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P35868

- SYR_CORGL

UniProt

P35868 - SYR_CORGL

Protein

Arginine--tRNA ligase

Gene

argS

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arginine--tRNA ligase (EC:6.1.1.19)
    Alternative name(s):
    Arginyl-tRNA synthetase
    Short name:
    ArgRS
    Gene namesi
    Name:argS
    Ordered Locus Names:Cgl1179, cg1333
    OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
    Taxonomic identifieri196627 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
    ProteomesiUP000000582: Chromosome, UP000001009: Chromosome

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 550550Arginine--tRNA ligasePRO_0000151554Add
    BLAST

    Expressioni

    Inductioni

    Up-regulated by arginine and repressed by lysine.1 Publication

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi196627.cg1333.

    Structurei

    3D structure databases

    ProteinModelPortaliP35868.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi130 – 14011"HIGH" regionAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0018.
    KOiK01887.
    OMAiQQEVFRS.
    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.

    P35868-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTPADLATLI KETAVEVLTS RELDTSVLPE QVVVERPRNP EHGDYATNIA    50
    LQVAKKVGQN PRDLATWLAE ALAADDAIDS AEIAGPGFLN IRLAAAAQGE 100
    IVAKILAQGE TFGNSDHLSH LDVNLEFVSA NPTGPIHLGG TRWAAVGDSL 150
    GRVLEASGAK VTREYYFNDH GRQIDRFALS LLAAAKGEPT PEDGYGGEYI 200
    KEIAEAIVEK HPEALALEPA ATQELFRAEG VEMMFEHIKS SLHEFGTDFD 250
    VYYHENSLFE SGAVDKAVQV LKDNGNLYEN EGAWWLRSTE FGDDKDRVVI 300
    KSDGDAAYIA GDIAYVADKF SRGHNLNIYM LGADHHGYIA RLKAAAAALG 350
    YKPEGVEVLI GQMVNLLRDG KAVRMSKRAG TVVTLDDLVE AIGIDAARYS 400
    LIRSSVDSSL DIDLGLWESQ SSDNPVYYVQ YGHARLCSIA RKAETLGVTE 450
    EGADLSLLTH DREGDLIRTL GEFPAVVKAA ADLREPHRIA RYAEELAGTF 500
    HRFYDSCHIL PKVDEDTAPI HTARLALAAA TRQTLANALH LVGVSAPEKM 550
    Length:550
    Mass (Da):59,723
    Last modified:February 1, 1996 - v2
    Checksum:i3AF724BDEE8DC4C1
    GO

    Sequence cautioni

    The sequence CAA38537.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti355 – 3551G → D in CAA79710. (PubMed:8226683)Curated
    Sequence conflicti412 – 4121I → M in CAA79710. (PubMed:8226683)Curated
    Sequence conflicti513 – 5131V → A in CAA79710. (PubMed:8226683)Curated
    Sequence conflicti540 – 5401H → R in CAA79710. (PubMed:8226683)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54740 Genomic DNA. Translation: CAA38537.1. Different initiation.
    Z21501 Genomic DNA. Translation: CAA79710.1.
    BA000036 Genomic DNA. Translation: BAB98572.1.
    BX927151 Genomic DNA. Translation: CAF19883.1.
    PIRiA49936.
    S12227.
    RefSeqiNP_600405.1. NC_003450.3.
    YP_225469.1. NC_006958.1.

    Genome annotation databases

    EnsemblBacteriaiBAB98572; BAB98572; BAB98572.
    CAF19883; CAF19883; cg1333.
    GeneIDi1019162.
    KEGGicgb:cg1333.
    cgl:NCgl1132.
    PATRICi21494404. VBICorGlu203724_1158.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54740 Genomic DNA. Translation: CAA38537.1 . Different initiation.
    Z21501 Genomic DNA. Translation: CAA79710.1 .
    BA000036 Genomic DNA. Translation: BAB98572.1 .
    BX927151 Genomic DNA. Translation: CAF19883.1 .
    PIRi A49936.
    S12227.
    RefSeqi NP_600405.1. NC_003450.3.
    YP_225469.1. NC_006958.1.

    3D structure databases

    ProteinModelPortali P35868.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 196627.cg1333.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB98572 ; BAB98572 ; BAB98572 .
    CAF19883 ; CAF19883 ; cg1333 .
    GeneIDi 1019162.
    KEGGi cgb:cg1333.
    cgl:NCgl1132.
    PATRICi 21494404. VBICorGlu203724_1158.

    Phylogenomic databases

    eggNOGi COG0018.
    KOi K01887.
    OMAi QQEVFRS.
    OrthoDBi EOG6JB13C.

    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. "Nucleotide sequence and organization of the upstream region of the Corynebacterium glutamicum lysA gene."
      Marcel T., Archer J.A.C., Mengin-Lecreulx D., Sinskey A.J.
      Mol. Microbiol. 4:1819-1830(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613.
    2. "A gene encoding arginyl-tRNA synthetase is located in the upstream region of the lysA gene in Brevibacterium lactofermentum: regulation of argS-lysA cluster expression by arginine."
      Oguiza J.A., Malumbres M., Eriani G., Pisabarro A., Mateos L.M., Martin F., Martin J.F.
      J. Bacteriol. 175:7356-7362(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
      Strain: ATCC 13869 / DSMZ 1412 / NCIMB 9567.
    3. "The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
      Ikeda M., Nakagawa S.
      Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
    5. "Corynebacterium glutamicum arginyl-tRNA synthetase."
      Sharp P.M., Mitchell K.J.
      Mol. Microbiol. 8:200-200(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.

    Entry informationi

    Entry nameiSYR_CORGL
    AccessioniPrimary (citable) accession number: P35868
    Secondary accession number(s): P41253
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 111 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, 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