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P15625

- SYFA_YEAST

UniProt

P15625 - SYFA_YEAST

Protein

Phenylalanine--tRNA ligase alpha subunit

Gene

FRS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phenylalanine-tRNA ligase activity Source: UniProtKB-EC
    3. protein binding Source: IntAct
    4. tRNA binding Source: InterPro

    GO - Biological processi

    1. phenylalanyl-tRNA aminoacylation Source: SGD

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30438-MONOMER.

    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:FRS2
    Ordered Locus Names:YFL022C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VI

    Organism-specific databases

    SGDiS000001872. FRS2.

    Subcellular locationi

    GO - Cellular componenti

    1. phenylalanine-tRNA ligase complex Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 503502Phenylalanine--tRNA ligase alpha subunitPRO_0000126828Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP15625.
    PaxDbiP15625.
    PeptideAtlasiP15625.

    Expressioni

    Gene expression databases

    GenevestigatoriP15625.

    Interactioni

    Subunit structurei

    Tetramer of two alpha and two beta subunits.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FRS1P156243EBI-18678,EBI-18684

    Protein-protein interaction databases

    BioGridi31124. 25 interactions.
    DIPiDIP-5428N.
    IntActiP15625. 7 interactions.
    MINTiMINT-479586.
    STRINGi4932.YFL022C.

    Structurei

    3D structure databases

    ProteinModelPortaliP15625.
    SMRiP15625. Positions 155-500.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 173172Contains the major tRNA-Phe binding sitesAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0016.
    GeneTreeiENSGT00390000006387.
    HOGENOMiHOG000230294.
    KOiK01889.
    OMAiHEESFRT.
    OrthoDBiEOG7BGHVT.

    Family and domain databases

    InterProiIPR006195. aa-tRNA-synth_II.
    IPR004529. Phe-tRNA-synth_IIc_asu.
    IPR002319. Phenylalanyl-tRNA_Synthase.
    [Graphical view]
    PfamiPF01409. tRNA-synt_2d. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00468. pheS. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P15625-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDFQLEILK KLDELDEIKS TLATFPQHGS QDVLSALNSL KAHNKLEFSK    50
    VDTVTYDLTK EGAQILNEGS YEIKLVKLIQ ELGQLQIKDV MSKLGPQVGK 100
    VGQARAFKNG WIAKNASNEL ELSAKLQNTD LNELTDETQS ILAQIKNNSH 150
    LDSIDAKILN DLKKRKLIAQ GKITDFNVTK GPEFSTDLTK LETDLTSDMV 200
    STNAYKDLKF KPYNFNSQGV QISSGALHPL NKVREEFRQI FFSMGFTEMP 250
    SNQYVETGFW NFDALYVPQQ HPARDLQDTF YIKDPLTADL PDDKTYMDNI 300
    KAVHEQGRFG SIGYRYNWKP EECQKLVLRT HSTAISARML HDLAKDPKPT 350
    RLFSIDRVFR NEAVDATHLA EFHQVEGVLA DYNITLGDLI KFMEEFFERM 400
    GVTGLRFKPT YNPYTEPSME IFSWHEGLQK WVEIGNSGMF RPEMLESMGL 450
    PKDLRVLGWG LSLERPTMIK YKVQNIRELL GHKVSLDFIE TNPAARLDED 500
    LYE 503
    Length:503
    Mass (Da):57,511
    Last modified:January 23, 2007 - v3
    Checksum:i50B7EAC675AB559B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti177 – 1771N → S in AAA35152. (PubMed:3049607)Curated
    Sequence conflicti289 – 2891D → E in AAA35152. (PubMed:3049607)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03965 Genomic DNA. Translation: AAA35152.1.
    D50617 Genomic DNA. Translation: BAA09216.1.
    BK006940 Genomic DNA. Translation: DAA12418.1.
    PIRiS56232. YFBYAC.
    RefSeqiNP_116631.1. NM_001179944.2.

    Genome annotation databases

    EnsemblFungiiYFL022C; YFL022C; YFL022C.
    GeneIDi850522.
    KEGGisce:YFL022C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03965 Genomic DNA. Translation: AAA35152.1 .
    D50617 Genomic DNA. Translation: BAA09216.1 .
    BK006940 Genomic DNA. Translation: DAA12418.1 .
    PIRi S56232. YFBYAC.
    RefSeqi NP_116631.1. NM_001179944.2.

    3D structure databases

    ProteinModelPortali P15625.
    SMRi P15625. Positions 155-500.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31124. 25 interactions.
    DIPi DIP-5428N.
    IntActi P15625. 7 interactions.
    MINTi MINT-479586.
    STRINGi 4932.YFL022C.

    Proteomic databases

    MaxQBi P15625.
    PaxDbi P15625.
    PeptideAtlasi P15625.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YFL022C ; YFL022C ; YFL022C .
    GeneIDi 850522.
    KEGGi sce:YFL022C.

    Organism-specific databases

    SGDi S000001872. FRS2.

    Phylogenomic databases

    eggNOGi COG0016.
    GeneTreei ENSGT00390000006387.
    HOGENOMi HOG000230294.
    KOi K01889.
    OMAi HEESFRT.
    OrthoDBi EOG7BGHVT.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30438-MONOMER.

    Miscellaneous databases

    NextBioi 966257.
    PROi P15625.

    Gene expression databases

    Genevestigatori P15625.

    Family and domain databases

    InterProi IPR006195. aa-tRNA-synth_II.
    IPR004529. Phe-tRNA-synth_IIc_asu.
    IPR002319. Phenylalanyl-tRNA_Synthase.
    [Graphical view ]
    Pfami PF01409. tRNA-synt_2d. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00468. pheS. 1 hit.
    PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and expression of the genes encoding the alpha and beta subunits of yeast phenylalanyl-tRNA synthetase."
      Sanni A., Mirande M., Ebel J.-P., Boulanger Y., Waller J.-P., Fasiolo F.
      J. Biol. Chem. 263:15407-15415(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Identification of the major tRNA(Phe) binding domain in the tetrameric structure of cytoplasmic phenylalanyl-tRNA synthetase from baker's yeast."
      Fasiolo F., Sanni A., Potier S., Ebel J.-P., Boulanger Y.
      FEBS Lett. 242:351-356(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, DOMAIN TRNA-BINDING.
    5. "Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
      Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.
      Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT SER-2.

    Entry informationi

    Entry nameiSYFA_YEAST
    AccessioniPrimary (citable) accession number: P15625
    Secondary accession number(s): D6VTK8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 144 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally erroneously assigned as a beta subunit.1 Publication

    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
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome VI
      Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

    External Data

    Dasty 3