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)

Q2NVY6

- SYI_SODGM

UniProt

Q2NVY6 - SYI_SODGM

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Sodalis glossinidius (strain morsitans)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (07 Feb 2006)
      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

    BioCyciSGLO343509:GJJC-439-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:SG0414
    OrganismiSodalis glossinidius (strain morsitans)
    Taxonomic identifieri343509 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSodalis
    ProteomesiUP000001932: 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_1000022126Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi343509.SG0414.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2NVY6.
    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.
    KOiK01870.
    OMAiKKRIELM.
    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.

    Q2NVY6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDYKNTLNL PDTGFPMRGD LAKREPGMLE RWYEQDLYGI ICQARKGKKT    50
    FILHDGPPYA NGSIHIGHSV NKILKDIIIK SKGLMGYDSP YVPGWDCHGL 100
    PIELKVEQLI GKPGEKVSAA EFRTACRRYA AEQVEGQKKD FIRLGVLGDW 150
    EHPYLTMNFA TEANIIRALG KIIANGHLHK GAKPVHWCID CRSALAEAEV 200
    EYYDRTSPSI DVAFAADDVR AVAAKFGAAD FAGQISLIIW TTTPWTLPAN 250
    RAIAVHPDFD YQLVEVEGQG YILAADLVDS VMARAGITCW TVLGSAKGSA 300
    LELLRFRHPF MGFDVPAILG QHVTLDAGTG AVHTAPGHGP DDYVIGQQYG 350
    LEVANPVGPD GCYLPGTLPA LDGLQVFKAN DVVINLLCDS GALLHVEKLQ 400
    HSYPHCWRHK TSIIFRATPQ WFVSMDQRGL RKQSLAEIKD VQWIPGWGQA 450
    RIETMVANRP DWCISRQRTW GVPMALFVHN ETEALHPRTI ELMESVAQRV 500
    EQDGIQAWWD LDPAEILGDD AAHYHKVPDT LDVWFDSGST HSSIVAVRPE 550
    FEGHAPDMYL EGSDQHRGWF MSSLMISTAM HGKAPYRQVL THGFTVDGQG 600
    RKMSKSVGNV VSPQQVMDKL GADILRLWVA STDYTGEMAV SDEILKRSAD 650
    AYRRIRNTAR FLLANLNGFD PARHSVSPEQ MVVLDRWAVG RAQAAQAEIV 700
    AAYDSYDFHN VVQRMMQFCS VEMGSFYLDI IKDRQYTTKA DSIARRSCQT 750
    ALYHIIEALV RWMAPIMSFT ADEIWGFMPG ERAQYVFTEE WYDGLFGLDA 800
    AQPLNDAYWQ ILLQVRSETN KVIEQARADK RIGGSLEARV TLYAEPDLAA 850
    SLRELGDELY FTLLTSNAVV ADYADAGDDA VQCEGLKGLK IALAKAEGEK 900
    CPRCWHYETD IGQHADHPEI CGRCVTNVAG PGEERKFV 938
    Length:938
    Mass (Da):104,502
    Last modified:February 7, 2006 - v1
    Checksum:i06C0E8D4763ABF4B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008232 Genomic DNA. Translation: BAE73689.1.
    RefSeqiYP_454094.1. NC_007712.1.

    Genome annotation databases

    EnsemblBacteriaiBAE73689; BAE73689; SG0414.
    GeneIDi3867525.
    KEGGisgl:SG0414.
    PATRICi23647513. VBISodGlo61428_1080.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008232 Genomic DNA. Translation: BAE73689.1 .
    RefSeqi YP_454094.1. NC_007712.1.

    3D structure databases

    ProteinModelPortali Q2NVY6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 343509.SG0414.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAE73689 ; BAE73689 ; SG0414 .
    GeneIDi 3867525.
    KEGGi sgl:SG0414.
    PATRICi 23647513. VBISodGlo61428_1080.

    Phylogenomic databases

    eggNOGi COG0060.
    KOi K01870.
    OMAi KKRIELM.
    OrthoDBi EOG644ZM1.

    Enzyme and pathway databases

    BioCyci SGLO343509:GJJC-439-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. "Massive genome erosion and functional adaptations provide insights into the symbiotic lifestyle of Sodalis glossinidius in the tsetse host."
      Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M., Aksoy S.
      Genome Res. 16:149-156(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: morsitans.

    Entry informationi

    Entry nameiSYI_SODGM
    AccessioniPrimary (citable) accession number: Q2NVY6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: February 7, 2006
    Last modified: October 1, 2014
    This is version 67 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