EIF3F_MAGO7
ID EIF3F_MAGO7 Reviewed; 370 AA.
AC A4R0E5; G4MS04;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=MGG_10653;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(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: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; CM001231; EHA57470.1; -; Genomic_DNA.
DR RefSeq; XP_003710082.1; XM_003710034.1.
DR AlphaFoldDB; A4R0E5; -.
DR SMR; A4R0E5; -.
DR STRING; 318829.MGG_10653T0; -.
DR EnsemblFungi; MGG_10653T0; MGG_10653T0; MGG_10653.
DR GeneID; 2682266; -.
DR KEGG; mgr:MGG_10653; -.
DR VEuPathDB; FungiDB:MGG_10653; -.
DR eggNOG; KOG2975; Eukaryota.
DR HOGENOM; CLU_027018_0_0_1; -.
DR InParanoid; A4R0E5; -.
DR OMA; MADTDSF; -.
DR OrthoDB; 1038775at2759; -.
DR Proteomes; UP000009058; 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:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IEA:EnsemblFungi.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:EnsemblFungi.
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..370
FT /note="Eukaryotic translation initiation factor 3 subunit
FT F"
FT /id="PRO_0000364330"
FT DOMAIN 31..170
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 313..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 370 AA; 40388 MW; E710DC8D9F31D972 CRC64;
MAVDHDDFLH LSKPLAPSAV GFNANVAPLT VTIQPQAILS ILDHAVRRDI RDTQATRVIG
ALVGVRSEDG TDVEVRSTFA IPHTENEDQV EVDVEYQKNM LALTLKASPR ESLLGWYTTS
HELNSFSALI QNFFASPETG TFPHPAVHLT MSTDPGADIE PRCYISAPAA VSPDRAAESC
FFIQVPHRTP PTNESDRAAL EAIAAGKDDE ARTAPVLSDV EALARSLEQT IDMLDRTSEY
VGAVLDEERE PSHALGQYLM NNLSLAPKVD SVSIEHDFNN HIQDVLMVSY LTNTIRTQVD
LAQRLALANL TDKDEKKEGE DGKAERGGGG RGGRGGKRGG GRGGGQQREP REPREPRESR
EPREPRESGE