ID A0A318Z0C0_9EURO Unreviewed; 451 AA.
AC A0A318Z0C0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit E {ECO:0000256|HAMAP-Rule:MF_03004, ECO:0000256|PIRNR:PIRNR016255};
DE Short=eIF3e {ECO:0000256|HAMAP-Rule:MF_03004};
GN Name=INT6 {ECO:0000256|HAMAP-Rule:MF_03004};
GN ORFNames=BP01DRAFT_213045 {ECO:0000313|EMBL:PYH40446.1};
OS Aspergillus saccharolyticus JOP 1030-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH40446.1, ECO:0000313|Proteomes:UP000248349};
RN [1] {ECO:0000313|EMBL:PYH40446.1, ECO:0000313|Proteomes:UP000248349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH40446.1,
RC ECO:0000313|Proteomes:UP000248349};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_03004}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03004,
CC ECO:0000256|PIRNR:PIRNR016255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03004,
CC ECO:0000256|PIRNR:PIRNR016255}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit E family. {ECO:0000256|HAMAP-
CC Rule:MF_03004, ECO:0000256|PIRNR:PIRNR016255}.
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DR EMBL; KZ821286; PYH40446.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318Z0C0; -.
DR STRING; 1450539.A0A318Z0C0; -.
DR OrthoDB; 226348at2759; -.
DR Proteomes; UP000248349; Unassembled WGS sequence.
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:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR CDD; cd21378; eIF3E; 1.
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; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT E; 1.
DR PANTHER; PTHR10317:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT E; 1.
DR Pfam; PF09440; eIF3_N; 1.
DR Pfam; PF21357; EIF3E_C; 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; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03004};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_03004};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03004}; Reference proteome {ECO:0000313|Proteomes:UP000248349}.
FT DOMAIN 256..425
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
SQ SEQUENCE 451 AA; 51445 MW; 4F33E7E575C9E89D CRC64;
MAANAPPSAE TLLSGAAAHT PKTAEEIANH DLLPKLIPYL DRHLVFPLLE FSSGGQDDDK
ETIRAKYELL KHTNMTDYVA NLWKELNDSD SIPEEFIKKR EEVLAKLQHY QDQSAKITEL
LQDESVVGNL RSDKVANLKF LEEQHGVTAE MVNSLFDYGR FQYSCGSYGN AAELLYQFRV
LSTDNDKVAS ATWGKLASEI LTTSWEGAME EVIKVKDSID TRFFNNPLGQ LQNRSWLIHW
SLFPFFNYDP ARDVLTDLFF SPAYINTIQT SCPWILRYLA AAVITNRNRA HKNSSVYQKQ
LKDLIRVVRQ EGYEYSDPIT DFVKALYVDF DFEEAQKKLG EAEDVLRSDF FLVSAADAFI
EAARHLISES YCKIHQRIDI KDLSTRLGLN QDDGEKWIVN LIRDTRVDAK IDYKEGTVIM
NHPPQSVYQQ VIEKTKGAFF RTQVLSAAVA K
//
