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Database: UniProt
Entry: EIF3E_USTMA
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Original site: EIF3E_USTMA 
ID   EIF3E_USTMA             Reviewed;         541 AA.
AC   Q4PHN4; A0A0D1D0G4;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit E {ECO:0000255|HAMAP-Rule:MF_03004};
DE            Short=eIF3e {ECO:0000255|HAMAP-Rule:MF_03004};
GN   Name=INT6 {ECO:0000255|HAMAP-Rule:MF_03004}; ORFNames=UMAG_00379;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) 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:0000255|HAMAP-Rule:MF_03004}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03004}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit E family. {ECO:0000255|HAMAP-
CC       Rule:MF_03004}.
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DR   EMBL; CM003140; KIS71953.1; -; Genomic_DNA.
DR   RefSeq; XP_011386265.1; XM_011387963.1.
DR   AlphaFoldDB; Q4PHN4; -.
DR   SMR; Q4PHN4; -.
DR   STRING; 237631.Q4PHN4; -.
DR   EnsemblFungi; KIS71953; KIS71953; UMAG_00379.
DR   GeneID; 23561698; -.
DR   KEGG; uma:UMAG_00379; -.
DR   VEuPathDB; FungiDB:UMAG_00379; -.
DR   eggNOG; KOG2758; Eukaryota.
DR   HOGENOM; CLU_031132_0_0_1; -.
DR   InParanoid; Q4PHN4; -.
DR   OMA; TIQTNCP; -.
DR   OrthoDB; 226348at2759; -.
DR   Proteomes; UP000000561; Chromosome 1.
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:0005852; C:eukaryotic translation initiation factor 3 complex; IBA:GO_Central.
DR   GO; GO:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IEA:UniProtKB-UniRule.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..541
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   E"
FT                   /id="PRO_0000365992"
FT   DOMAIN          252..443
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          466..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..525
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..541
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   541 AA;  60520 MW;  F1B76FA38CC3254C CRC64;
     MAVKYDLTQT LLPYLDRHLG LPLLSHLAGS GIFSETDIAK AQYELAKNTS MVDYALQLYE
     QAYPNQPAPA EIEKQRENAI ALNDKLGSEV DHVLEVIQDP SVASALKQDK AQNLQWLEEK
     YNLTSEQINA LYRYGYFQFS CGNYGDASSY LYHFRVLSTD PVLTMSSHWG KLASDILVGE
     WEQALSELKL LREQLDSSAA HVTASYAQPS TSNGSSQNDD LTQEGLLKKR AWLLHWALFI
     FFNHPGGREQ LVEMFLSPVY LNTIQTTCWW LLRYVVAALL LSRRTTRVYL VQQPAPATLM
     ASVSGANVNK LSPQQAIKDI VNIIDSESYR IAGTDPIVDF LSKLFVDFDF EAAQEQLTLA
     EQVASKDFFL ADFKDELVEA CRVVISEAYC RIHSKVDIAD LVKRLNLSKE DGEKWIVNLV
     RDTRADAKID FKEGMVFMNP THPPVYQTII EKTRGFTFRT SAMGTAIDRK AHPPSLNNTH
     NLNGNDKRGN AGGRGGRGGQ RNQGGQRDRS HAHNNEAKRE GESASAEEAQ QQQPAQAIAA
     N
//
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