ID A0AAE0MUT2_9PEZI Unreviewed; 442 AA.
AC A0AAE0MUT2;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 6.
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=B0H65DRAFT_178397 {ECO:0000313|EMBL:KAK3348548.1};
OS Neurospora tetraspora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=94610 {ECO:0000313|EMBL:KAK3348548.1, ECO:0000313|Proteomes:UP001278500};
RN [1] {ECO:0000313|EMBL:KAK3348548.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 560.94 {ECO:0000313|EMBL:KAK3348548.1};
RX PubMed=37820761;
RA Hensen N., Bonometti L., Westerberg I., Brannstrom I.O., Guillou S.,
RA Cros-Aarteil S., Calhoun S., Haridas S., Kuo A., Mondo S., Pangilinan J.,
RA Riley R., LaButti K., Andreopoulos B., Lipzen A., Chen C., Yan M., Daum C.,
RA Ng V., Clum A., Steindorff A., Ohm R.A., Martin F., Silar P., Natvig D.O.,
RA Lalanne C., Gautier V., Ament-Velasquez S.L., Kruys A., Hutchinson M.I.,
RA Powell A.J., Barry K., Miller A.N., Grigoriev I.V., Debuchy R.,
RA Gladieux P., Hiltunen Thoren M., Johannesson H.;
RT "Genome-scale phylogeny and comparative genomics of the fungal order
RT Sordariales.";
RL Mol. Phylogenet. Evol. 189:0-0(2023).
RN [2] {ECO:0000313|EMBL:KAK3348548.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 560.94 {ECO:0000313|EMBL:KAK3348548.1};
RG Lawrence Berkeley National Laboratory;
RA Haridas S., Hensen N., Bonometti L., Westerberg I., Brannstrom I.O.,
RA Guillou S., Cros-Aarteil S., Calhoun S., Kuo A., Mondo S., Pangilinan J.,
RA Riley R., Labutti K., Andreopoulos B., Lipzen A., Chen C., Yanf M.,
RA Daum C., Ng V., Clum A., Steindorff A., Ohm R., Martin F., Silar P.,
RA Natvig D., Lalanne C., Gautier V., Ament-Velasquez S.L., Kruys A.,
RA Hutchinson M.I., Powell A.J., Barry K., Miller A.N., Grigoriev I.V.,
RA Debuchy R., Gladieux P., Thoren M.H., Johannesson H.;
RL Submitted (JUN-2023) 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:KAK3348548.1}.
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DR EMBL; JAUEPP010000003; KAK3348548.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAE0MUT2; -.
DR Proteomes; UP001278500; 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 Gene3D; 1.25.40.570; -; 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 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:UP001278500}.
FT DOMAIN 248..416
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
SQ SEQUENCE 442 AA; 50879 MW; 424EACD181ABE406 CRC64;
MASTSPATNG DAAPANYDLV LKLAPHLDRH MIFPLLEFNA GRLKEDETDK AREILAAKYA
LLKKTNMTDY VANLYCELEG LKEPPAEYAE RRQKVFHQLE KYEQETAKIT ELLQRDDVVN
NLRSDKVANL EFLKKEHDVT IDMVNALYDF GQLQYSCGNY ADASELLYRF RVLSTDNDKV
SYATWGRLAC EILSMSWESA MEELQKVRES IDTRLANNPL AQLQHRTQLV HWALFPLFNY
DKAREPLLDL FFNAGFINTI QANSPWILRY LTVAVITNRG RAKNAGVQQK QMKDIVRIVK
QEAYEYQDPV TRFVHALCID FDFEEAQHQL VLAEEVLRSD FFLLAHADDF VDSARHLIFE
SYCKIHARIS LKDLSARLGL NNDDAEKWIV NLIRDTRLDA KIDYKEGTVV MNHPPSSVYQ
QVIERTKGGF FRTQVLTAAV AR
//
