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)

B6J1S2

- SYI_COXB2

UniProt

B6J1S2 - SYI_COXB2

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Coxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212))
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 41 (01 Oct 2014)
      Sequence version 1 (16 Dec 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 bindingi899 – 8991ZincUniRule annotation
    Metal bindingi902 – 9021ZincUniRule annotation
    Metal bindingi919 – 9191ZincUniRule annotation
    Metal bindingi922 – 9221ZincUniRule 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

    BioCyciCBUR434923:GC8S-1609-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:CbuG_1612
    OrganismiCoxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212))
    Taxonomic identifieri434923 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
    ProteomesiUP000007729: 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 – 936936Isoleucine--tRNA ligasePRO_1000189143Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi434923.CbuG_1612.

    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.
    InterProiIPR002300. 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.

    Sequencei

    Sequence statusi: Complete.

    B6J1S2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDYKDTLNL PQTDFPMRAN LPEREPQTLA RWQTLDLYRK IRKDREGQPK    50
    FILHDGPPYA NGRAHLGTAF NKTLKDIVVK SKTLSGFDAP FVPGWDCHGL 100
    PIELNVEKKL GKDKLSANAF RQACRDYAFS QIELQRDDFQ RLGVLGDWQH 150
    PYLTMDFGYE ADTVRALAKI VANGHLLRGQ KPVHWCAACG SALAEAEVEY 200
    RDKASPAVDV GFEAVDAEAV RQRFGVKNAT TRVLVPIWTT TPWTLPANEA 250
    VSVHPELHYA LVKSELQNQP VYLILAKDLV DSAMQRYGVD DYEVHGNLKG 300
    DALEGMQLQH PFLDRIVPII LGEHVTTEAG TGNVHTAPAH GLEDYFVAEK 350
    YNLPINNPVD ARGRFIPDTF LVGGQPVFKA NEPIIVLLAD SGHLLHSETI 400
    QHSYPHCWRH KTPLIFRATP QWFIGMNKNG LRERALAEIE KVTWLPAWGE 450
    ARIGKMVADR PDWCISRQRL WGIPIPLFIH KKSGELHPKS PALMEKVAQL 500
    IEKESVDAWF DLDPKVLLGD DADHYEKVTD VLDVWFDSGV THFCVLEKRR 550
    ELKVPADIYL EGSDQHRGWF QSSLLTSLAI RDKAPYKSVL TYGFVVDSQG 600
    RKMSKSLGNV ILPADVVKNL GADVLRLWAA SMDYTVEVNV SDEILKRASD 650
    AYRRIRNTAR FLLSNLYDFD PKKDKVAVDQ LVALDRWAIF TTQKLQEKII 700
    TAYDRYRFPA IYQAIHNFCT VEMGSFYLDI IKDRLYTSKE SGLPRRSAQT 750
    ALYYIAEAFV RWIAPIISFT ADEIWQFMPG DREPSVFLTQ WFSDFPNAAL 800
    SGEEEQRWQL LLQIRDEVNK ALETYRNEGK IGSALTAEVV LYADERLNAA 850
    IATLGEELRF VLITSEASVL PFNEKSKAAF DTALPGLALE INVSEFEKCA 900
    RCWQRRSSVG QIKEHADLCD RCVSNAFEDG DMRQFA 936
    Length:936
    Mass (Da):106,126
    Last modified:December 16, 2008 - v1
    Checksum:i11B778F5F7F9C450
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001019 Genomic DNA. Translation: ACJ18900.1.
    RefSeqiWP_012570344.1. NC_011527.1.
    YP_002304045.1. NC_011527.1.

    Genome annotation databases

    EnsemblBacteriaiACJ18900; ACJ18900; CbuG_1612.
    GeneIDi7014028.
    KEGGicbg:CbuG_1612.
    PATRICi17914305. VBICoxBur10955_1611.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001019 Genomic DNA. Translation: ACJ18900.1 .
    RefSeqi WP_012570344.1. NC_011527.1.
    YP_002304045.1. NC_011527.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 434923.CbuG_1612.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACJ18900 ; ACJ18900 ; CbuG_1612 .
    GeneIDi 7014028.
    KEGGi cbg:CbuG_1612.
    PATRICi 17914305. VBICoxBur10955_1611.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci CBUR434923:GC8S-1609-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 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.
    ProtoNeti Search...

    Publicationsi

    1. "Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
      Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A.
      Infect. Immun. 77:642-656(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CbuG_Q212.

    Entry informationi

    Entry nameiSYI_COXB2
    AccessioniPrimary (citable) accession number: B6J1S2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 41 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