ID   EIF3E_BOTFB             Reviewed;         452 AA.
AC   A6SM77;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit E {ECO:0000255|HAMAP-Rule:MF_03004};
DE            Short=eIF3e {ECO:0000255|HAMAP-Rule:MF_03004};
GN   Name=int6; ORFNames=BC1G_13956;
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
CC   -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is involved in protein synthesis of a
CC       specialized repertoire of mRNAs and, together with other initiation
CC       factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC       ribosome. The eIF-3 complex specifically targets and initiates
CC       translation of a subset of mRNAs involved in cell proliferation.
CC       {ECO:0000255|HAMAP-Rule:MF_03004}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03004}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit E family. {ECO:0000255|HAMAP-
CC       Rule:MF_03004}.
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DR   EMBL; CH476969; EDN19988.1; -; Genomic_DNA.
DR   RefSeq; XP_001547625.1; XM_001547575.1.
DR   AlphaFoldDB; A6SM77; -.
DR   SMR; A6SM77; -.
DR   GeneID; 5428085; -.
DR   KEGG; bfu:BCIN_02g08260; -.
DR   VEuPathDB; FungiDB:Bcin02g08260; -.
DR   OMA; TWGKLAC; -.
DR   OrthoDB; 1151808at2759; -.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070196; P:eukaryotic translation initiation factor 3 complex assembly; IEA:EnsemblFungi.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR   HAMAP; MF_03004; eIF3e; 1.
DR   InterPro; IPR016650; eIF3e.
DR   InterPro; IPR019010; eIF3e_N.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10317; PTHR10317; 1.
DR   Pfam; PF09440; eIF3_N; 1.
DR   Pfam; PF01399; PCI; 1.
DR   PIRSF; PIRSF016255; eIF3e_su6; 1.
DR   SMART; SM01186; eIF3_N; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Protein biosynthesis.
FT   CHAIN           1..452
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   E"
FT                   /id="PRO_0000366889"
FT   DOMAIN          246..426
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   452 AA;  51797 MW;  B0FA89FCAA1BA9C1 CRC64;
     MADNTPTTAN DLLNDATQAA AKSPEEIAKE NDLLPKLITH LDRHLIFPLL QFVGDQDDEP
     SPEITKAKFE LLKKTNMTDY VASLHCEIEG VDEAPKEYAN KRQEILQRLE IFGQESEKIT
     DLLGREDVVT GLRSDKVANL EFLKKEHDVT IEMVNVLYDF GNFQYSCGNY GAAAELLYQF
     RVLSTDDDKV TAATWGKLAC EILTGNWESA MEEVQKVKES IETKLFNKPL AQLHHRTWLI
     HWALFPFFNH EPARDVICDL FFSPAFINTI QTACPWILRY LTAAVITNRN RTRNTGQYQK
     QLKDIIRIVK QENYEYSDPV TDFIKALYLD FDFEEAQKKL SEAEEVLRSD FFLVAASENF
     VEAARHLISE SYCKIHQRID IKDLSARLGL NQDDGEKWIV NLIRDTRVDA KIDYKEGTVV
     MNHPPSSVYQ QVIERTKGGF FRTQVLSAAV AK