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B0JY53

- SYE_MICAN

UniProt

B0JY53 - SYE_MICAN

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Microcystis aeruginosa (strain NIES-843)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (18 Mar 2008)
      Previous versions | rss
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    Functioni

    Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).UniRule annotation

    Catalytic activityi

    ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei253 – 2531ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. glutamate-tRNA ligase activity Source: UniProtKB-HAMAP
    3. tRNA binding Source: InterPro

    GO - Biological processi

    1. glutamyl-tRNA aminoacylation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMAER449447:GHO8-5310-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate--tRNA ligaseUniRule annotation (EC:6.1.1.17UniRule annotation)
    Alternative name(s):
    Glutamyl-tRNA synthetaseUniRule annotation
    Short name:
    GluRSUniRule annotation
    Gene namesi
    Name:gltXUniRule annotation
    Ordered Locus Names:MAE_52690
    OrganismiMicrocystis aeruginosa (strain NIES-843)
    Taxonomic identifieri449447 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesMicrocystis
    ProteomesiUP000001510: 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 – 480480Glutamate--tRNA ligasePRO_1000074325Add
    BLAST

    Proteomic databases

    PaxDbiB0JY53.
    PRIDEiB0JY53.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi449447.MAE_52690.

    Structurei

    3D structure databases

    ProteinModelPortaliB0JY53.
    SMRiB0JY53. Positions 2-478.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi9 – 1911"HIGH" regionAdd
    BLAST
    Motifi250 – 2545"KMSKS" region

    Sequence similaritiesi

    Belongs to the class-I aminoacyl-tRNA synthetase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252722.
    KOiK01885.
    OMAiVTGQTHG.
    OrthoDBiEOG6DRPF7.

    Family and domain databases

    Gene3Di1.10.10.350. 1 hit.
    1.10.1160.10. 1 hit.
    3.40.50.620. 2 hits.
    HAMAPiMF_00022_B. Glu_tRNA_synth_B.
    InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
    IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
    IPR001412. aa-tRNA-synth_I_CS.
    IPR004527. Glu-tRNA-ligase_bac/mito.
    IPR000924. Glu/Gln-tRNA-synth.
    IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
    IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PANTHERiPTHR10119. PTHR10119. 1 hit.
    PfamiPF00749. tRNA-synt_1c. 1 hit.
    [Graphical view]
    PRINTSiPR00987. TRNASYNTHGLU.
    SUPFAMiSSF48163. SSF48163. 1 hit.
    TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B0JY53-1 [UniParc]FASTAAdd to Basket

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    MTVRVRIAPS PTGNLHIGTA RTAVFNWLFA RHHRGKFILR VEDTDLERSR    50
    PEYTENIQAG LQWLGLNWDE GPFFQTQRLN YYRQAIQTLL DRGLAYRCYC 100
    TPEELEKMRE EQKARNLAPR YDNRHRYLTP EQQAQFEQAG RKAVIRFIID 150
    DDQEIIWQDL IREKVIWKGS DLGGDMVIAR TSENGEENFG QPLYNLAVVV 200
    DDIDMEITHV IRGEDHIANT AKQILLYEAL GAKVPEFAHS PLILNQEGRK 250
    LSKRDGVTSI DDFRKLGFLP QALVNYMTLL GWTPPDSTEE IFTLEAAAEV 300
    FSLERVNKAG AKFDWTKLDW INSQYLHRLT GEELVPLLLP YWQEAGYNFA 350
    AETDRAWLIG LATLIGPSLT RLSDAVAESR LLLTPLANYN QEALSQLQLE 400
    GVKDIIKDIL AAITPDLTGE VAKGIVETTT KAHRVKKGLV MKSLRAALMG 450
    ELHGPDLMQS WLLLNQKGWD ISRLQQAVNS 480
    Length:480
    Mass (Da):54,663
    Last modified:March 18, 2008 - v1
    Checksum:i0A7A5D456C43761D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP009552 Genomic DNA. Translation: BAG05091.1.
    RefSeqiYP_001660283.1. NC_010296.1.

    Genome annotation databases

    EnsemblBacteriaiBAG05091; BAG05091; MAE_52690.
    GeneIDi5866106.
    KEGGimar:MAE_52690.
    PATRICi22634997. VBIMicAer59304_4802.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP009552 Genomic DNA. Translation: BAG05091.1 .
    RefSeqi YP_001660283.1. NC_010296.1.

    3D structure databases

    ProteinModelPortali B0JY53.
    SMRi B0JY53. Positions 2-478.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 449447.MAE_52690.

    Proteomic databases

    PaxDbi B0JY53.
    PRIDEi B0JY53.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAG05091 ; BAG05091 ; MAE_52690 .
    GeneIDi 5866106.
    KEGGi mar:MAE_52690.
    PATRICi 22634997. VBIMicAer59304_4802.

    Phylogenomic databases

    eggNOGi COG0008.
    HOGENOMi HOG000252722.
    KOi K01885.
    OMAi VTGQTHG.
    OrthoDBi EOG6DRPF7.

    Enzyme and pathway databases

    BioCyci MAER449447:GHO8-5310-MONOMER.

    Family and domain databases

    Gene3Di 1.10.10.350. 1 hit.
    1.10.1160.10. 1 hit.
    3.40.50.620. 2 hits.
    HAMAPi MF_00022_B. Glu_tRNA_synth_B.
    InterProi IPR008925. aa-tRNA-synth_I_codon-bd.
    IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
    IPR001412. aa-tRNA-synth_I_CS.
    IPR004527. Glu-tRNA-ligase_bac/mito.
    IPR000924. Glu/Gln-tRNA-synth.
    IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
    IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    PANTHERi PTHR10119. PTHR10119. 1 hit.
    Pfami PF00749. tRNA-synt_1c. 1 hit.
    [Graphical view ]
    PRINTSi PR00987. TRNASYNTHGLU.
    SUPFAMi SSF48163. SSF48163. 1 hit.
    TIGRFAMsi TIGR00464. gltX_bact. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NIES-843.

    Entry informationi

    Entry nameiSYE_MICAN
    AccessioniPrimary (citable) accession number: B0JY53
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: March 18, 2008
    Last modified: October 1, 2014
    This is version 42 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