ID A0A0W0GFA5_9AGAR Unreviewed; 457 AA.
AC A0A0W0GFA5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=WG66_158 {ECO:0000313|EMBL:KTB47257.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB47257.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB47257.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB47257.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) 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}.
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:KTB47257.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LATX01000073; KTB47257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0GFA5; -.
DR eggNOG; KOG2758; Eukaryota.
DR Proteomes; UP000054988; 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; 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:UP000054988}.
FT DOMAIN 230..417
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
SQ SEQUENCE 457 AA; 51822 MW; 44658D6164B7938C CRC64;
MAEHDLSKTI IPYLDRHLTF PLLAHLTETG IFPEQEVQVA QYELASGTNM FDYAASLFKQ
IHPDREVPKE FDEKRQNVVS THERLQQEAQ AVLDVIENPE VAQSLRQDKN QNLQYLKEHY
SLTLDQITAL YNFGKFQYSY GNYSGAADYL YHFRVLSTDA DLNMSAHWGK LACDILTGKW
DVALEELNTL REAIDSRTPA SFAPSTNPSI DPALAQLHSR TWLVHWSLFV YFNHPQGRSL
LLETFLSPTY LNTIQTSCPW ILRYLAAAAI ISTPTPSSNS IPLSSRVKNA VREIVKVIQM
EGYQYSDPVT EFLMQLHVEF DFEAAQKELG KAEKVVADDF FLGDFRDEFL ESARCLVSEA
YCRIHQRIDI GDLSDRLNLP RDEGEKWIVN LIRETRMGQD AKIDLEKNLI QISRPPQPIY
QSVIEKTRGL AIRTQALGAA VARPGISGSA TPPVAVN
//
