ID   EIF3F_PHANO             Reviewed;         342 AA.
AC   Q0UTQ6;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit F {ECO:0000255|HAMAP-Rule:MF_03005};
DE            Short=eIF3f {ECO:0000255|HAMAP-Rule:MF_03005};
GN   ORFNames=SNOG_04858;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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_03005}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03005}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03005}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit F family. {ECO:0000255|HAMAP-
CC       Rule:MF_03005}.
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DR   EMBL; CH445331; EAT87249.1; -; Genomic_DNA.
DR   RefSeq; XP_001795271.1; XM_001795219.1.
DR   AlphaFoldDB; Q0UTQ6; -.
DR   SMR; Q0UTQ6; -.
DR   STRING; 13684.SNOT_04858; -.
DR   PRIDE; Q0UTQ6; -.
DR   EnsemblFungi; SNOT_04858; SNOT_04858; SNOG_04858.
DR   GeneID; 5972146; -.
DR   KEGG; pno:SNOG_04858; -.
DR   eggNOG; KOG2975; Eukaryota.
DR   HOGENOM; CLU_027018_0_0_1; -.
DR   InParanoid; Q0UTQ6; -.
DR   OMA; MADTDSF; -.
DR   OrthoDB; 1038775at2759; -.
DR   Proteomes; UP000001055; 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:EnsemblFungi.
DR   GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IBA:GO_Central.
DR   GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
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; cd08064; MPN_eIF3f; 1.
DR   HAMAP; MF_03005; eIF3f; 1.
DR   InterPro; IPR027531; eIF3f.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR024969; Rpn11/EIF3F_C.
DR   PANTHER; PTHR10540:SF6; PTHR10540:SF6; 1.
DR   Pfam; PF01398; JAB; 1.
DR   Pfam; PF13012; MitMem_reg; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..342
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   F"
FT                   /id="PRO_0000364334"
FT   DOMAIN          30..166
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          310..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..342
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   342 AA;  37568 MW;  8E8500C474E7C708 CRC64;
     MSERDSFLHL ARPLGPAPVG AQPSTAPLNV AIQPQAVFSI LDHSLRRPAD QERVIGTLLG
     TRSEDGTEIE IRNCYAVPHT ETAEQVEVDM DYQKQMLALH LRANPREVLV GWYATSSDLN
     TFSALIQNFY SQQGDGTWPH PAVHLTVSTV PGQDIESRTY ISAPIGVTAE RAADSCLFIP
     VPHEIKYGEA EKSGLELISS AKDREDRSQE IMTDLDSLER AVQHVLDMLE RVSNYVNNVL
     DEEAEPSSAL GQFLMNALSL APKVDPADIE RDFNNHIQDV LVVSYLANTI RTQIDLSNRL
     ATAALTMGGT DALAGDGQKD GGDRKQGGDR RNKGRQQRTQ EA