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EIF3G_BOTFB
ID   EIF3G_BOTFB             Reviewed;         288 AA.
AC   A6SGN8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit G {ECO:0000255|HAMAP-Rule:MF_03006};
DE            Short=eIF3g {ECO:0000255|HAMAP-Rule:MF_03006};
DE   AltName: Full=Eukaryotic translation initiation factor 3 RNA-binding subunit {ECO:0000255|HAMAP-Rule:MF_03006};
DE            Short=eIF-3 RNA-binding subunit {ECO:0000255|HAMAP-Rule:MF_03006};
DE   AltName: Full=Translation initiation factor eIF3 p33 subunit homolog {ECO:0000255|HAMAP-Rule:MF_03006};
DE            Short=eIF3 p33 homolog {ECO:0000255|HAMAP-Rule:MF_03006};
GN   Name=tif35; ORFNames=BC1G_11662;
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
CC   -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC       initiation factor 3 (eIF-3) complex, which is involved in protein
CC       synthesis of a specialized repertoire of mRNAs and, together with other
CC       initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC       the 40S ribosome. The eIF-3 complex specifically targets and initiates
CC       translation of a subset of mRNAs involved in cell proliferation. This
CC       subunit can bind 18S rRNA. {ECO:0000255|HAMAP-Rule:MF_03006}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03006}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03006}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit G family. {ECO:0000255|HAMAP-
CC       Rule:MF_03006}.
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DR   EMBL; CH476932; EDN33307.1; -; Genomic_DNA.
DR   RefSeq; XP_001549630.1; XM_001549580.1.
DR   AlphaFoldDB; A6SGN8; -.
DR   SMR; A6SGN8; -.
DR   GeneID; 5430122; -.
DR   KEGG; bfu:BCIN_07g06230; -.
DR   VEuPathDB; FungiDB:Bcin07g06230; -.
DR   OMA; TTKCPFK; -.
DR   OrthoDB; 1226059at2759; -.
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:0043614; C:multi-eIF complex; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; 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   GO; GO:0032781; P:positive regulation of ATP-dependent activity; IEA:EnsemblFungi.
DR   GO; GO:0002188; P:translation reinitiation; IEA:EnsemblFungi.
DR   GO; GO:0006415; P:translational termination; IEA:EnsemblFungi.
DR   CDD; cd12933; eIF3G; 1.
DR   CDD; cd12408; RRM_eIF3G_like; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   HAMAP; MF_03006; eIF3g; 1.
DR   InterPro; IPR017334; eIF3_g.
DR   InterPro; IPR024675; eIF3g_N.
DR   InterPro; IPR034240; eIF3G_RRM.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF12353; eIF3g; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PIRSF; PIRSF037949; Transl_init_eIF-3_RNA-bind; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; RNA-binding.
FT   CHAIN           1..288
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   G"
FT                   /id="PRO_0000366891"
FT   DOMAIN          208..286
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03006"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   288 AA;  31720 MW;  8E9C6F94BA000260 CRC64;
     MSRVANNRDW ADDEDLEDSN ELPQSTTTTN KDGTQTIVTW RFNDDGKKVK TTRRIRFTKV
     KEIVNPRVAE RKSWGKFGLS QKDAAGPASD TTSVGENIIF RPSTNWRKDA KEEVSDAGAM
     KNKLKDKQVK CRICSGEHFT AKCPFKGTMA PLGEEGAVDV AAGHADTPEG PGGLGAGKSS
     YVPPHLRNGG TAGGERMGGG KFERDDLATL RVTNVSEMAE EQELRDMFER FGRVTRVFLA
     KDRETGLAKG FAFISFQERS DAAKACEKMD GYGFKHLILR VEFAKKAS
 
 
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