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B5Y7R0

- SYE_COPPD

UniProt

B5Y7R0 - SYE_COPPD

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / BT)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 39 (01 Oct 2014)
      Sequence version 1 (25 Nov 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 sitei252 – 2521ATPUniRule 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

    BioCyciCPRO309798:GH7M-437-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:COPRO5265_0442
    OrganismiCoprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / BT)
    Taxonomic identifieri309798 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermodesulfobiaceaeCoprothermobacter
    ProteomesiUP000001732: 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 – 467467Glutamate--tRNA ligasePRO_0000367653Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi309798.COPRO5265_0442.

    Structurei

    3D structure databases

    ProteinModelPortaliB5Y7R0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi15 – 2511"HIGH" regionAdd
    BLAST
    Motifi249 – 2535"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252720.
    KOiK01885.
    OMAiFFVEEVD.
    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.

    B5Y7R0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVNDSTHIK TRFAPSPTGY LHVGGARTAL FNYLFAKKFG GTFLLRIEDT    50
    DPERSKPEYS EQILISMKWL GLDWDEGPYH QSERMHIYQQ YTQKLLEEGK 100
    AYRCFCTTEE LEQMREQQRQ QGLPTRYDGR CSRLTQEEIE ERLNKGMPFA 150
    VRLKVPQDRG IIAWDDMVKG HIEINSSELD DFILVRSDGT PTYNFAVVID 200
    DHTMGVTHVL RGEDHIPNTP KQILIYEALG WETPEFGHVP MILGKDKTKL 250
    SKRHGAVGVE AYRDEGFLPE ALFNFLALLG ASYDPDREVY TKQELIDLFD 300
    PKKIGLHPAV FDPDKLYYIN REHMKMLPPE ELLDRIRPFA EAKGFQIEPY 350
    HLRLIPLLVE RMRTLKDFVE LADYIFTDDF TVDEKAQELL AKDLPLGGLA 400
    EQLDATVWDA DHIEAVLRQY AQDKGIKPRD YFPFIRAVIS GKSVGPSLFH 450
    LMEAMPKDMV LRRLRKS 467
    Length:467
    Mass (Da):53,985
    Last modified:November 25, 2008 - v1
    Checksum:iD9995F970A95DB0E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001145 Genomic DNA. Translation: ACI16900.1.
    RefSeqiYP_002246807.1. NC_011295.1.

    Genome annotation databases

    EnsemblBacteriaiACI16900; ACI16900; COPRO5265_0442.
    GeneIDi6944687.
    KEGGicpo:COPRO5265_0442.
    PATRICi21473736. VBICopPro72829_0423.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001145 Genomic DNA. Translation: ACI16900.1 .
    RefSeqi YP_002246807.1. NC_011295.1.

    3D structure databases

    ProteinModelPortali B5Y7R0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 309798.COPRO5265_0442.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACI16900 ; ACI16900 ; COPRO5265_0442 .
    GeneIDi 6944687.
    KEGGi cpo:COPRO5265_0442.
    PATRICi 21473736. VBICopPro72829_0423.

    Phylogenomic databases

    eggNOGi COG0008.
    HOGENOMi HOG000252720.
    KOi K01885.
    OMAi FFVEEVD.
    OrthoDBi EOG6DRPF7.

    Enzyme and pathway databases

    BioCyci CPRO309798:GH7M-437-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. "The complete genome sequence of Coprothermobacter proteolyticus strain ATCC 5245 / DSM 5265 / BT."
      Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.
      Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35245 / DSM 5265 / BT.

    Entry informationi

    Entry nameiSYE_COPPD
    AccessioniPrimary (citable) accession number: B5Y7R0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 39 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