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Database: UniProt
Entry: A0A0D2DPZ2_9EURO
LinkDB: A0A0D2DPZ2_9EURO
Original site: A0A0D2DPZ2_9EURO 
ID   A0A0D2DPZ2_9EURO        Unreviewed;       227 AA.
AC   A0A0D2DPZ2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Elongation factor 1-beta {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV06_09883 {ECO:0000313|EMBL:KIW37904.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW37904.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW37904.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW37904.1,
RC   ECO:0000313|Proteomes:UP000053342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
CC       {ECO:0000256|ARBA:ARBA00007411, ECO:0000256|RuleBase:RU003791}.
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DR   EMBL; KN847342; KIW37904.1; -; Genomic_DNA.
DR   RefSeq; XP_016258120.1; XM_016411366.1.
DR   AlphaFoldDB; A0A0D2DPZ2; -.
DR   STRING; 215243.A0A0D2DPZ2; -.
DR   GeneID; 27361957; -.
DR   VEuPathDB; FungiDB:PV06_09883; -.
DR   HOGENOM; CLU_050172_0_2_1; -.
DR   OrthoDB; 77945at2759; -.
DR   Proteomes; UP000053342; Unassembled WGS sequence.
DR   GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd00292; EF1B; 1.
DR   Gene3D; 1.20.1050.130; -; 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; IPR049720; EF1B_bsu/dsu.
DR   InterPro; IPR014038; EF1B_bsu/dsu_GNE.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR014717; Transl_elong_EF1B/ribsomal_bS6.
DR   InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR   PANTHER; PTHR11595; EF-HAND AND COILED-COIL DOMAIN-CONTAINING FAMILY MEMBER; 1.
DR   PANTHER; PTHR11595:SF21; ELONGATION FACTOR 1-BETA; 1.
DR   Pfam; PF10587; EF-1_beta_acid; 1.
DR   Pfam; PF00736; EF1_GNE; 1.
DR   SMART; SM01182; EF-1_beta_acid; 1.
DR   SMART; SM00888; EF1_GNE; 1.
DR   SUPFAM; SSF54984; eEF-1beta-like; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   PROSITE; PS00824; EF1BD_1; 1.
DR   PROSITE; PS00825; EF1BD_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768,
KW   ECO:0000256|RuleBase:RU003791};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU003791};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053342}.
FT   DOMAIN          105..132
FT                   /note="Elongation factor 1 beta central acidic region
FT                   eukaryote"
FT                   /evidence="ECO:0000259|SMART:SM01182"
FT   DOMAIN          141..227
FT                   /note="Translation elongation factor EF1B beta/delta
FT                   subunit guanine nucleotide exchange"
FT                   /evidence="ECO:0000259|SMART:SM00888"
FT   REGION          72..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..116
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   227 AA;  25562 MW;  12343A2084E92529 CRC64;
     MGFTDFVSDS GLTLLNNWLQ TRSYISGYTP SQADVVSFKA LDKAPAVEKY PHAYRWYNHV
     KSYEADFSTL PGDPSKPFTT YGPDKVALTE NPKNAPADDD DDMDLFGSDD EEEDPEVVAE
     RERRLAEYKK KKEGKTKPAA KSIVTLDVKP WDDETDMNEL VQNVIGIEMD GLVWGAHKLE
     AVGFGIKKLQ INLVIEDEKV SLTDLQEKIE EDEDHVQSTD VIAMQKL
//
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