add
    BLAST

    Proteomic databases

    PRIDEiQ39DM8.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi269483.Bcep18194_A5844.

    Structurei

    3D structure databases

    ProteinModelPortaliQ39DM8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi66 – 7611"HIGH" regionAdd
    BLAST
    Motifi622 – 6265"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.

    Q39DM8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNKKADSKP QAKYPVNLLD TPFPMRGDLP KREPQWVKEW EERGIYEKIR    50
    AASAGRPKFI LHDGPPYANG DIHLGHAVNK ILKDIVVKSR NMAGFDAPYV 100
    PGWDCHGMPI EIQIEKQFGK SLPAAEVMSK ARAYATEQIE KQKVGFKRLG 150
    VLGDWANPYK TMNFVNEAEE LRALGKIIEK GYVYRGLKPV NWCFDCGSAL 200
    AEAEVEYKDR TDPTIDVMFA FAEPEKTAQA FGLPALPRAE GGIVIWTTTP 250
    WTIPANQALN LHPEIVYALV DTERGLLIIA EERVEACMTD FKLTGRVVAT 300
    APGVKLAGLR FHHPLASAHP GYKRTAPVYL GDYVTTDTGT GVVHSSPAYG 350
    IEDFVSCKAH GMTDSDFINP VMGDGRYIES LPLFGGLSIW DANPKIVEAL 400
    NAAGSLLRSE KYTHSYMHCW RHKTPIIYRA TSQWFAGMDV TPRDGGKTLR 450
    ETALEGVDAT AFYPSWGKQR LFSMIANRPD WTLSRQRQWG VPMAFFVHKE 500
    TGELHPRTLE LLEEVAKRVE QSGIEAWQTL DPRELIGDDA NLYEKNRDTL 550
    DVWFDSGTTH WHVLRGSHKD QLQFPADLYL EGSDQHRGWF HSSLLTASMI 600
    DGRAPYKGLL THGFTVDGEG RKMSKSLGNG IDPHEVANRL GAEIIRLWIA 650
    STDYSGELAI SEEILKRVTE GYRRIRNTLR FLLANLSDFD FAQHAVPVDE 700
    WLEIDRYAVA FSQQLQTELL GHYEKYEFHP VVAKLQTYCS EDLGGFYLDV 750
    LKDRLYTSAA DSRARRSAQT ALYHLTHGLL RVLAPFLSFT AEEAWKVFQP 800
    ASDTIYTETY YAYPEVAGSA ALIEKWALLR DVRGNVTKAL EEARTANRIG 850
    SSLQAEVAVH ASGARYDALT SLGDDLKFVL ITSAATVVKV DDEAQESVDV 900
    AASKYQKCER CWHYREDVGA HADHPTLCGR CFSNLFENGE IRSAA 945
    Length:945
    Mass (Da):105,866
    Last modified:November 22, 2005 - v1
    Checksum:iC6F393E268E23A29
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000151 Genomic DNA. Translation: ABB09438.1.
    RefSeqiWP_011352960.1. NC_007510.1.
    YP_370082.1. NC_007510.1.

    Genome annotation databases

    EnsemblBacteriaiABB09438; ABB09438; Bcep18194_A5844.
    GeneIDi3751075.
    KEGGibur:Bcep18194_A5844.
    PATRICi19289189. VBIBurSp120713_3972.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000151 Genomic DNA. Translation: ABB09438.1 .
    RefSeqi WP_011352960.1. NC_007510.1.
    YP_370082.1. NC_007510.1.

    3D structure databases

    ProteinModelPortali Q39DM8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 269483.Bcep18194_A5844.

    Proteomic databases

    PRIDEi Q39DM8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB09438 ; ABB09438 ; Bcep18194_A5844 .
    GeneIDi 3751075.
    KEGGi bur:Bcep18194_A5844.
    PATRICi 19289189. VBIBurSp120713_3972.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BSP269483:GHLS-2731-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 sequence of chromosome 1 of Burkholderia sp. 383."
      US DOE Joint Genome Institute
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
      Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 383.

    Entry informationi

    Entry nameiSYI_BURS3
    AccessioniPrimary (citable) accession number: Q39DM8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: November 22, 2005
    Last modified: October 1, 2014
    This is version 69 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