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P40329

- SYRC_RAT

UniProt

P40329 - SYRC_RAT

Protein

Arginine--tRNA ligase, cytoplasmic

Gene

Rars

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 2 (13 Jul 2010)
      Previous versions | rss
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    Functioni

    Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1 By similarity.By similarity

    Catalytic activityi

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

    GO - Molecular functioni

    1. arginine binding Source: RGD
    2. arginine-tRNA ligase activity Source: RGD
    3. ATP binding Source: RGD
    4. tRNA binding Source: RGD

    GO - Biological processi

    1. arginyl-tRNA aminoacylation Source: RGD

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_212517. Cytosolic tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arginine--tRNA ligase, cytoplasmic (EC:6.1.1.19)
    Alternative name(s):
    Arginyl-tRNA synthetase
    Short name:
    ArgRS
    Gene namesi
    Name:Rars
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 10

    Organism-specific databases

    RGDi1309215. Rars.

    Subcellular locationi

    GO - Cellular componenti

    1. aminoacyl-tRNA synthetase multienzyme complex Source: RGD
    2. mitochondrion Source: Ensembl
    3. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 660660Arginine--tRNA ligase, cytoplasmicPRO_0000151660Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP40329.

    Expressioni

    Gene expression databases

    GenevestigatoriP40329.

    Interactioni

    Subunit structurei

    Interacts (via N-terminus) with AIMP1 (via N-terminus); this stimulates its catalytic activity. Interacts with EPRS (via N-terminus). Interacts with LARS2. Monomer; also part of a multisubunit complex that groups tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro By similarity. Interacts with QARS By similarity.By similarity

    Protein-protein interaction databases

    BioGridi252058. 1 interaction.
    STRINGi10116.ENSRNOP00000010252.

    Structurei

    3D structure databases

    ProteinModelPortaliP40329.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 7272Could be involved in the assembly of the multisynthetase complexBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi201 – 21212"HIGH" regionBy similarityAdd
    BLAST

    Domaini

    The N-terminus (AA 1-72) has two regions predicted to be alpha-helical that might be involved in the multisynthetase complex assembly.By similarity

    Sequence similaritiesi

    Phylogenomic databases

    GeneTreeiENSGT00530000063407.
    HOGENOMiHOG000247212.
    HOVERGENiHBG029238.
    KOiK01887.
    OMAiKCFDILG.
    OrthoDBiEOG764725.
    PhylomeDBiP40329.
    TreeFamiTF106111.

    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.

    P40329-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDGLVAQCSA RLLQQEKEIK SLTAEIDRLK NCSYLEASPS LEQLREENLK    50
    LKYRLNILRR SLQAERKRPT KNMININSRL QELFGCAIKA AYPDLENPPL 100
    VVTPSQQPKF GDYQCNSAMG ISQMLKAKEQ KVSPREIAEN ITKHLPNNEY 150
    IDRVEIAGPG FINVHLRKDF VSEQLTNLLV NGVQLPVLGE NEKVIVDFSS 200
    PNIAKEMHVG HLRSTIIGES MSRLFEFAGY NVLRLNHVGD WGTQFGMLIA 250
    HLQDKFPDYL TVSPPIGDLQ AFYKESKKRF DTEEEFKKRA YECVVLLQSK 300
    NPDIMKAWNL ICDVSREEFN KIYDALDITL IERGESFYQD RMKDIVKEFE 350
    DKGFVQVDDG RKIVFVPGCS VPLTIVKSDG GYTYDTSDLA AIKQRLFEEK 400
    ANKIIYVVDN GQATHFQTVF AAAQMIGWYD PKVTRVAHVG FGVVLGEDKK 450
    KFKTRSGETV RLMDLLEEGL RRSMDKLKEK ERDKVLTEEE LKAAQTSVAY 500
    GCIKYADLSH NRLNDYVFSF DKMLDDRGNT AAYLLYAFTR IRSIARLANI 550
    DEEMLQRAAR ETKIILDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY 600
    IYELATTFTE FYDSCYCVEK DRQTGKVLKV NMWRMLLCEA VAAVMAKGFD 650
    ILGIKPVQRM 660
    Length:660
    Mass (Da):75,810
    Last modified:July 13, 2010 - v2
    Checksum:i3C2D718AECDC4655
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC161929 mRNA. Translation: AAI61929.1.
    PIRiA35857.
    RefSeqiNP_001099247.2. NM_001105777.2.
    UniGeneiRn.18711.

    Genome annotation databases

    EnsembliENSRNOT00000010252; ENSRNOP00000010252; ENSRNOG00000007739.
    GeneIDi287191.
    KEGGirno:287191.
    UCSCiRGD:1309215. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC161929 mRNA. Translation: AAI61929.1 .
    PIRi A35857.
    RefSeqi NP_001099247.2. NM_001105777.2.
    UniGenei Rn.18711.

    3D structure databases

    ProteinModelPortali P40329.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 252058. 1 interaction.
    STRINGi 10116.ENSRNOP00000010252.

    Proteomic databases

    PRIDEi P40329.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000010252 ; ENSRNOP00000010252 ; ENSRNOG00000007739 .
    GeneIDi 287191.
    KEGGi rno:287191.
    UCSCi RGD:1309215. rat.

    Organism-specific databases

    CTDi 5917.
    RGDi 1309215. Rars.

    Phylogenomic databases

    GeneTreei ENSGT00530000063407.
    HOGENOMi HOG000247212.
    HOVERGENi HBG029238.
    KOi K01887.
    OMAi KCFDILG.
    OrthoDBi EOG764725.
    PhylomeDBi P40329.
    TreeFami TF106111.

    Enzyme and pathway databases

    Reactomei REACT_212517. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    NextBioi 625686.

    Gene expression databases

    Genevestigatori P40329.

    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. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Brown Norway/NHsdMcwi.
      Tissue: Liver.
    2. "Existence of two forms of rat liver arginyl-tRNA synthetase suggests channeling of aminoacyl-tRNA for protein synthesis."
      Sivaram P., Deutscher M.P.
      Proc. Natl. Acad. Sci. U.S.A. 87:3665-3669(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 73-92.

    Entry informationi

    Entry nameiSYRC_RAT
    AccessioniPrimary (citable) accession number: P40329
    Secondary accession number(s): B1WBX8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: July 13, 2010
    Last modified: October 1, 2014
    This is version 79 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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