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A5IMM2

- SYE2_THEP1

UniProt

A5IMM2 - SYE2_THEP1

Protein

Glutamate--tRNA ligase 2

Gene

gltX2

Organism
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (26 Jun 2007)
      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

    BioCyciTPET390874:GHJI-1478-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate--tRNA ligase 2UniRule annotation (EC:6.1.1.17UniRule annotation)
    Alternative name(s):
    Glutamyl-tRNA synthetase 2UniRule annotation
    Short name:
    GluRS 2UniRule annotation
    Gene namesi
    Name:gltX2UniRule annotation
    Ordered Locus Names:Tpet_1432
    OrganismiThermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
    Taxonomic identifieri390874 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000006558: 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 – 469469Glutamate--tRNA ligase 2PRO_0000367791Add
    BLAST

    Proteomic databases

    PRIDEiA5IMM2.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi390874.Tpet_1432.

    Structurei

    3D structure databases

    ProteinModelPortaliA5IMM2.
    SMRiA5IMM2. Positions 1-468.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi8 – 1811"HIGH" regionAdd
    BLAST
    Motifi250 – 2545"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252720.
    KOiK09698.
    OMAiPEGMLNY.
    OrthoDBiEOG6DRPF7.

    Family and domain databases

    Gene3Di1.10.10.350. 1 hit.
    1.10.1160.10. 1 hit.
    1.10.8.70. 1 hit.
    3.40.50.620. 2 hits.
    HAMAPiMF_00022_B. Glu_tRNA_synth_B.
    InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
    IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
    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.

    A5IMM2-1 [UniParc]FASTAAdd to Basket

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    MVRVRFAPSP TGFLHVGGAR TALFNFLFAR KEKGKFILRI EDTDLERSER    50
    EYEEKLMESL RWLGLLWDEG PDVGGDHGPY RQSERVEIYR EHAERLVKEG 100
    KAYYVYAYPE EIEEMREKLL SEGKAPHYSQ EMFEKFDTPE RRREYEEKGL 150
    RPAVFFKMPR KDYVLNDVVK GEVVFKTGAI GDFVIMRSNG LPTYNFACVV 200
    DDMLMEITHV IRGDDHLSNT LRQLALYEAF EKAPPVFAHV STILGPDGKK 250
    LSKRHGATSV EAFRDMGYLP EALVNYLALL GWSHPEGKEL LTLEELISSF 300
    SLDRLSPNPA IFDPQKLKWM NGYYLRNMPI EKLAELAKPF FEKAGIKIID 350
    EEYFKKVLEI TKERVEVLSE FPEESRFFFE DPAPVEIPEE MKEVFSQLKE 400
    ELQNVRWTME EITPVFKKVL KQHGVKPKEF YMTLRRVLTG REEGPELVNI 450
    IPLLGKEIFL RRIERSLGG 469
    Length:469
    Mass (Da):54,607
    Last modified:June 26, 2007 - v1
    Checksum:iF27D3AB4FE070BD8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000702 Genomic DNA. Translation: ABQ47445.1.
    RefSeqiYP_001245021.1. NC_009486.1.

    Genome annotation databases

    EnsemblBacteriaiABQ47445; ABQ47445; Tpet_1432.
    GeneIDi5170216.
    KEGGitpt:Tpet_1432.
    PATRICi23945711. VBIThePet65348_1452.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000702 Genomic DNA. Translation: ABQ47445.1 .
    RefSeqi YP_001245021.1. NC_009486.1.

    3D structure databases

    ProteinModelPortali A5IMM2.
    SMRi A5IMM2. Positions 1-468.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 390874.Tpet_1432.

    Proteomic databases

    PRIDEi A5IMM2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ47445 ; ABQ47445 ; Tpet_1432 .
    GeneIDi 5170216.
    KEGGi tpt:Tpet_1432.
    PATRICi 23945711. VBIThePet65348_1452.

    Phylogenomic databases

    eggNOGi COG0008.
    HOGENOMi HOG000252720.
    KOi K09698.
    OMAi PEGMLNY.
    OrthoDBi EOG6DRPF7.

    Enzyme and pathway databases

    BioCyci TPET390874:GHJI-1478-MONOMER.

    Family and domain databases

    Gene3Di 1.10.10.350. 1 hit.
    1.10.1160.10. 1 hit.
    1.10.8.70. 1 hit.
    3.40.50.620. 2 hits.
    HAMAPi MF_00022_B. Glu_tRNA_synth_B.
    InterProi IPR008925. aa-tRNA-synth_I_codon-bd.
    IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
    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: RKU-1 / ATCC BAA-488 / DSM 13995.

    Entry informationi

    Entry nameiSYE2_THEP1
    AccessioniPrimary (citable) accession number: A5IMM2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: June 26, 2007
    Last modified: October 1, 2014
    This is version 51 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