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Q10119

- EF1A2_SCHPO

UniProt

Q10119 - EF1A2_SCHPO

Protein

Elongation factor 1-alpha-B/C

Gene

tef1b

more
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi14 – 218GTPBy similarity
    Nucleotide bindingi91 – 955GTPBy similarity
    Nucleotide bindingi153 – 1564GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: InterPro
    2. GTP binding Source: UniProtKB-KW
    3. translation elongation factor activity Source: PomBase

    GO - Biological processi

    1. cytoplasmic translational elongation Source: PomBase
    2. translational elongation Source: PomBase

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_202295. HSF1 activation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation factor 1-alpha-B/C
    Short name:
    EF-1-alpha-B/C
    Gene namesi
    Name:tef1b
    Synonyms:ef1a-b
    ORF Names:SPAC23A1.10
    AND
    Name:tef1c
    Synonyms:ef1a-c, tef1d
    ORF Names:SPBC24E9.15c, SPBC839.15c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I, UP000002485: Chromosome II

    Organism-specific databases

    PomBaseiSPAC23A1.10.
    SPBC839.15c.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: PomBase
    2. eukaryotic translation elongation factor 1 complex Source: PomBase
    3. nucleus Source: PomBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 460460Elongation factor 1-alpha-B/CPRO_0000090969Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei23 – 231Phosphothreonine1 Publication
    Modified residuei24 – 241Phosphothreonine1 Publication
    Modified residuei158 – 1581Phosphothreonine1 Publication
    Modified residuei289 – 2891Phosphoserine1 Publication
    Modified residuei296 – 2961Phosphoserine1 Publication
    Modified residuei314 – 3141Phosphoserine1 Publication
    Modified residuei388 – 3881Phosphoserine1 Publication
    Modified residuei394 – 3941Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ10119.
    PRIDEiQ10119.

    Interactioni

    Protein-protein interaction databases

    BioGridi276461. 7 interactions.
    278469. 7 interactions.
    IntActiQ10119. 1 interaction.
    MINTiMINT-4697049.
    STRINGi4896.SPBC839.15c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ10119.
    SMRiQ10119. Positions 2-441.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 240236tr-type GAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni14 – 218G1By similarity
    Regioni70 – 745G2By similarity
    Regioni91 – 944G3By similarity
    Regioni153 – 1564G4By similarity
    Regioni192 – 1943G5By similarity

    Sequence similaritiesi

    Phylogenomic databases

    HOGENOMiHOG000229291.
    KOiK03231.
    OMAiVWHPSAI.
    OrthoDBiEOG715QCW.
    PhylomeDBiQ10119.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00118_A. EF_Tu_A.
    InterProiIPR000795. EF_GTP-bd_dom.
    IPR027417. P-loop_NTPase.
    IPR009000. Transl_B-barrel.
    IPR009001. Transl_elong_EF1A/Init_IF2_C.
    IPR004539. Transl_elong_EF1A_euk/arc.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    IPR004160. Transl_elong_EFTu/EF1A_C.
    [Graphical view]
    PfamiPF00009. GTP_EFTU. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    PF03143. GTP_EFTU_D3. 1 hit.
    [Graphical view]
    PRINTSiPR00315. ELONGATNFCT.
    SUPFAMiSSF50447. SSF50447. 1 hit.
    SSF50465. SSF50465. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00483. EF-1_alpha. 1 hit.
    PROSITEiPS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q10119-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKEKGHINV VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEATELG    50
    KGSFKYAWVL DKLKAERERG ITIDIALWKF ETPKYNVTVI DAPGHRDFIK 100
    NMITGTSQAD CAILIIGGGT GEFEAGISKD GQTREHALLA YTLGVKQLIV 150
    AVNKMDTTGW SQARFEEIVK ETSNFIKKVG FNPKTVPFVP VSGFQGDNMI 200
    EPTTNMPWYQ GWQKETKAGV VKGKTLLEAI DSIEPPARPT DKPLRLPLQD 250
    VYKIGGIGTV PVGRVETGVI KPGMIVTFAP AGVTTEVKSV EMHHESLDAG 300
    LPGDNVGFNV KNVSVKDIRR GNVCGDSKND PPMGCASFTA QVIILNHPGQ 350
    ISAGYSPVLD CHTAHIACKF AELIEKIDRR SGKKIEESPK FVKSGDACIA 400
    KMVPSKPMCV EAFTDYAPLG RFAVRDMRQT VAVGVIKAVE KVAPGAAKVT 450
    KAAVKAGAKK 460
    Length:460
    Mass (Da):49,675
    Last modified:November 1, 1996 - v1
    Checksum:i2D8429568A5F98D4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211S → F in BAA11571. (PubMed:9099890)Curated
    Sequence conflicti139 – 1391L → R in BAA11571. (PubMed:9099890)Curated
    Sequence conflicti139 – 1391L → V in BAA19867. (PubMed:9501991)Curated
    Sequence conflicti388 – 3881S → A in AAP86554. (PubMed:12748053)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D82572 mRNA. Translation: BAA11570.1.
    D82573 mRNA. Translation: BAA11571.1.
    D89112 mRNA. Translation: BAA19867.1.
    CU329670 Genomic DNA. Translation: CAA16984.1.
    CU329671 Genomic DNA. Translation: CAB46708.1.
    AF402093 Genomic DNA. Translation: AAP86554.1.
    PIRiB41453.
    T38230.
    T42089.
    RefSeqiNP_594440.1. NM_001019869.2.
    NP_595255.1. NM_001021161.2.

