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Database: UniProt
Entry: A0A090L9G7_STRRB
LinkDB: A0A090L9G7_STRRB
Original site: A0A090L9G7_STRRB 
ID   A0A090L9G7_STRRB        Unreviewed;       436 AA.
AC   A0A090L9G7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 54.
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};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 6 {ECO:0000256|HAMAP-Rule:MF_03004};
GN   ORFNames=SRAE_2000106100 {ECO:0000313|EMBL:CEF66392.1,
GN   ECO:0000313|WBParaSite:SRAE_2000106100.1,
GN   ECO:0000313|WormBase:SRAE_2000106100};
OS   Strongyloides ratti (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF66392.1};
RN   [1] {ECO:0000313|EMBL:CEF66392.1, ECO:0000313|Proteomes:UP000035682}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC   ECO:0000313|WBParaSite:SRAE_2000106100.1}, and ED321 Heterogonic
RC   {ECO:0000313|EMBL:CEF66392.1};
RA   Martin A.A.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SRAE_2000106100.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (DEC-2020) to UniProtKB.
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; LN609529; CEF66392.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090L9G7; -.
DR   STRING; 34506.A0A090L9G7; -.
DR   EnsemblMetazoa; SRAE_2000106100.1; SRAE_2000106100.1; WBGene00261262.
DR   WBParaSite; SRAE_2000106100.1; SRAE_2000106100.1; WBGene00261262.
DR   WormBase; SRAE_2000106100; SRP09338; WBGene00261262; -.
DR   eggNOG; KOG2758; Eukaryota.
DR   OMA; TIQTNCP; -.
DR   OrthoDB; 226348at2759; -.
DR   Proteomes; UP000035682; Chromosome X.
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:UP000035682}.
FT   DOMAIN          221..396
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
SQ   SEQUENCE   436 AA;  51465 MW;  9BBD0688D5D1B864 CRC64;
     MADFDLTYRM TPFFDVHLVI PLLEFIEARK IYSEESLVKV QRNVLLKTNM IDSLIETYPK
     DKIPEGLITR KDEILAQRKR LKEEADEILT ILEKPEVKEL IENKSERESG TKLIELLSAK
     HGFKPEMLDT LFKYAKFLYE CGNYNTSANM LMYYRTLVSP TDKNFLNALY GKLASEILLQ
     EWVHAKNDLM RIRLFIENNP FNDEIELIKH RAWVMHWALF VCFNNPEGRD EIIDMFLNVQ
     QYANAIQIVS PHLLRYLAVA IVTSKHKQTN SLKELVKLLE SYGEHYKDPI TEFLTCLYIK
     YDFNEAQKYL KQCQGVLAND FFLTAYADEF NEACRLLVFE SFCRIHNCVK LDMLAERLNM
     DTEEAEKWIV DLIRKYKIEG AKIDSQNREV VMTPNVQSLH EQVMESTKRI YTRIHSMVMN
     LEKIQLEREV QDNEVY
//
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