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Database: UniProt
Entry: A0A1X7RGI3_ZYMTR
LinkDB: A0A1X7RGI3_ZYMTR
Original site: A0A1X7RGI3_ZYMTR 
ID   A0A1X7RGI3_ZYMTR        Unreviewed;       231 AA.
AC   A0A1X7RGI3;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Translation elongation factor EF1B beta/delta subunit guanine nucleotide exchange domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ZT3D7_G1476 {ECO:0000313|EMBL:SMQ46330.1};
OS   Zymoseptoria tritici ST99CH_3D7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ46330.1, ECO:0000313|Proteomes:UP000215127};
RN   [1] {ECO:0000313|EMBL:SMQ46330.1, ECO:0000313|Proteomes:UP000215127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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; LT853692; SMQ46330.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7RGI3; -.
DR   STRING; 1276538.A0A1X7RGI3; -.
DR   Proteomes; UP000215127; Chromosome 1.
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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000215127}.
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..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          199..226
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        101..120
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   231 AA;  25650 MW;  13708A822B2464CF CRC64;
     MGFLDFVNDT AYSLLDSWVS TRSYIVGYGP SQADVKTYQA LKSAPDADKY PHAARWYKHT
     ATFESEFASL PGDPSKAHTA YGPESHELTV NPAKAPAKAE EEDDDDVDLF GSDDEEEDAE
     AARIRDERLA EYKKKKEGKT KPAAKSIVTL DVKPWDDETD MKELEAAVRA IEQEGLVWGG
     SKLVAVGFGI KKLQINLVVE DEKVSLDELQ EKIQDLEDYV QSSDVAAMQK L
//
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