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Q058C8

- SYE_BUCCC

UniProt

Q058C8 - SYE_BUCCC

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Buchnera aphidicola subsp. Cinara cedri (strain Cc)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (14 Nov 2006)
      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 sitei241 – 2411ATPUniRule 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

    BioCyciBAPH372461:GHAJ-42-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:BCc_042
    OrganismiBuchnera aphidicola subsp. Cinara cedri (strain Cc)
    Taxonomic identifieri372461 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
    ProteomesiUP000000669: 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 – 474474Glutamate--tRNA ligasePRO_1000001877Add
    BLAST

    Proteomic databases

    PRIDEiQ058C8.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi372461.BCc_042.

    Structurei

    3D structure databases

    ProteinModelPortaliQ058C8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi9 – 1911"HIGH" regionAdd
    BLAST
    Motifi238 – 2425"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252722.
    KOiK01885.
    OMAiHYIKELD.
    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.

    Q058C8-1 [UniParc]FASTAAdd to Basket

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    MKIKTRFSPS PTGLLHMGGV RTALYSWLFA RKNNGSFILR IEDTDKNRVK    50
    NNSVQDILYG LRYLQLNWDE GPFFQSNRIN IYKNIILFML KKGIAYKCYC 100
    SKNRLDKLRK NQILNKKKPK YDNKCRNKNF FLKKSNIPYV IRFKNPTKGL 150
    VEFRDMIRGK ISISNKELDD LVIQRSNGMP TYNFCVVVDD WQMNITHIIR 200
    GEDHIHNTPR QINLLSSLNA YIPQYAHTSM ILDKKRKKLS KRCSSYSIIN 250
    YINNGFIPEA ILNYALQLGW SYKNQEIFSI NEMKNIFNIK YINKSPSIID 300
    KKKFLWFNHY YLNNISFNLK YKYFFSYCKK NNIFFDKDVN ISGVIKDFLG 350
    RHSTFKDFIQ TYDYFYKEIN ISNIKNIYLY NKLINITILK FLYKKFNLLN 400
    NWDLKNILLI IKESILYFKI SFKEIAILIR IVITGKKQTP SISSIIFYIG 450
    KKKFLLRIKN FLKYLQLNNS NFSK 474
    Length:474
    Mass (Da):56,540
    Last modified:November 14, 2006 - v1
    Checksum:i4A62292F1D55B43B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000263 Genomic DNA. Translation: ABJ90521.1.
    RefSeqiWP_011672440.1. NC_008513.1.
    YP_802614.1. NC_008513.1.

    Genome annotation databases

    EnsemblBacteriaiABJ90521; ABJ90521; BCc_042.
    GeneIDi4440970.
    KEGGibcc:BCc_042.
    PATRICi21246021. VBIBucAph7855_0036.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000263 Genomic DNA. Translation: ABJ90521.1 .
    RefSeqi WP_011672440.1. NC_008513.1.
    YP_802614.1. NC_008513.1.

    3D structure databases

    ProteinModelPortali Q058C8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 372461.BCc_042.

    Proteomic databases

    PRIDEi Q058C8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABJ90521 ; ABJ90521 ; BCc_042 .
    GeneIDi 4440970.
    KEGGi bcc:BCc_042.
    PATRICi 21246021. VBIBucAph7855_0036.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BAPH372461:GHAJ-42-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. "A small microbial genome: the end of a long symbiotic relationship?"
      Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M., Silva F.J., Moya A., Latorre A.
      Science 314:312-313(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Cc.

    Entry informationi

    Entry nameiSYE_BUCCC
    AccessioniPrimary (citable) accession number: Q058C8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: November 14, 2006
    Last modified: October 1, 2014
    This is version 56 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