ID   EIF3B_NEOFI             Reviewed;         740 AA.
AC   A1D558;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001};
DE            Short=eIF3b {ECO:0000255|HAMAP-Rule:MF_03001};
DE   AltName: Full=Eukaryotic translation initiation factor 3 90 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03001};
DE            Short=eIF3 p90 {ECO:0000255|HAMAP-Rule:MF_03001};
DE   AltName: Full=Translation initiation factor eIF3 p90 subunit homolog;
GN   Name=prt1; ORFNames=NFIA_022620;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_03001}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03001}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000255|HAMAP-
CC       Rule:MF_03001}.
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DR   EMBL; DS027688; EAW23551.1; -; Genomic_DNA.
DR   RefSeq; XP_001265448.1; XM_001265447.1.
DR   AlphaFoldDB; A1D558; -.
DR   SMR; A1D558; -.
DR   STRING; 36630.CADNFIAP00001756; -.
DR   EnsemblFungi; EAW23551; EAW23551; NFIA_022620.
DR   GeneID; 4590650; -.
DR   KEGG; nfi:NFIA_022620; -.
DR   VEuPathDB; FungiDB:NFIA_022620; -.
DR   eggNOG; KOG2314; Eukaryota.
DR   HOGENOM; CLU_011152_4_0_1; -.
DR   OMA; NVADCKI; -.
DR   OrthoDB; 1194797at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
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:0042802; F:identical protein binding; 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:0031369; F:translation initiation factor binding; IEA:InterPro.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   CDD; cd12278; RRM_eIF3B; 1.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   HAMAP; MF_03001; eIF3b; 1.
DR   InterPro; IPR011400; EIF3B.
DR   InterPro; IPR034363; eIF3B_RRM.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR013979; TIF_beta_prop-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR14068; PTHR14068; 1.
DR   Pfam; PF08662; eIF2A; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PIRSF; PIRSF036424; eIF3b; 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; Reference proteome;
KW   Repeat; RNA-binding; WD repeat.
FT   CHAIN           1..740
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   B"
FT                   /id="PRO_0000363822"
FT   DOMAIN          40..126
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT   REPEAT          193..230
FT                   /note="WD 1"
FT   REPEAT          232..289
FT                   /note="WD 2"
FT   REPEAT          302..343
FT                   /note="WD 3"
FT   REPEAT          455..496
FT                   /note="WD 4"
FT   REPEAT          513..556
FT                   /note="WD 5"
FT   REPEAT          571..609
FT                   /note="WD 6"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          695..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..711
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   740 AA;  84400 MW;  B01AA4AFB083E851 CRC64;
     MAPSFDTLSE QDLHEEEEEE IDFSDLKAQY EVKLEEGLDT FVVIDGLPVV PEESRQKLIK
     FLLRKLNTVG HTSEDAVFMP LNDKNMSEGY AFVEFETPEQ AVAAVKQLHG TPLDKKHTLL
     VNKLMDIERY GREGRIDEEY KPPAIEPFKE KEHLRSWLAD PNARDQFALH RGDKVGVFWN
     NKNNPPENVV DRAHWTQLFA QWSPKGTYLA SVHPQGVQLW GGPAFSKQKQ FPHPFVQLIE
     FSPGESYLTT WSARPIQVEE GQSILTYEEE GKNIIVWDIA TGKPLRSFVS HDLTAGPAGD
     AEPKKKVQWP AFKWSADEKY VARMLQHQSI SIYELPRMNL LGKTSVKIDG VMDFEWSPAT
     VTREGVKQYE QLLCFWTPEI GSSPARVAMM SVPSKEIVRT RNLFNVSDVK LHWQSQGSYV
     CVKVDRHSKS KKSMATNLEI FRVREKGVPV EVVDSLKDTV INFAWEPNGN RFVLITTGEA
     VAGAAVAPKT AVSFFAPEKK GGAIGNFKLI RTIEKKNSNA IYWSPKGRFV VVATVHSQTS
     FDMDFWDMDF EGEKPEAEKD FAANLQLMKT IEHYGVTDID WDPTGRYVVS SASVWTHQLE
     NGWNMHTFAG QTLSENPTDK FKQFLWRPRP PTLLSKEEQK QVRKNLREYS KEFDEEDRYA
     VDIANTAVVE KRKRVLNEWV AWIRREKELL AEEKDAYGLP EEADDPKLAK DAAATTQEQG
     ETVVEEIVEE IIEESEEVIG