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)

Q39YT0

- Q39YT0_GEOMG

UniProt

Q39YT0 - Q39YT0_GEOMG

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (22 Nov 2005)
      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 annotationSAAS annotation

    Catalytic activityi

    ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile).UniRule annotationSAAS annotation

    Cofactori

    Binds 1 zinc ion per subunit.UniRule annotationSAAS annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei560 – 5601Aminoacyl-adenylateUniRule annotation
    Binding sitei604 – 6041ATPUniRule annotation
    Metal bindingi895 – 8951ZincUniRule annotation
    Metal bindingi898 – 8981ZincUniRule annotation
    Metal bindingi915 – 9151ZincUniRule annotation
    Metal bindingi918 – 9181ZincUniRule 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 synthetaseUniRule annotationSAAS annotationImported, Ligase

    Keywords - Biological processi

    Protein biosynthesisUniRule annotationSAAS annotation

    Keywords - Ligandi

    ATP-bindingUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, Nucleotide-binding, ZincUniRule annotationSAAS annotation

    Enzyme and pathway databases

    BioCyciGMET269799:GHNY-351-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isoleucine--tRNA ligaseUniRule annotation (EC:6.1.1.5UniRule annotation)
    Alternative name(s):
    Isoleucyl-tRNA synthetaseUniRule annotation
    Gene namesi
    Name:ileSUniRule annotationImported
    Ordered Locus Names:Gmet_0351Imported
    OrganismiGeobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210)Imported
    Taxonomic identifieri269799 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter
    ProteomesiUP000007073: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotationSAAS annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    CytoplasmUniRule annotationSAAS annotation

    Interactioni

    Subunit structurei

    Monomer.UniRule annotationSAAS annotation

    Protein-protein interaction databases

    STRINGi269799.Gmet_0351.

    Structurei

    3D structure databases

    ProteinModelPortaliQ39YT0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi57 – 6711"HIGH" regionUniRule annotationAdd
    BLAST
    Motifi601 – 6055"KMSKS" regionUniRule annotation

    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.

    Q39YT0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEYKNTLNLP VTDFPMKANL PQREPEILAG WQKNDLYGKL TAAGEGKPRY    50
    VLHDGPPYAN GHIHIGHALN KILKDIILKS KRMQGFDAPY VPGWDCHGLP 100
    IELQVEKNLG SKKHETTKLQ MRKQCREYAE KFVKIQRDEF ERLGVIGDWD 150
    RPYLTMTHDY EGITARELAR FAANGGLYKG KKPVHWCSSC VTALAEAEVE 200
    YADKTSPSIY VKFLLQDDIS ASVPALAGKK VSLVIWTTTP WTIPANLAVA 250
    LHPELEYVAL EAGGEVLVVA EGLKDAFMAA TGVQGSVIAT FRADILYRKR 300
    CKHPFYDRDS IVLLGEHVTL DAGTGCVHTA PGHGQEDYEL ALVEGLDIYN 350
    PVDNRGRYIQ SLEFFGGQFV FDANATVIEK LQEVGALVGQ GSVEHSYPHC 400
    WRCKKPIIFR ATEQWFISME KNDLRKKALE EIDRVSWVPK WGRERIHGMI 450
    ENRPDWCISR QRSWGVPITA FYCTECGEIL ADGTIMHHVA DLFMEGGADL 500
    WYEKEAAELL PPGTVCPQCG KSAFEKEMDI LDVWFDSGVS HAAVLENRPE 550
    LGSPANMYLE GSDQHRGWFH SSLLASVGTR GTAPYKEVLT HGFVVDGSGR 600
    KMSKSVGNVV APEEVIKKYG AEILRLWVAA QDYRDDVRIS QEILTRLAEA 650
    YRRIRNTCRY LLGNLYDFDP ATDMVPFGEM TELDRWALHQ LEVLKEKVFT 700
    AYNEYEFHIL YHAVNGFCTV EMSAFYLDII KERYTSRKDS PERRSAQTVM 750
    YLVLESLVRL MAPVLSFTAD EVWGYMPKRA EASVHLASFP ELCPERKDEA 800
    LVERWARTMA VRGDVSKALE QARVQKTIGH SLDAAVTLSA EPELLGFLKE 850
    YAGELATVFI VSKVELVGEI AGEFVEAEGV KGLKIGVTAA PGDKCERCWH 900
    YDEEIGGDAE HPTLCPKCVA AVK 923
    Length:923
    Mass (Da):103,598
    Last modified:November 22, 2005 - v1
    Checksum:i7BCF7E69BF1B2E7F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000148 Genomic DNA. Translation: ABB30594.1.
    RefSeqiYP_006719314.1. NC_007517.1.

    Genome annotation databases

    EnsemblBacteriaiABB30594; ABB30594; Gmet_0351.
    GeneIDi3739717.
    KEGGigme:Gmet_0351.
    PATRICi21999848. VBIGeoMet55070_0371.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000148 Genomic DNA. Translation: ABB30594.1 .
    RefSeqi YP_006719314.1. NC_007517.1.

    3D structure databases

    ProteinModelPortali Q39YT0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 269799.Gmet_0351.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB30594 ; ABB30594 ; Gmet_0351 .
    GeneIDi 3739717.
    KEGGi gme:Gmet_0351.
    PATRICi 21999848. VBIGeoMet55070_0371.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci GMET269799:GHNY-351-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 Geobacter metallireducens GS-15."
      US DOE Joint Genome Institute
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
      Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: GS-15 / ATCC 53774 / DSM 7210Imported.

    Entry informationi

    Entry nameiQ39YT0_GEOMG
    AccessioniPrimary (citable) accession number: Q39YT0
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 22, 2005
    Last sequence update: November 22, 2005
    Last modified: October 1, 2014
    This is version 78 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3