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P00953

- SYW_GEOSE

UniProt

P00953 - SYW_GEOSE

Protein

Tryptophan--tRNA ligase

Gene

trpS

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei195 – 1951ATPBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. tryptophanyl-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:
    Tryptophan--tRNA ligase (EC:6.1.1.2)
    Alternative name(s):
    Tryptophanyl-tRNA synthetase
    Short name:
    TrpRS
    Gene namesi
    Name:trpS
    OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    Taxonomic identifieri1422 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 328328Tryptophan--tRNA ligasePRO_0000136601Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    DIPiDIP-48697N.

    Structurei

    Secondary structure

    1
    328
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86
    Helixi16 – 216
    Helixi23 – 297
    Turni30 – 323
    Beta strandi33 – 397
    Helixi41 – 444
    Helixi51 – 6717
    Turni72 – 743
    Beta strandi75 – 795
    Helixi80 – 823
    Helixi85 – 9612
    Helixi99 – 1035
    Helixi106 – 1127
    Helixi120 – 1234
    Helixi125 – 13410
    Turni135 – 1373
    Beta strandi139 – 1424
    Helixi145 – 1473
    Helixi148 – 16518
    Beta strandi173 – 1753
    Beta strandi178 – 1825
    Helixi200 – 2023
    Helixi210 – 21910
    Turni232 – 2343
    Helixi236 – 24914
    Helixi253 – 2597
    Turni260 – 2623
    Helixi265 – 29127
    Helixi295 – 32228

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D2RX-ray2.90A/B/C/D/E/F1-326[»]
    1I6KX-ray1.72A1-328[»]
    1I6LX-ray1.72A1-328[»]
    1I6MX-ray1.72A1-328[»]
    1M83X-ray2.20A1-328[»]
    1MAUX-ray2.15A1-328[»]
    1MAWX-ray3.00A/B/C/D/E/F1-328[»]
    1MB2X-ray2.70A/B/C/D/E/F1-328[»]
    2OV4X-ray2.50A1-328[»]
    3FHJX-ray2.65A/B/C/D/E/F1-326[»]
    3FI0X-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R1-326[»]
    ProteinModelPortaliP00953.
    SMRiP00953. Positions 1-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00953.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi10 – 189"HIGH" region
    Motifi192 – 1965"KMSKS" region

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    HAMAPiMF_00140_B. Trp_tRNA_synth_B.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR002305. aa-tRNA-synth_Ic.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR002306. Trp-tRNA-ligase.
    IPR024109. Trp-tRNA-ligase_bac-type.
    [Graphical view]
    PANTHERiPTHR10055. PTHR10055. 1 hit.
    PfamiPF00579. tRNA-synt_1b. 1 hit.
    [Graphical view]
    PRINTSiPR01039. TRNASYNTHTRP.
    TIGRFAMsiTIGR00233. trpS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P00953-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTIFSGIQP SGVITIGNYI GALRQFVELQ HEYNCYFCIV DQHAITVWQD    50
    PHELRQNIRR LAAKYLAVGI DPTQATLFIQ SEVPAHAQAA WMLQCIVYIG 100
    ELERMTQFKE KSAGKEAVSA GLLTYPPLMA ADILLYNTDI VPVGEDQKQH 150
    IELTRDLAER FNKRYGELFT IPEARIPKVG ARIMSLVDPT KKMSKSDPNP 200
    KAYITLLDDA KTIEKKIKSA VTDSEGTIRY DKEAKPGISN LLNIYSTLSG 250
    QSIEELERQY EGKGYGVFKA DLAQVVIETL RPIQERYHHW MESEELDRVL 300
    DEGAEKANRV ASEMVRKMEQ AMGLGRRR 328
    Length:328
    Mass (Da):37,193
    Last modified:November 1, 1988 - v1
    Checksum:iB8C4C6028F0913B0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14742 Genomic DNA. Translation: AAA22873.1.
    PIRiA26055. YWBSF.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14742 Genomic DNA. Translation: AAA22873.1 .
    PIRi A26055. YWBSF.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D2R X-ray 2.90 A/B/C/D/E/F 1-326 [» ]
    1I6K X-ray 1.72 A 1-328 [» ]
    1I6L X-ray 1.72 A 1-328 [» ]
    1I6M X-ray 1.72 A 1-328 [» ]
    1M83 X-ray 2.20 A 1-328 [» ]
    1MAU X-ray 2.15 A 1-328 [» ]
    1MAW X-ray 3.00 A/B/C/D/E/F 1-328 [» ]
    1MB2 X-ray 2.70 A/B/C/D/E/F 1-328 [» ]
    2OV4 X-ray 2.50 A 1-328 [» ]
    3FHJ X-ray 2.65 A/B/C/D/E/F 1-326 [» ]
    3FI0 X-ray 2.70 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R 1-326 [» ]
    ProteinModelPortali P00953.
    SMRi P00953. Positions 1-328.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48697N.

    Chemistry

    DrugBanki DB00150. L-Tryptophan.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P00953.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    HAMAPi MF_00140_B. Trp_tRNA_synth_B.
    InterProi IPR001412. aa-tRNA-synth_I_CS.
    IPR002305. aa-tRNA-synth_Ic.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR002306. Trp-tRNA-ligase.
    IPR024109. Trp-tRNA-ligase_bac-type.
    [Graphical view ]
    PANTHERi PTHR10055. PTHR10055. 1 hit.
    Pfami PF00579. tRNA-synt_1b. 1 hit.
    [Graphical view ]
    PRINTSi PR01039. TRNASYNTHTRP.
    TIGRFAMsi TIGR00233. trpS. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and complete nucleotide sequence of the Bacillus stearothermophilus tryptophanyl tRNA synthetase gene."
      Barstow D.A., Sharman A.F., Atkinson T., Minton N.P.
      Gene 46:37-45(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The amino acid sequence of tryptophanyl tRNA synthetase from Bacillus stearothermophilus."
      Winter G.P., Hartley B.S.
      FEBS Lett. 80:340-342(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-327.
    3. "Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetase."
      Doublie S., Bricogne G., Gilmore C., Carter C.W. Jr.
      Structure 3:17-31(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
    4. "2.9-A crystal structure of ligand-free tryptophanyl-tRNA synthetase: domain movements fragment the adenine nucleotide binding site."
      Ilyin V.A., Temple B., Hu M., Li G.-P., Yin Y., Vachette P., Carter C.W. Jr.
      Protein Sci. 9:218-231(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).

    Entry informationi

    Entry nameiSYW_GEOSE
    AccessioniPrimary (citable) accession number: P00953
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: November 1, 1988
    Last modified: October 1, 2014
    This is version 101 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

    3D-structure, Direct protein sequencing

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3