ID Q4N5B4_THEPA Unreviewed; 527 AA.
AC Q4N5B4;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 08-OCT-2025, entry version 98.
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 OrderedLocusNames=TP02_0376 {ECO:0000313|EMBL:EAN32659.1};
OS Theileria parva (East coast fever infection agent).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5875 {ECO:0000313|EMBL:EAN32659.1, ECO:0000313|Proteomes:UP000001949};
RN [1] {ECO:0000313|EMBL:EAN32659.1, ECO:0000313|Proteomes:UP000001949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Muguga {ECO:0000313|EMBL:EAN32659.1,
RC ECO:0000313|Proteomes:UP000001949};
RX PubMed=15994558; DOI=10.1126/science.1110439;
RA Gardner M.J., Bishop R., Shah T., de Villiers E.P., Carlton J.M., Hall N.,
RA Ren Q., Paulsen I.T., Pain A., Berriman M., Wilson R.J.M., Sato S.,
RA Ralph S.A., Mann D.J., Xiong Z., Shallom S.J., Weidman J., Jiang L.,
RA Lynn J., Weaver B., Shoaibi A., Domingo A.R., Wasawo D., Crabtree J.,
RA Wortman J.R., Haas B., Angiuoli S.V., Creasy T.H., Lu C., Suh B.,
RA Silva J.C., Utterback T.R., Feldblyum T.V., Pertea M., Allen J.,
RA Nierman W.C., Taracha E.L.N., Salzberg S.L., White O.R., Fitzhugh H.A.,
RA Morzaria S., Venter J.C., Fraser C.M., Nene V.;
RT "Genome sequence of Theileria parva, a bovine pathogen that transforms
RT lymphocytes.";
RL Science 309:134-137(2005).
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:EAN32659.1}.
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DR EMBL; AAGK01000002; EAN32659.1; -; Genomic_DNA.
DR RefSeq; XP_764942.1; XM_759849.1.
DR AlphaFoldDB; Q4N5B4; -.
DR FunCoup; Q4N5B4; 438.
DR STRING; 5875.Q4N5B4; -.
DR GeneID; 3501537; -.
DR KEGG; tpv:TP02_0376; -.
DR VEuPathDB; PiroplasmaDB:TpMuguga_02g00376; -.
DR eggNOG; KOG2758; Eukaryota.
DR InParanoid; Q4N5B4; -.
DR OMA; ENEFTNG; -.
DR Proteomes; UP000001949; 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 HAMAP; MF_03004; eIF3e; 1.
DR InterPro; IPR016650; eIF3e.
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; PF21357; EIF3E_C; 1.
DR Pfam; PF01399; PCI; 1.
DR PIRSF; PIRSF016255; eIF3e_su6; 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:UP000001949}.
FT DOMAIN 258..447
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 506..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..516
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 527 AA; 61809 MW; E3D00BCB5D3310F4 CRC64;
MKESNFPDCH KYDITSKLSP YLEPKMVLYV LDWLSSKNIY SADDLSSIRE ELNKKLQSRK
LSDEEFSKLE TDSLSKIEQF KVVLSMYKKE QLHRISSTFE KTTVPSLIQW ANSSQLNVST
DFPHDVDELI LKLAKAYFDR EDYENCKSLL IYYVNSVSKY TVEGSSTRNK MKCYWGIISC
NMLSVLLPSS HEELQEMSSM VIVQQDSDND KDTTLIDQRT PRSGVYCVLK FAELLNSEEM
SRDKKDLILK RCWLLHWSLF YIFKYHLALF HLSNKSTKSF EWPQLQEYFL DERNLAVVNL
LTPHLLRYYA VYAILNRNRK DHFKTISNVI ANTKHKYNDT FTSLLGALFV DFNFEAAQKH
IVEIKEACYV DVLLNPLKDA IEESSRHIIF ETYCRIHKSI NLDIIAQNVN MTSLDAERWI
VNIIRHSHVE AKIDSEKNCV EISTVPPNLY QQVIEKTQNL TLRSNMILQN FSQMTGSADN
TLQNMRTSDL GDRNLQRRPF VYNQQKKNQH KFNQGKDFQR TDQESLW
//
