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A7I338

- SYE2_CAMHC

UniProt

A7I338 - SYE2_CAMHC

Protein

Glutamate--tRNA ligase 2

Gene

gltX2

Organism
Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 1 (11 Sep 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 sitei238 – 2381ATPUniRule 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

    BioCyciCHOM360107:GHCX-1384-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:CHAB381_1380
    OrganismiCampylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A)
    Taxonomic identifieri360107 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
    ProteomesiUP000002407: 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 – 433433Glutamate--tRNA ligase 2PRO_0000367637Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi360107.CHAB381_1380.

    Structurei

    3D structure databases

    ProteinModelPortaliA7I338.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi6 – 1611"HIGH" regionAdd
    BLAST
    Motifi235 – 2395"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252720.
    KOiK01885.
    OMAiIFNYICS.
    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.

    A7I338-1 [UniParc]FASTAAdd to Basket

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    MYRFAPSPTG DMHIGNLRAA IFNYICSLQD KSGFILRIED TDTARNISGK    50
    GEEIKEILKQ FGIKWDKLYI QSENLKFHRE LASKLLNDKK AFCCFCSEEE 100
    LAAKKAAAKK AGVAYRYDGT CEKLSDLEVL NCEKPFVIRM KKPNRILKFN 150
    DLIKGEIGFE PENIDSFVIM RVDKTPTYNF ACAVDDMLEG VTCVIRGEDH 200
    VSNTPKQNWI RECLGYTEEI SYAHLPIILN EDGKKMSKRE NSSSVKWLLQ 250
    SGYLPEAIAN YLILLGNKTP CEVFTLDEAV EWFDISKISK NPAKFDISKL 300
    AFLNREHIKR ADSARLVEVF GLDESFSELI KFYTQEASLV GEIKEKIKSI 350
    FSKKEIPAEF AENVKILKDE ILKIKELPEN FENFKEILTK ATNLKGKNFF 400
    MPLRILLTGA NHGPELKELY PLLRSQIKRI VNL 433
    Length:433
    Mass (Da):49,568
    Last modified:September 11, 2007 - v1
    Checksum:i2F8E4B56B734C9AD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000776 Genomic DNA. Translation: ABS51058.1.
    RefSeqiWP_012109232.1. NC_009714.1.
    YP_001406929.1. NC_009714.1.

    Genome annotation databases

    EnsemblBacteriaiABS51058; ABS51058; CHAB381_1380.
    GeneIDi5408726.
    KEGGicha:CHAB381_1380.
    PATRICi20040876. VBICamHom81367_1332.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000776 Genomic DNA. Translation: ABS51058.1 .
    RefSeqi WP_012109232.1. NC_009714.1.
    YP_001406929.1. NC_009714.1.

    3D structure databases

    ProteinModelPortali A7I338.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 360107.CHAB381_1380.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABS51058 ; ABS51058 ; CHAB381_1380 .
    GeneIDi 5408726.
    KEGGi cha:CHAB381_1380.
    PATRICi 20040876. VBICamHom81367_1332.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci CHOM360107:GHCX-1384-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 genome sequence of Campylobacter hominis ATCC BAA-381, a commensal isolated from the human gastrointestinal tract."
      Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Nelson K.E.
      Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A.

    Entry informationi

    Entry nameiSYE2_CAMHC
    AccessioniPrimary (citable) accession number: A7I338
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 47 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