ID G1XMF4_ARTOA Unreviewed; 467 AA.
AC G1XMF4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=AOL_s00169g7 {ECO:0000313|EMBL:EGX45673.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX45673.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX45673.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(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: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:EGX45673.1}.
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; ADOT01000258; EGX45673.1; -; Genomic_DNA.
DR RefSeq; XP_011125666.1; XM_011127364.1.
DR AlphaFoldDB; G1XMF4; -.
DR STRING; 756982.G1XMF4; -.
DR GeneID; 22896884; -.
DR eggNOG; KOG2758; Eukaryota.
DR HOGENOM; CLU_031132_0_0_1; -.
DR InParanoid; G1XMF4; -.
DR OMA; TIQTNCP; -.
DR OrthoDB; 226348at2759; -.
DR Proteomes; UP000008784; 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:UP000008784}.
FT DOMAIN 259..441
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 53789 MW; 2C71007120048F61 CRC64;
MSLEEPQVPA VADATSQAEG PSAIETARKY DLTPKIMPFL DRHLIFHLLA FLRDQQFYPA
EELLQNTYDL LEPTNMTDYL MDLWKQIHGK EDIDIPREFL LKREKVMQEW SALQDETTKI
TGLLENPDVV SNFRSDKMQN LQFLKDNHGV TDDMIDALLR YGQAAYSRGS YDQASDILYS
FRILSTDSDK VNQATWGKLA CEILTVNWEG AMEEIQKIKE AIDTKPFLSP TAQLQQRTWL
IHWALFPLFN HEAARDTILE LFFSPNFINT IQTSCPWVLR YLVAAVITSK KNSGSSRAAA
IQQKQFKDLV RVVRQELYEY SDPITEFIAA LHLDFDFEEA QKKLGEAEEV IRSDFFLQVF
CATEQSEGVE SKNAFVESAR HLISEAYCRI HQRIDITDLS QRLNLSQEDG EKWIVNLIKD
TRVDAKIDYK NGTVIMNHPP QSVYQQVIEK TKGGFFRTQV LHAAVTR
//
