Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

C4ZQG0

- SYR_ECOBW

UniProt

C4ZQG0 - SYR_ECOBW

Protein

Arginine--tRNA ligase

Gene

argS

Organism
Escherichia coli (strain K12 / MC4100 / BW2952)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 37 (01 Oct 2014)
      Sequence version 1 (28 Jul 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).UniRule annotation

    GO - Molecular functioni

    1. arginine-tRNA ligase activity Source: UniProtKB-HAMAP
    2. ATP binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. arginyl-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

    BioCyciECOL595496:GI18-1742-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arginine--tRNA ligaseUniRule annotation (EC:6.1.1.19UniRule annotation)
    Alternative name(s):
    Arginyl-tRNA synthetaseUniRule annotation
    Short name:
    ArgRSUniRule annotation
    Gene namesi
    Name:argSUniRule annotation
    Ordered Locus Names:BWG_1690
    OrganismiEscherichia coli (strain K12 / MC4100 / BW2952)
    Taxonomic identifieri595496 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000001478: 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 – 577577Arginine--tRNA ligasePRO_1000203092Add
    BLAST

    Proteomic databases

    PRIDEiC4ZQG0.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi595496.BWG_1690.

    Structurei

    3D structure databases

    ProteinModelPortaliC4ZQG0.
    SMRiC4ZQG0. Positions 1-576.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi122 – 13211"HIGH" regionAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0018.
    HOGENOMiHOG000247212.
    KOiK01887.
    OMAiMEHMGFG.
    OrthoDBiEOG6JB13C.

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    3.30.1360.70. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPiMF_00123. Arg_tRNA_synth.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR001278. Arg-tRNA-ligase.
    IPR005148. Arg-tRNA-synth_N.
    IPR008909. DALR_anticod-bd.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    [Graphical view]
    PANTHERiPTHR11956. PTHR11956. 1 hit.
    PfamiPF03485. Arg_tRNA_synt_N. 1 hit.
    PF05746. DALR_1. 1 hit.
    PF00750. tRNA-synt_1d. 1 hit.
    [Graphical view]
    PRINTSiPR01038. TRNASYNTHARG.
    SMARTiSM01016. Arg_tRNA_synt_N. 1 hit.
    SM00836. DALR_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF47323. SSF47323. 1 hit.
    SSF55190. SSF55190. 1 hit.
    TIGRFAMsiTIGR00456. argS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    C4ZQG0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNIQALLSEK VRQAMIAAGA PADCEPQVRQ SAKVQFGDYQ ANGMMAVAKK    50
    LGMAPRQLAE QVLTHLDLNG IASKVEIAGP GFINIFLDPA FLAEHVQQAL 100
    ASDRLGVATP EKQTIVVDYS APNVAKEMHV GHLRSTIIGD AAVRTLEFLG 150
    HKVIRANHVG DWGTQFGMLI AWLEKQQQEN AGEMELADLE GFYRDAKKHY 200
    DEDEEFAERA RNYVVKLQSG DEYFREMWRK LVDITMTQNQ ITYDRLNVTL 250
    TRDDVMGESL YNPMLPGIVA DLKAKGLAVE SEGATVVFLD EFKNKEGEPM 300
    GVIIQKKDGG YLYTTTDIAC AKYRYETLHA DRVLYYIDSR QHQHLMQAWA 350
    IVRKAGYVPE SVPLEHHMFG MMLGKDGKPF KTRAGGTVKL ADLLDEALER 400
    ARRLVAEKNP DMPADELEKL ANAVGIGAVK YADLSKNRTT DYIFDWDNML 450
    AFEGNTAPYM QYAYTRVLSV FRKAEIDEEQ LAAAPVIIRE DREAQLAARL 500
    LQFEETLTVV AREGTPHVMC AYLYDLAGLF SGFYEHCPIL SAENEEVRNS 550
    RLKLAQLTAK TLKLGLDTLG IETVERM 577
    Length:577
    Mass (Da):64,683
    Last modified:July 28, 2009 - v1
    Checksum:iC107D346660CF9B8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001396 Genomic DNA. Translation: ACR62012.1.
    RefSeqiYP_002926887.1. NC_012759.1.

    Genome annotation databases

    EnsemblBacteriaiACR62012; ACR62012; BWG_1690.
    GeneIDi7955146.
    KEGGiebw:BWG_1690.
    PATRICi18272627. VBIEscCol60876_1846.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001396 Genomic DNA. Translation: ACR62012.1 .
    RefSeqi YP_002926887.1. NC_012759.1.

    3D structure databases

    ProteinModelPortali C4ZQG0.
    SMRi C4ZQG0. Positions 1-576.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 595496.BWG_1690.

    Proteomic databases

    PRIDEi C4ZQG0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACR62012 ; ACR62012 ; BWG_1690 .
    GeneIDi 7955146.
    KEGGi ebw:BWG_1690.
    PATRICi 18272627. VBIEscCol60876_1846.

    Phylogenomic databases

    eggNOGi COG0018.
    HOGENOMi HOG000247212.
    KOi K01887.
    OMAi MEHMGFG.
    OrthoDBi EOG6JB13C.

    Enzyme and pathway databases

    BioCyci ECOL595496:GI18-1742-MONOMER.

    Family and domain databases

    Gene3Di 1.10.730.10. 1 hit.
    3.30.1360.70. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPi MF_00123. Arg_tRNA_synth.
    InterProi IPR001412. aa-tRNA-synth_I_CS.
    IPR001278. Arg-tRNA-ligase.
    IPR005148. Arg-tRNA-synth_N.
    IPR008909. DALR_anticod-bd.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    [Graphical view ]
    PANTHERi PTHR11956. PTHR11956. 1 hit.
    Pfami PF03485. Arg_tRNA_synt_N. 1 hit.
    PF05746. DALR_1. 1 hit.
    PF00750. tRNA-synt_1d. 1 hit.
    [Graphical view ]
    PRINTSi PR01038. TRNASYNTHARG.
    SMARTi SM01016. Arg_tRNA_synt_N. 1 hit.
    SM00836. DALR_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47323. SSF47323. 1 hit.
    SSF55190. SSF55190. 1 hit.
    TIGRFAMsi TIGR00456. argS. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic sequencing reveals regulatory mutations and recombinational events in the widely used MC4100 lineage of Escherichia coli K-12."
      Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R., Wang L.
      J. Bacteriol. 191:4025-4029(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MC4100 / BW2952.

    Entry informationi

    Entry nameiSYR_ECOBW
    AccessioniPrimary (citable) accession number: C4ZQG0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 37 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