ID   EF1B_PENCI              Reviewed;         228 AA.
AC   Q69BZ7;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Elongation factor 1-beta {ECO:0000303|PubMed:15679724};
DE            Short=EF-1-beta {ECO:0000303|PubMed:15679724};
DE   AltName: Allergen=Pen c 24 {ECO:0000303|PubMed:15679724};
OS   Penicillium citrinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5077 {ECO:0000312|EMBL:AAR17475.1};
RN   [1] {ECO:0000312|EMBL:AAR17475.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], ALLERGEN, AND REGION.
RC   STRAIN=52-5 {ECO:0000303|PubMed:15679724};
RX   PubMed=15679724; DOI=10.1111/j.1398-9995.2005.00706.x;
RA   Tang R.B., Chen Y.S., Chou H., Lee S.S., Tai H.Y., Shen H.D.;
RT   "cDNA cloning and immunologic characterization of a novel EF-1beta allergen
RT   from Penicillium citrinum.";
RL   Allergy 60:366-371(2005).
CC   -!- FUNCTION: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound
CC       to EF-1-alpha to GTP. {ECO:0000250|UniProtKB:P32471}.
CC   -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta, and gamma.
CC       {ECO:0000305}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 8% of
CC       92 Taipei area patients suffering from bronchial asthma.
CC       {ECO:0000269|PubMed:15679724}.
CC   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
CC       {ECO:0000255|RuleBase:RU003791, ECO:0000305}.
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DR   EMBL; AY363911; AAR17475.1; -; mRNA.
DR   AlphaFoldDB; Q69BZ7; -.
DR   SMR; Q69BZ7; -.
DR   Allergome; 1311; Pen c 24.
DR   Allergome; 3404; Pen c 24.0101.
DR   GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; ISS:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd00292; EF1B; 1.
DR   Gene3D; 3.30.70.60; -; 1.
DR   InterPro; IPR036219; eEF-1beta-like_sf.
DR   InterPro; IPR018940; EF-1_beta_acid_region_euk.
DR   InterPro; IPR014038; EF1B_bsu/dsu_GNE.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR   InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR   Pfam; PF10587; EF-1_beta_acid; 1.
DR   Pfam; PF00736; EF1_GNE; 1.
DR   SMART; SM00888; EF1_GNE; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF54984; SSF54984; 1.
DR   PROSITE; PS00825; EF1BD_2; 1.
PE   1: Evidence at protein level;
KW   Allergen; Elongation factor; IgE-binding protein; Protein biosynthesis.
FT   CHAIN           1..228
FT                   /note="Elongation factor 1-beta"
FT                   /id="PRO_0000446262"
FT   REGION          74..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..93
FT                   /note="IgE-binding"
FT                   /evidence="ECO:0000269|PubMed:15679724"
FT   COMPBIAS        97..113
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   228 AA;  25049 MW;  9FAEC66501F7CF53 CRC64;
     MGFTDFVSDA GLSLANNYLA TRSYIVGHAP SQADVVTYKA FTASPDAEKY PHVARWYKHI
     ASYESEFPTL PGDASKAFTA YGPEGSEASA NPKDKPAEEE EEEDLFASDS EDEDPAVVAE
     RNKNLEEYKK KKAAKGPKPA AKSLVTLEVK PWDDETNLEE LEANVRAIEM DGLVWGASKF
     VAVGFGIKKL QINLVVEDEK VSTDELQAQI EEDEDHVQST DVAAMQKL