    Genome annotation databases

    EnsemblFungiiSPAC23A1.10.1; SPAC23A1.10.1:pep; SPAC23A1.10.
    SPBC839.15c.1; SPBC839.15c.1:pep; SPBC839.15c.
    GeneIDi2539917.
    2541984.
    KEGGispo:SPAC23A1.10.
    spo:SPBC839.15c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D82572 mRNA. Translation: BAA11570.1 .
    D82573 mRNA. Translation: BAA11571.1 .
    D89112 mRNA. Translation: BAA19867.1 .
    CU329670 Genomic DNA. Translation: CAA16984.1 .
    CU329671 Genomic DNA. Translation: CAB46708.1 .
    AF402093 Genomic DNA. Translation: AAP86554.1 .
    PIRi B41453.
    T38230.
    T42089.
    RefSeqi NP_594440.1. NM_001019869.2.
    NP_595255.1. NM_001021161.2.

    3D structure databases

    ProteinModelPortali Q10119.
    SMRi Q10119. Positions 2-441.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 276461. 7 interactions.
    278469. 7 interactions.
    IntActi Q10119. 1 interaction.
    MINTi MINT-4697049.
    STRINGi 4896.SPBC839.15c-1.

    Proteomic databases

    MaxQBi Q10119.
    PRIDEi Q10119.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC23A1.10.1 ; SPAC23A1.10.1:pep ; SPAC23A1.10 .
    SPBC839.15c.1 ; SPBC839.15c.1:pep ; SPBC839.15c .
    GeneIDi 2539917.
    2541984.
    KEGGi spo:SPAC23A1.10.
    spo:SPBC839.15c.

    Organism-specific databases

    PomBasei SPAC23A1.10.
    SPBC839.15c.

    Phylogenomic databases

    HOGENOMi HOG000229291.
    KOi K03231.
    OMAi VWHPSAI.
    OrthoDBi EOG715QCW.
    PhylomeDBi Q10119.

    Enzyme and pathway databases

    Reactomei REACT_202295. HSF1 activation.

    Miscellaneous databases

    NextBioi 20801060.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    HAMAPi MF_00118_A. EF_Tu_A.
    InterProi IPR000795. EF_GTP-bd_dom.
    IPR027417. P-loop_NTPase.
    IPR009000. Transl_B-barrel.
    IPR009001. Transl_elong_EF1A/Init_IF2_C.
    IPR004539. Transl_elong_EF1A_euk/arc.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    IPR004160. Transl_elong_EFTu/EF1A_C.
    [Graphical view ]
    Pfami PF00009. GTP_EFTU. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    PF03143. GTP_EFTU_D3. 1 hit.
    [Graphical view ]
    PRINTSi PR00315. ELONGATNFCT.
    SUPFAMi SSF50447. SSF50447. 1 hit.
    SSF50465. SSF50465. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00483. EF-1_alpha. 1 hit.
    PROSITEi PS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Comprehensive cloning of Schizosaccharomyces pombe genes encoding translation elongation factors."
      Mita K., Morimyo M., Ito K., Sugaya K., Ebihara K., Hongo E., Higashi T., Hirayama Y., Nakamura Y.
      Gene 187:259-266(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (TEF1B AND TEF1C).
      Strain: 972 / ATCC 24843.
    2. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
      Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
      DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: PR745.
    3. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TEF1B AND TEF1C).
      Strain: 972 / ATCC 24843.
    4. "Phylogenetic relationships among yeasts of the 'Saccharomyces complex' determined from multigene sequence analyses."
      Kurtzman C.P., Robnett C.J.
      FEMS Yeast Res. 3:417-432(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-397.
      Strain: NRRL Y-12796.
    5. "Peptide elongation factor 1 from yeasts: purification and biochemical characterization of peptide elongation factors 1alpha and 1beta(gamma) from Saccharomyces carlsbergensis and Schizosaccharomyces pombe."
      Miyazaki M., Uritani M., Fujimura K., Yamakatsu H., Kageyama T., Takahashi K.
      J. Biochem. 103:508-521(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 64-94.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-23; THR-24; THR-158; SER-289; SER-296; SER-314; SER-388 AND SER-394, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiEF1A2_SCHPO
    AccessioniPrimary (citable) accession number: Q10119
    Secondary accession number(s): P78764
    , Q10158, Q7M4U9, Q7Z8V5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 117 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3