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Q5PAG8

- SYE2_ANAMM

UniProt

Q5PAG8 - SYE2_ANAMM

Protein

Glutamate--tRNA ligase 2

Gene

gltX2

Organism
Anaplasma marginale (strain St. Maries)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 2 (07 Jun 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 sitei239 – 2391ATPUniRule 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

    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:AM775
    OrganismiAnaplasma marginale (strain St. Maries)
    Taxonomic identifieri234826 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma
    ProteomesiUP000006557: 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 – 466466Glutamate--tRNA ligase 2PRO_0000119493Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi234826.AM775.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5PAG8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi9 – 1911"HIGH" regionAdd
    BLAST
    Motifi236 – 2405"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252722.
    KOiK01885.
    OMAiCITHIIR.
    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.

    Q5PAG8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRVITRFAPS PTGSLHLGGA RTALFNWLFA RRHGGQFLLR MEDTDQERSS    50
    ETVAQSIIED MAWLGLHHDQ DVVIQSARRE RHTQVAEELL ARGKAYYCYC 100
    SEDDIAAEKL RHENEGKHYR HHCPSRDANH AQSGTAGVLR LKSPENREIK 150
    FTDGVYGEIS VSSEQIDDMV ILRSNGHPTY LLAVVVDDHD MCITHIIRGS 200
    DHITNTIKQM LLAEAMGWDN PQFCHIPLIH DEGGAKLSKR NRAPGVHEYR 250
    ELGFLPEAVC NYLLRMGWSH KDEEIITMQS ATQLFSIEKI GTSHSCLDSK 300
    KLLFLNHHYM NQKTELEILG LLLPFLEQEL GHTVAETKLA RLSLGVKKLM 350
    ERAKTLADLA RDSVFYVQNI PISVDDDAKQ VILKSSELLA KLVGAMSQIE 400
    PKTWTKDFLS SYIKEWTKSN DVVISDVYHL LRAAIAGRLS TPSISEVMEI 450
    LGQEECISRL RFFLNS 466
    Length:466
    Mass (Da):52,783
    Last modified:June 7, 2005 - v2
    Checksum:i779D34443F542391
    GO

    Sequence cautioni

    The sequence AAV86712.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000030 Genomic DNA. Translation: AAV86712.1. Different initiation.
    RefSeqiYP_153967.1. NC_004842.2.

    Genome annotation databases

    EnsemblBacteriaiAAV86712; AAV86712; AM775.
    GeneIDi3171550.
    KEGGiama:AM775.
    PATRICi20947507. VBIAnaMar46146_0669.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000030 Genomic DNA. Translation: AAV86712.1 . Different initiation.
    RefSeqi YP_153967.1. NC_004842.2.

    3D structure databases

    ProteinModelPortali Q5PAG8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 234826.AM775.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV86712 ; AAV86712 ; AM775 .
    GeneIDi 3171550.
    KEGGi ama:AM775.
    PATRICi 20947507. VBIAnaMar46146_0669.

    Phylogenomic databases

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

    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 genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
      Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
      Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: St. Maries.

    Entry informationi

    Entry nameiSYE2_ANAMM
    AccessioniPrimary (citable) accession number: Q5PAG8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 68 of the entry and version 2 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