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)

B2T6I7

- SYI_BURPP

UniProt

B2T6I7 - SYI_BURPP

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Burkholderia phytofirmans (strain DSM 17436 / PsJN)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 50 (01 Oct 2014)
      Sequence version 1 (01 Jul 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 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

    BioCyciBPHY398527:GJEX-3204-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:Bphyt_3159
    OrganismiBurkholderia phytofirmans (strain DSM 17436 / PsJN)
    Taxonomic identifieri398527 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia
    ProteomesiUP000001739: 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_1000189140Add
    BLAST

    Proteomic databases

    PRIDEiB2T6I7.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi398527.Bphyt_3159.

    Structurei

    3D structure databases

    ProteinModelPortaliB2T6I7.
    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.
    OMAiEYPEGHI.
    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.

    B2T6I7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNKKADSKP QSRYPVNLLD TPFPMRGDLP KREPQWVKEW QERKVYETIR    50
    AASKGRKKFI LHDGPPYANG DIHLGHAVNK ILKDMIVKAR NLAGFDAVYV 100
    PGWDCHGMPI EIQIEKQFGK SLPAAEVMQK ARAYATEQIE KQKVGFRRLG 150
    VLGDWDNPYK TMNFTNEAGE IRALAKIMEK GYVFRGLKPV NWCFDCGSAL 200
    AEAEVEYKDK TDPTIDVLFS FAEPEKTAQA FGLSALPREE GGIVIWTTTP 250
    WTIPANQALN LHPEIVYALV DTPRGLLILA EERVEACLKL YGLEGTIVAT 300
    APGAKLVNVR FNHPLASAHP GYKRTAPVFL GDYVTTETGT GIVHSSPAYG 350
    VEDFVSCKAH GMADSDIINP VMGDGRYIES LALFGGLSIW AANPQIVEAL 400
    QGAGSLMRTE KYTHSYMHCW RHKTPIIYRA TSQWFAGMDV KPNDTDKTLR 450
    ETALEGIENT AFYPAWGKQR LFSMIANRPD WTLSRQRQWG VPMAFFVHKE 500
    TGELHPRTLE LLEEVAQRVE KAGIEAWQTL DPRELLGDDA NMYEKNRDTL 550
    DVWFDSGTTH WHVLRGSHKD ELQFPADLYL EGSDQHRGWF HSSLLTASML 600
    DGRPPYNALL THGFTVDGEG RKMSKSLGNG IDPHEVANRL GAEIIRLWIA 650
    STDYSGELAI SEEILKRVTE GYRRIRNTLR FLLANLSDFD FAQHARPVED 700
    WLEIDRYAVA LSTNLQNDIL SHYDKYEFHP VVAKLQTFCS EDLGGFYLDV 750
    LKDRLYTTAA DSVARRSAQT ALYHIAHGLL RLMAPFLSFT AEEAWKIFQP 800
    NSETIFTETY HAFPAVPDAG ALLDKWTLLR AARSDVTKAL EEARVANLIG 850
    SSLQAEVEIR ASGARYDALT SLGDDLKFVL ITSAATVVKV DSEAEEAVEV 900
    IASKYLKCER CWHYRADVGA NAEHPTLCDR CFSNLFGNGE IRSAA 945
    Length:945
    Mass (Da):105,985
    Last modified:July 1, 2008 - v1
    Checksum:iB698B672B54B10FA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001052 Genomic DNA. Translation: ACD17551.1.
    RefSeqiWP_012434123.1. NC_010681.1.
    YP_001896775.1. NC_010681.1.

    Genome annotation databases

    EnsemblBacteriaiACD17551; ACD17551; Bphyt_3159.
    GeneIDi6283688.
    KEGGibpy:Bphyt_3159.
    PATRICi19216798. VBIBurPhy117947_7147.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001052 Genomic DNA. Translation: ACD17551.1 .
    RefSeqi WP_012434123.1. NC_010681.1.
    YP_001896775.1. NC_010681.1.

    3D structure databases

    ProteinModelPortali B2T6I7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 398527.Bphyt_3159.

    Proteomic databases

    PRIDEi B2T6I7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACD17551 ; ACD17551 ; Bphyt_3159 .
    GeneIDi 6283688.
    KEGGi bpy:Bphyt_3159.
    PATRICi 19216798. VBIBurPhy117947_7147.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BPHY398527:GJEX-3204-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 phytofirmans PsJN."
      Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.
      , Nowak J., Sessitsch A., Lazarovits G., Compant S., Barka E., Tiedje J.
      Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 17436 / PsJN.

    Entry informationi

    Entry nameiSYI_BURPP
    AccessioniPrimary (citable) accession number: B2T6I7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: July 1, 2008
    Last modified: October 1, 2014
    This is version 50 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