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)

P46906

- SYR_BACSU

UniProt

P46906 - SYR_BACSU

Protein

Arginine--tRNA ligase

Gene

argS

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Enzyme and pathway databases

    BioCyciBSUB:BSU37330-MONOMER.

    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:BSU37330
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU37330. [Micado]

    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 – 556556Arginine--tRNA ligasePRO_0000151530Add
    BLAST

    Proteomic databases

    PaxDbiP46906.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    IntActiP46906. 1 interaction.
    MINTiMINT-8366397.
    STRINGi224308.BSU37330.

    Structurei

    3D structure databases

    ProteinModelPortaliP46906.
    SMRiP46906. Positions 1-556.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi132 – 14211"HIGH" regionAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0018.
    HOGENOMiHOG000247214.
    KOiK01887.
    OMAiMEHMGFG.
    OrthoDBiEOG6JB13C.
    PhylomeDBiP46906.

    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.

    P46906-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNIAEQMKDV LKEEIKAAVL KAGLAEESQI PNVVLETPKD KTHGDYSTNM    50
    AMQLARVAKK APRQIAEEIV AHFDKGKASI EKLDIAGPGF INFYMNNQYL 100
    TKLIPSVLEA GEAYGETNIG NGERVQVEFV SANPTGDLHL GHARGAAVGD 150
    SLCNVLSKAG YDVSREYYIN DAGNQINNLA LSVEVRYFEA LGLEKPMPED 200
    GYRGEDIIAI GKRLAEEYGD RFVNEEESER LAFFREYGLK YELEKLRKDL 250
    ENFRVPFDVW YSETSLYQNG KIDKALEALR EKGHVYEEDG ATWFRSTTFG 300
    DDKDRVLIKK DGTYTYLLPD IAYHKDKLDR GFDKLINVWG ADHHGYIPRM 350
    KAAIEALGYE KGTLEVEIIQ LVHLYKNGEK MKMSKRTGKA VTMRDLIEEV 400
    GLDAVRYFFA MRSADTHMDF DLDLAVSTSN ENPVYYAQYA HARICSMLRQ 450
    GEEQGLKPAA DLDFSHIQSE KEYDLLKTIG GFPEAVAEAA EKRIPHRVTN 500
    YIYDLASALH SFYNAEKVID PENEEKSRAR LALMKATQIT LNNALQLIGV 550
    SAPEKM 556
    Length:556
    Mass (Da):62,723
    Last modified:July 15, 1998 - v2
    Checksum:i0D92ED44E50BCD7F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z97024 Genomic DNA. Translation: CAB09703.1.
    AL009126 Genomic DNA. Translation: CAB15761.1.
    Z49884 Genomic DNA. Translation: CAA90040.1.
    PIRiE69589.
    RefSeqiNP_391614.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15761; CAB15761; BSU37330.
    GeneIDi937054.
    KEGGibsu:BSU37330.
    PATRICi18979504. VBIBacSub10457_3914.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z97024 Genomic DNA. Translation: CAB09703.1 .
    AL009126 Genomic DNA. Translation: CAB15761.1 .
    Z49884 Genomic DNA. Translation: CAA90040.1 .
    PIRi E69589.
    RefSeqi NP_391614.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P46906.
    SMRi P46906. Positions 1-556.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P46906. 1 interaction.
    MINTi MINT-8366397.
    STRINGi 224308.BSU37330.

    Proteomic databases

    PaxDbi P46906.

    Protocols and materials databases

    DNASUi 937054.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15761 ; CAB15761 ; BSU37330 .
    GeneIDi 937054.
    KEGGi bsu:BSU37330.
    PATRICi 18979504. VBIBacSub10457_3914.

    Organism-specific databases

    GenoListi BSU37330. [Micado ]

    Phylogenomic databases

    eggNOGi COG0018.
    HOGENOMi HOG000247214.
    KOi K01887.
    OMAi MEHMGFG.
    OrthoDBi EOG6JB13C.
    PhylomeDBi P46906.

    Enzyme and pathway databases

    BioCyci BSUB:BSU37330-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. "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)."
      Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P.
      Microbiology 143:3313-3328(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "Anaerobic transcription activation in Bacillus subtilis: identification of distinct FNR-dependent and -independent regulatory mechanisms."
      Cruz Ramos H., Boursier L., Moszer I., Kunst F., Danchin A., Glaser P.
      EMBO J. 14:5984-5994(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 442-556.
      Strain: 168.

    Entry informationi

    Entry nameiSYR_BACSU
    AccessioniPrimary (citable) accession number: P46906
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 113 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. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3