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P27001

- SYFA_THETH

UniProt

P27001 - SYFA_THETH

Protein

Phenylalanine--tRNA ligase alpha subunit

Gene

pheS

Organism
Thermus thermophilus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).

    Cofactori

    Binds 2 magnesium ions per tetramer.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi262 – 2621Magnesium

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. magnesium ion binding Source: UniProtKB-HAMAP
    3. phenylalanine-tRNA ligase activity Source: UniProtKB-HAMAP
    4. tRNA binding Source: InterPro

    GO - Biological processi

    1. phenylalanyl-tRNA aminoacylation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phenylalanine--tRNA ligase alpha subunit (EC:6.1.1.20)
    Alternative name(s):
    Phenylalanyl-tRNA synthetase alpha subunit
    Short name:
    PheRS
    Gene namesi
    Name:pheS
    OrganismiThermus thermophilus
    Taxonomic identifieri274 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 350350Phenylalanine--tRNA ligase alpha subunitPRO_0000126786Add
    BLAST

    Interactioni

    Subunit structurei

    Tetramer of two alpha and two beta subunits.

    Protein-protein interaction databases

    DIPiDIP-6104N.
    MINTiMINT-88286.
    STRINGi262724.TTC1594.

    Structurei

    Secondary structure

    1
    350
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi16 – 3116
    Turni39 – 413
    Helixi42 – 443
    Helixi49 – 6113
    Helixi63 – 7311
    Helixi76 – 838
    Beta strandi88 – 903
    Helixi102 – 11514
    Turni116 – 1183
    Beta strandi126 – 1294
    Helixi130 – 1334
    Turni134 – 1385
    Beta strandi141 – 1433
    Turni144 – 1474
    Beta strandi153 – 1553
    Beta strandi173 – 1753
    Beta strandi177 – 1793
    Helixi181 – 1899
    Beta strandi192 – 20312
    Beta strandi214 – 22512
    Helixi230 – 24415
    Beta strandi251 – 2555
    Beta strandi261 – 27111
    Turni272 – 2754
    Beta strandi276 – 28611
    Helixi288 – 30013
    Beta strandi307 – 3093
    Beta strandi311 – 3188
    Helixi319 – 3268
    Helixi332 – 3343
    Turni335 – 3373
    Helixi340 – 3434
    Helixi344 – 3463

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B70X-ray2.70A1-350[»]
    1B7YX-ray2.50A1-350[»]
    2AKWX-ray2.80A85-350[»]
    2ALYX-ray2.60A85-350[»]
    2AMCX-ray2.70A85-350[»]
    2IY5X-ray3.10A1-350[»]
    3TEHX-ray2.85A1-350[»]
    DisProtiDP00053.
    ProteinModelPortaliP27001.
    SMRiP27001. Positions 6-350.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27001.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    HAMAPiMF_00281. Phe_tRNA_synth_alpha1.
    InterProiIPR006195. aa-tRNA-synth_II.
    IPR004529. Phe-tRNA-synth_IIc_asu.
    IPR004188. Phe-tRNA_ligase_II_N.
    IPR022911. Phe_tRNA_ligase_alpha1_bac.
    IPR002319. Phenylalanyl-tRNA_Synthase.
    IPR010978. tRNA-bd_arm.
    [Graphical view]
    PfamiPF02912. Phe_tRNA-synt_N. 1 hit.
    PF01409. tRNA-synt_2d. 1 hit.
    [Graphical view]
    SUPFAMiSSF46589. SSF46589. 1 hit.
    TIGRFAMsiTIGR00468. pheS. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P27001-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLEEALAAIQ NARDLEELKA LKARYLGKKG LLTQEMKGLS ALPLEERRKR    50
    GQELNAIKAA LEAALEAREK ALEEAALKEA LERERVDVSL PGASLFSGGL 100
    HPITLMEREL VEIFRALGYQ AVEGPEVESE FFNFDALNIP EHHPARDMWD 150
    TFWLTGEGFR LEGPLGEEVE GRLLLRTHTS PMQVRYMVAH TPPFRIVVPG 200
    RVFRFEQTDA THEAVFHQLE GLVVGEGIAM AHLKGAIYEL AQALFGPDSK 250
    VRFQPVYFPF VEPGAQFAVW WPEGGKWLEL GGAGMVHPKV FQAVDAYRER 300
    LGLPPAYRGV TGFAFGLGVE RLAMLRYGIP DIRYFFGGRL KFLEQFKGVL 350
    Length:350
    Mass (Da):39,259
    Last modified:August 1, 1992 - v1
    Checksum:iDEE0237F7CD9A461
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B70 X-ray 2.70 A 1-350 [» ]
    1B7Y X-ray 2.50 A 1-350 [» ]
    2AKW X-ray 2.80 A 85-350 [» ]
    2ALY X-ray 2.60 A 85-350 [» ]
    2AMC X-ray 2.70 A 85-350 [» ]
    2IY5 X-ray 3.10 A 1-350 [» ]
    3TEH X-ray 2.85 A 1-350 [» ]
    DisProti DP00053.
    ProteinModelPortali P27001.
    SMRi P27001. Positions 6-350.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6104N.
    MINTi MINT-88286.
    STRINGi 262724.TTC1594.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P27001.

    Family and domain databases

    HAMAPi MF_00281. Phe_tRNA_synth_alpha1.
    InterProi IPR006195. aa-tRNA-synth_II.
    IPR004529. Phe-tRNA-synth_IIc_asu.
    IPR004188. Phe-tRNA_ligase_II_N.
    IPR022911. Phe_tRNA_ligase_alpha1_bac.
    IPR002319. Phenylalanyl-tRNA_Synthase.
    IPR010978. tRNA-bd_arm.
    [Graphical view ]
    Pfami PF02912. Phe_tRNA-synt_N. 1 hit.
    PF01409. tRNA-synt_2d. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46589. SSF46589. 1 hit.
    TIGRFAMsi TIGR00468. pheS. 1 hit.
    PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Crystal structures of phenylalanyl-tRNA synthetase complexed with phenylalanine and a phenylalanyl-adenylate analogue."
      Reshetnikova L., Moor N., Lavrik O., Vassylyev D.G.
      J. Mol. Biol. 287:555-568(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

    Entry informationi

    Entry nameiSYFA_THETH
    AccessioniPrimary (citable) accession number: P27001
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 104 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    The sequence shown here has been extracted from PDB entry 1B70.Curated

    Keywords - Technical termi

    3D-structure

    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