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Q31C61

- SYE_PROM9

UniProt

Q31C61 - SYE_PROM9

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Prochlorococcus marinus (strain MIT 9312)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (06 Dec 2005)
      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 sitei251 – 2511ATPUniRule 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

    BioCyciPMAR74546:GHRG-490-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:PMT9312_0473
    OrganismiProchlorococcus marinus (strain MIT 9312)
    Taxonomic identifieri74546 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
    ProteomesiUP000002715: 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 – 479479Glutamate--tRNA ligasePRO_0000237385Add
    BLAST

    Proteomic databases

    PRIDEiQ31C61.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi74546.PMT9312_0473.

    Structurei

    3D structure databases

    ProteinModelPortaliQ31C61.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi9 – 1911"HIGH" regionAdd
    BLAST
    Motifi248 – 2525"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252720.
    KOiK01885.
    OMAiKHYDGDF.
    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.

    Q31C61-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEIRLRLAPS PTGLFHIGTA RTALFNWLYA QKIGGKFLIR IEDTDFLRSK    50
    SEYTKNILDG LKWLGLQWNE EPVKQSDRIS IHKKYIKKLL ECGAAYRCFT 100
    TEDEISELRE EQKKKGLPPK HDNRHRNLSK EEIETFISQG RTSVIRFKID 150
    EEIQIKWIDQ IRGEIKWQGK DLGGDLVLSR RAMGYEIGDP LYNLAVVVDD 200
    NFMNITHVVR GEDHISNTAK QILIYEALDF KLPTFSHTPL ILNNEGKKLS 250
    KRDCVTSIDE FRDMGYLPEA LSNYMAFLGW SPKSATSEIL SLDEISKIFE 300
    LSDINKAGAK FSWEKLNWIN SQYIKNMETV KLSETIGKYW DNMGWDPPSQ 350
    EWAIKLAILI KDSMTLLKDA IDQSKPFFLL PPIQKEGKDF LESNDGKTSL 400
    KLILNYLIEQ NTGKVDKDKA KEIINEISKM HNVKKGILMK SLRVAFFGSL 450
    SGPDLIQSWE LFSESKSDIS RIERCLKSI 479
    Length:479
    Mass (Da):55,167
    Last modified:December 6, 2005 - v1
    Checksum:i468D4900AD2942D3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000111 Genomic DNA. Translation: ABB49534.1.
    RefSeqiWP_011376033.1. NC_007577.1.
    YP_396970.1. NC_007577.1.

    Genome annotation databases

    EnsemblBacteriaiABB49534; ABB49534; PMT9312_0473.
    GeneIDi3765270.
    KEGGipmi:PMT9312_0473.
    PATRICi23004620. VBIProMar70153_0493.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000111 Genomic DNA. Translation: ABB49534.1 .
    RefSeqi WP_011376033.1. NC_007577.1.
    YP_396970.1. NC_007577.1.

    3D structure databases

    ProteinModelPortali Q31C61.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 74546.PMT9312_0473.

    Proteomic databases

    PRIDEi Q31C61.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB49534 ; ABB49534 ; PMT9312_0473 .
    GeneIDi 3765270.
    KEGGi pmi:PMT9312_0473.
    PATRICi 23004620. VBIProMar70153_0493.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PMAR74546:GHRG-490-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. "Complete sequence of Prochlorococcus marinus str. MIT 9312."
      US DOE Joint Genome Institute
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MIT 9312.

    Entry informationi

    Entry nameiSYE_PROM9
    AccessioniPrimary (citable) accession number: Q31C61
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 62 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