ID A0A2S6CHL9_9PEZI Unreviewed; 231 AA.
AC A0A2S6CHL9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Translation elongation factor EF1B beta/delta subunit guanine nucleotide exchange domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CBER1_05345 {ECO:0000313|EMBL:PPJ59211.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ59211.1, ECO:0000313|Proteomes:UP000237631};
RN [1] {ECO:0000313|Proteomes:UP000237631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT mechanisms and extends production to the genus Colletotrichum.";
RL bioRxiv 0:0-0(2017).
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
CC {ECO:0000256|ARBA:ARBA00007411, ECO:0000256|RuleBase:RU003791}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PPJ59211.1}.
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DR EMBL; PNEN01000413; PPJ59211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6CHL9; -.
DR STRING; 357750.A0A2S6CHL9; -.
DR OrthoDB; 77945at2759; -.
DR Proteomes; UP000237631; 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:UP000237631}.
FT DOMAIN 109..136
FT /note="Elongation factor 1 beta central acidic region
FT eukaryote"
FT /evidence="ECO:0000259|SMART:SM01182"
FT DOMAIN 145..231
FT /note="Translation elongation factor EF1B beta/delta
FT subunit guanine nucleotide exchange"
FT /evidence="ECO:0000259|SMART:SM00888"
FT REGION 71..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 231 AA; 25747 MW; 4F349565049200FC CRC64;
MGFTDFVSDT GLTLLDNWVK TRSYIVGYGP SQADVKVFQS FSEQPKVEKY PHAYRWYKHI
STFEPEFSSL PGDPSKAATA YGPESSDLTV NPAKAPEKAE EEDDDEVDLF GSDDEEEDAE
AVRIREERLA EYKKKKEGKT KPAAKSIVTL DVKPWDDETD MKALEAAVRG IEQDGLVWGG
GKLVAVGFGI KKLQINCVVE DDKVSMEELQ ETIEGFEDYV QSSDVAAMQK L
//
