ID   EIF3F_CHAGB             Reviewed;         357 AA.
AC   Q2HGJ2;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=CHGG_00662;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH408029; EAQ92427.1; -; Genomic_DNA.
DR   RefSeq; XP_001219883.1; XM_001219882.1.
DR   AlphaFoldDB; Q2HGJ2; -.
DR   SMR; Q2HGJ2; -.
DR   STRING; 38033.XP_001219883.1; -.
DR   PRIDE; Q2HGJ2; -.
DR   EnsemblFungi; EAQ92427; EAQ92427; CHGG_00662.
DR   GeneID; 4386693; -.
DR   eggNOG; KOG2975; Eukaryota.
DR   HOGENOM; CLU_027018_0_0_1; -.
DR   InParanoid; Q2HGJ2; -.
DR   OMA; MADTDSF; -.
DR   OrthoDB; 1038775at2759; -.
DR   Proteomes; UP000001056; 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:0005852; C:eukaryotic translation initiation factor 3 complex; IEA:UniProtKB-UniRule.
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; IEA:InterPro.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
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..357
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   F"
FT                   /id="PRO_0000364327"
FT   DOMAIN          30..169
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          309..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..330
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..357
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   357 AA;  38206 MW;  29E237F7B2C31120 CRC64;
     MAVEQEHFVH LARPLAPTSM GFTGSAPLTV HIQPQAVFSV IDHAVRRDTR DTQSTRVIGA
     LVGTRSEDGS EVEVRSTFAI PHTENEDQVE VDVEYQKNML ALTLKASPRE TLLGWYTTSH
     ELNSFSALIQ NFFASPETGT FPHPAVHLTI STEPGAPIAT KAYISAPVAV SPERAAESCL
     FIEVPHKLLF SDAERAALGT ATAAAETEAR SAPVISDIET LAQSLESVSD LLERVSGFVG
     EVLDEERDGS HALGQYLMNA LSLAPKVSAT QIEADFNNHV QDVLMVSYLA NTIRTQIDLA
     QRLATAPLVG GDKEGGEKGK DGEDGGRGGR GGKRGGGGRG GHRGEPREPR EPREPAE